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1,4-benzenediol + 2 H+ + H2O2
? + 2 H2O
2 KBr + 2 H+ + H2O2
Br2 + 2 H2O + 2 K+
-
-
-
-
?
2 KI + 2 H+ + H2O2
I2 + 2 H2O + 2 K+
-
-
-
-
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
2 Mn2+ + 2 H+ + H2O2
2 Mn3+ + 2 H2O
2 Mn2+ + H2O2 + aflatoxin B1
2 Mn3+ + aflatoxin B1-8,9-dihydrodiol
2 veratryl alcohol + H2O2
2 veratraldehyde + H2O
2,2'-azino-bis(3-ethyl-benzothiazoline-6-sulfonic acid) + H2O2
?
2,2'-azino-bis(3-ethylbenzothiazoline)-6-sulphonate + H2O2
?
-
reaction with and without Mn2+
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H+ + H2O2
oxidized 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H2O
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulphonate) + H2O2
?
2,2'-azino-bis(3-ethylbenzthiazole-6-sulfonic acid) + H2O2
?
2,2'-azino-bis(3-ethylbenzthiazole-6-sulfonic acid) + H2O2 + H+
?
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + Mn2+ + ?
?
2,2'-azinobis(3-ethylbenzthiazoline)-6-sulfonic acid + H2O2
?
-
-
-
-
?
2,2'-azinobis(3-ethylbenzthiazoline)-6-sulfonic acid + H2O2 + Mn2+
?
-
-
-
-
?
2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate + H+ + H2O2
?
-
-
-
-
r
2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate + Mn2+ + H2O2
?
-
-
-
-
r
2,4,6-trichlorophenol + H2O2
?
2,6-dimethoxyphenol + 2 H+ + H2O2
coerulignone + 2 H2O
MnP activity is determined spectrophotometrically by measuring the oxidation of 2,6-dimethoxyphenol to coerulignone (epsilon = 49.6 mM/cm) in 50 mM malonate buffer (pH 4.5) containing 1.0 mM MnSO4, 1.0 mM 2,6-dimethoxyphenol, and 0.2 mM H2O2 at 469 nm, 37°C
-
-
?
2,6-dimethoxyphenol + 2 H+ + H2O2
oxidized 2,6-dimethoxyphenol + 2 H2O
2,6-dimethoxyphenol + H+ + H2O2
?
2,6-dimethoxyphenol + H2O2
?
2,6-dimethoxyphenol + H2O2
coerulignone + H2O
-
-
-
-
r
2,6-dimethoxyphenol + H2O2 + H+
coerulignone + H2O
-
-
-
-
r
2,6-dimethoxyphenol + H2O2 + Mn2+
?
-
-
-
-
?
2,6-dimethoxyphenol + Mn2+ + ?
?
-
-
-
-
?
2,6-dimethoxyphenol + Mn2+ + H2O2
coerulignone + Mn3+ + H2O
2-bromonaphthalene + ?
?
-
oxidation in presence of Tween 80
-
-
?
4-(4-hydroxy-3-methoxy-phenyl)-2-butanone + H2O2
4-[6,2'-dihydroxy-5,3'-dimethoxy-5'-(3-oxo-butyl)-biphenyl]-butan-2-one + 4-(4-hydroxy-3-methoxyphenyl)-3-buten-2-one + 4-[6,2'-dihydroxy-5,3'-dimethoxy-5'-(3-oxo-butyl)-biphenyl]-3-buten-2-one + 3-(3-oxo-butyl)-hexa-2,4-dienedioic acid-1-methyl ester
4-aminophenol + H2O2
?
-
reaction in presence of Mn2+
-
-
?
4-methoxyphenol + H2O2
?
-
reaction in presence of Mn2+
-
-
?
acenaphthene + ?
?
-
oxidation in presence of Tween 80
-
-
?
acenaphthylene + ?
?
-
oxidation in presence of Tween 80
-
-
?
alizarin red S + H2O2
? + 2 H2O
substrate of A172W variants mutant enzymes, poor activity with the wild-type enzyme
-
-
?
alpha-naphthol + H2O2
?
-
reaction in presence of Mn2+
-
-
?
Amplex Red + H2O2
?
-
-
-
-
?
anthracene + ?
?
-
oxidation in presence of Tween 80
-
-
?
benzo[a]anthracene + ?
?
-
oxidation in presence of Tween 80
-
-
?
benzo[a]pyrene + ?
?
-
key enzyme in degradation of benzo[a]pyrene and other polycyclic aromatic hydrocarbons
-
-
?
benzo[a]pyrene + ?
benzo[a]pyrene-1,6-quinone + ?
-
oxidation in presence of Tween 80
-
-
?
benzo[b]fluoroanthrene + ?
?
-
oxidation in presence of Tween 80
-
-
?
benzo[g,h,i]perylene + H2O
?
-
oxidation in presence of Tween 80
-
-
?
brilliant blue R + H2O2
?
dye decolorization
-
-
?
bromocresol green + H2O2
?
-
-
-
-
?
bromocresol purple + H2O2
?
-
-
-
-
?
bromophenol blue + H2O2
?
bromophenol red + H2O2
?
-
-
-
-
?
bromothymol blue + H2O2
?
-
-
-
-
?
catechol + 2 H+ + H2O2
? + 2 H2O
1,2-benzenediol
-
-
?
catechol + H2O2
?
-
reaction in presence of Mn2+
-
-
?
chrysene + ?
?
-
oxidation in presence of Tween 80
-
-
?
Co2+ + H+ + H2O2
Co3+ + H2O
-
reduction of enzyme compound II, oxidation at 2% the rate of Mn2+ oxidation
-
?
Congo red + H2O2
?
dye decolorization
-
-
?
crystal violet + H2O2
? + 2 H2O
substrate of wild-type and A172W variants mutant enzymes
-
-
?
dibenzo[a,h]anthracene + ?
?
-
oxidation in presence of Tween 80
-
-
?
ferrocyanide + H+ + H2O2
ferricyanide + H2O
fluoranthene + ?
?
-
oxidation in presence of Tween 80
-
-
?
fluorene + ?
?
-
oxidation in presence of Tween 80
-
-
?
fluorene + H2O2
9H-fluorene-3,4-diol
denim bleaching PAH degradation, product analysis by HPLC
-
-
?
guaiacol + 2 H+ + H2O2
oxidized guaiacol + 2 H2O
guaiacol + 2 H+ + H2O2
oxidized guaiacol 4'-hydroxy-3',5-dimethoxy[1,1'-biphenyl]-3,4-dione + 2 H2O
Il-MnP1 oxidizes guaiacol and provides a first radical A, which undergoes a variety of non-enzymatic reactions that mainly consists of reactions of resonance stabilization to generate the next radical B. In turn the C-C radical coupling of two B radicals generates a dimeric 3',5-dimethoxy-3,4-dihydro[1,1'-biphenyl]-4,4'-diol, which can be further oxidized by Il-MnP1 to produce 3,3'-dimethoxy[1,1'-bi(cyclohexa-2,5-diene)]-4,4'-dione and 1-[[1(1')Z]-3'-methoxy-4,4'-dioxo[1,1'-bi(cyclohexa-2,5-dien-1-yliden)]-3-yl]-1-methyldioxidan-1-ium. Furthermore, Il-MnP1 oxidizes 3',5-dimethoxy-3,4-dihydro[1,1'-biphenyl]-4,4'-diol to produce a radical C,which is also subject to a variety of non-enzymatic reactions to produce a radical D. Finally, radical D is subjected to further oxidation and C-C coupling for the production of 4'-hydroxy-3',5-dimethoxy[1,1'-biphenyl]-3,4-dione, 1(3),2(5),3(3)-trimethoxy-2(3),2(4)-dihydro[1(1),2(1):2(3),3(1)-terphenyl]-1(4),2(4),3(4)-triol, and [1(1)(2(1))E]-3(4)-hydroxy-1(3),2(5),3(3)-trimethoxy-1(4)H,2(4)H-[1(1),2(1):2(3),3(1)-terphenyl]-1(4),2(4)-dione
-
-
?
guaiacol + H+ + H2O2
?
-
-
-
-
r
guaiacol + H2O2
tetraguaiacol + H2O
-
-
-
-
?
guaiacol + H2O2 + Mn2+
?
-
-
-
-
?
guaiacol + Mn2+ + ?
?
-
-
-
-
?
guaiacol + Mn2+ + H2O2
?
-
-
-
-
r
guaiacylglycerol-beta-guaiacyl ether + H2O2
? + 2 H2O
substrate of A172W variants mutant enzymes
-
-
?
H2O2 + 2,2'-azino-bis(3-ethyl)-benzothiazoline-6-sulfonic acid
H2O + ?
H2O2 + 2,6-dimethoxyphenol
H2O + ?
hydroquinone + H2O2
?
-
reaction in absence or in presence of Mn2+
-
-
?
indeno[1,2,3-c,d]pyrene + ?
?
-
oxidation in presence of Tween 80
-
-
?
indigo carmine + H2O2
? + 2 H2O
substrate of wild-type and A172W variants mutant enzymes
-
-
?
m-cresol purple + H2O2
?
-
-
-
-
?
methyl orange + H2O2
?
dye decolorization
-
-
?
methyl orange + H2O2
? + 2 H2O
substrate of wild-type and A172W variants mutant enzymes
-
-
?
Mn(III)-tartrate + H2O
Mn(II)-tartrate + H+ + H2O
-
-
-
-
r
Mn2+ + 2,6-dimethoxyphenol + H2O2
?
Mn2+ + di(2-methylpent-2-enyl) sulfide + H+
Mn3+ + 2,4-dimethylthiophene + 2-methyl-2-pentenal + H2O
-
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Mn2+ + H2O2 + oxytetracycline
Mn3+ + ?
Mn2+ + H2O2 + tetracycline
Mn3+ + ?
Mn2+ + hydroquinone
?
-
-
-
-
?
Mn2+ + methylhydroquinone
?
-
-
-
-
?
NADH + acetate
NAD+ + ?
-
-
-
-
?
NADH + H2O2 + H+
?
-
-
-
-
r
NADH + lactate
NAD+ + ?
-
-
-
-
?
NADH + malate
NAD+ + ?
-
-
-
-
?
NADH + tartrate
NAD+ + ?
-
-
-
-
?
naphthalene + ?
?
-
oxidation in presence of Tween 80
-
-
?
o-cresol red + H2O2
?
-
-
-
-
?
p-phenylenediamine + H2O2
?
-
in absence or in presence of Mn2+
-
-
?
phenanthrene + 2 H+ + 2 H2O2
phenanthrene-9,10-dione + 2 H2O
denim bleaching PAH degradation, product analysis by HPLC
-
-
?
phenol red
?
-
activity assay
-
-
?
pyrene + ?
?
-
oxidation in presence of Tween 80
-
-
?
pyrogallol + H2O2 + Mn2+
?
-
-
-
-
?
pyrogallol + Mn2+ + ?
?
-
-
-
-
?
Reactive Black 5 + 2 H+ + H2O2
oxidized Reactive Black 5 + 2 H2O
Reactive Black 5 + 2 H+ + H2O2
Reactive Black 5 + 2 H2O
dye decolorization
-
-
?
Reactive Black 5 + H2O2
? + H2O
Reactive Blue 19 + 2 H+ + H2O2
oxidized Reactive Blue 19 + 2 H2O
dye decolorization
-
-
?
Remazol Brilliant Blue R + H2O2
?
remazol brilliant blue R + H2O2
? + 2 H2O
substrate of wild-type and A172W variants mutant enzymes
-
-
?
thymol blue + H2O2
?
-
-
-
-
?
veratric acid + H2O2
? + 2 H2O
-
-
-
-
?
veratryl alcohol + H+ + H2O2
?
veratryl alcohol + H2O2
3,4-dimethoxybenzoic acid + 2 H2O
veratryl alcohol + H2O2
? + 2 H2O
veratryl alcohol + H2O2
? + H2O
veratryl alcohol + H2O2 + H+
?
veratryl alcohol + H2O2 + Mn2+
?
-
veratryl alcohol oxidation requires the simultaneous presence of H2O2 and Mn2+
-
-
?
veratryl alcohol + Mn2+ + ?
?
-
-
-
-
?
veratryl alcohol + Mn2+ + H2O2
?
-
-
-
-
r
veratrylglycerol-beta-guaiacyl ether + H2O2
? + 2 H2O
substrate of A172W variants mutant enzymes
-
-
?
additional information
?
-
1,4-benzenediol + 2 H+ + H2O2
? + 2 H2O
-
-
-
?
1,4-benzenediol + 2 H+ + H2O2
? + 2 H2O
-
-
-
?
1,4-benzenediol + 2 H+ + H2O2
? + 2 H2O
-
-
-
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
-
-
-
-
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
-
-
-
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
-
-
-
-
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
-
-
-
-
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
-
-
-
-
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
-
-
-
-
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
Bacillus velezensis Al-Dhabi 140
-
-
-
-
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
-
-
-
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
-
-
-
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
-
-
-
-
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
-
-
-
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
-
-
-
-
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
-
-
-
-
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
-
-
-
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
-
-
-
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
-
-
-
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
-
-
-
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
-
-
-
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
-
-
-
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
-
-
-
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
-
-
-
-
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
-
-
-
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
-
-
-
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
-
-
-
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
-
-
-
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
-
-
-
-
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
-
-
-
-
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
-
-
-
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
-
-
-
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
-
the kcat value for the reaction is dependent of the Mn(III) chelator molecules malonate, lactate and oxalate, indicating that the enzyme oxidizes chelated Mn(II) to Mn(III)
-
-
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
-
-
-
-
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
-
-
-
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
-
-
-
-
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
-
-
-
-
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
-
-
-
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
-
-
-
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
-
-
-
-
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
-
-
-
-
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
-
-
-
-
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
-
-
-
-
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
-
-
-
-
?
2 Mn(II) + 2 H+ + H2O2
2 Mn(III) + 2 H2O
-
-
-
-
?
2 Mn2+ + 2 H+ + H2O2
2 Mn3+ + 2 H2O
-
-
-
-
?
2 Mn2+ + 2 H+ + H2O2
2 Mn3+ + 2 H2O
-
-
-
-
?
2 Mn2+ + H2O2 + aflatoxin B1
2 Mn3+ + aflatoxin B1-8,9-dihydrodiol
-
maximum elimination of 86.0% of aflatoxin B1 is observed after 48 h in a reaction mixture containing 5 nkat of enzyme, and the addition of Tween 80 enhances elimination. The treatment of aflatoxin B1 by 20 nkat MnP reduces the mutagenic activity by 69.2%. Analysis suggests that aflatoxin B1 is first oxidized to aflatoxin B1-8,9-epoxide and then hydrolyzed to aflatoxin B1-8,9-dihydrodiol
-
-
?
2 Mn2+ + H2O2 + aflatoxin B1
2 Mn3+ + aflatoxin B1-8,9-dihydrodiol
-
maximum elimination of 86.0% of aflatoxin B1 is observed after 48 h in a reaction mixture containing 5 nkat of enzyme, and the addition of Tween 80 enhances elimination. The treatment of aflatoxin B1 by 20 nkat MnP reduces the mutagenic activity by 69.2%. Analysis suggests that aflatoxin B1 is first oxidized to aflatoxin B1-8,9-epoxide and then hydrolyzed to aflatoxin B1-8,9-dihydrodiol
-
-
?
2 veratryl alcohol + H2O2
2 veratraldehyde + H2O
no substrate of wild-type
-
-
?
2 veratryl alcohol + H2O2
2 veratraldehyde + H2O
no substrate of wild-type
-
-
?
2,2'-azino-bis(3-ethyl-benzothiazoline-6-sulfonic acid) + H2O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethyl-benzothiazoline-6-sulfonic acid) + H2O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H+ + H2O2
oxidized 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H2O
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H+ + H2O2
oxidized 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H2O
ABTS
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H+ + H2O2
oxidized 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H2O
ABTS
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H+ + H2O2
oxidized 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H2O
ABTS
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H+ + H2O2
oxidized 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H2O
ABTS
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H+ + H2O2
oxidized 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H2O
ABTS
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H+ + H2O2
oxidized 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H2O
substrate of A172W variants mutant enzymes
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H+ + H2O2
oxidized 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H2O
substrate of A172W variants mutant enzymes
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulphonate) + H2O2
?
-
in absence or presence of Mn2+
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulphonate) + H2O2
?
-
in absence or presence of Mn2+
-
-
?
2,2'-azino-bis(3-ethylbenzthiazole-6-sulfonic acid) + H2O2
?
no substrate of wild-type
-
-
?
2,2'-azino-bis(3-ethylbenzthiazole-6-sulfonic acid) + H2O2
?
no substrate of wild-type
-
-
?
2,2'-azino-bis(3-ethylbenzthiazole-6-sulfonic acid) + H2O2 + H+
?
-
-
-
-
r
2,2'-azino-bis(3-ethylbenzthiazole-6-sulfonic acid) + H2O2 + H+
?
-
-
-
-
r
2,2'-azino-bis(3-ethylbenzthiazole-6-sulfonic acid) + H2O2 + H+
?
-
-
-
-
r
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + Mn2+ + ?
?
-
-
-
-
?
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + Mn2+ + ?
?
-
-
-
-
?
2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) + Mn2+ + ?
?
-
-
-
-
?
2,4,6-trichlorophenol + H2O2
?
-
no oxidation in absence of Mn2+
-
-
?
2,4,6-trichlorophenol + H2O2
?
-
no oxidation in absence of Mn2+
-
-
?
2,6-dimethoxyphenol + 2 H+ + H2O2
oxidized 2,6-dimethoxyphenol + 2 H2O
-
-
-
-
?
2,6-dimethoxyphenol + 2 H+ + H2O2
oxidized 2,6-dimethoxyphenol + 2 H2O
Bacillus velezensis Al-Dhabi 140
-
-
-
-
?
2,6-dimethoxyphenol + 2 H+ + H2O2
oxidized 2,6-dimethoxyphenol + 2 H2O
-
-
-
?
2,6-dimethoxyphenol + 2 H+ + H2O2
oxidized 2,6-dimethoxyphenol + 2 H2O
-
-
-
?
2,6-dimethoxyphenol + 2 H+ + H2O2
oxidized 2,6-dimethoxyphenol + 2 H2O
-
-
-
?
2,6-dimethoxyphenol + 2 H+ + H2O2
oxidized 2,6-dimethoxyphenol + 2 H2O
-
-
-
?
2,6-dimethoxyphenol + 2 H+ + H2O2
oxidized 2,6-dimethoxyphenol + 2 H2O
-
-
-
?
2,6-dimethoxyphenol + 2 H+ + H2O2
oxidized 2,6-dimethoxyphenol + 2 H2O
-
-
-
?
2,6-dimethoxyphenol + 2 H+ + H2O2
oxidized 2,6-dimethoxyphenol + 2 H2O
-
-
-
?
2,6-dimethoxyphenol + 2 H+ + H2O2
oxidized 2,6-dimethoxyphenol + 2 H2O
-
-
-
?
2,6-dimethoxyphenol + 2 H+ + H2O2
oxidized 2,6-dimethoxyphenol + 2 H2O
substrate of A172W variants mutant enzymes, very low activity with the wild-type enzyme
-
-
?
2,6-dimethoxyphenol + 2 H+ + H2O2
oxidized 2,6-dimethoxyphenol + 2 H2O
substrate of A172W variants mutant enzymes, very low activity with the wild-type enzyme
-
-
?
2,6-dimethoxyphenol + H+ + H2O2
?
-
-
-
-
r
2,6-dimethoxyphenol + H+ + H2O2
?
-
-
-
-
r
2,6-dimethoxyphenol + H2O2
?
-
-
-
-
?
2,6-dimethoxyphenol + H2O2
?
-
-
-
-
?
2,6-dimethoxyphenol + H2O2
?
-
-
-
-
?
2,6-dimethoxyphenol + H2O2
?
-
-
-
-
?
2,6-dimethoxyphenol + H2O2
?
-
-
-
-
?
2,6-dimethoxyphenol + H2O2
?
-
-
-
-
?
2,6-dimethoxyphenol + H2O2
?
-
-
-
-
?
2,6-dimethoxyphenol + H2O2
?
-
-
-
-
?
2,6-dimethoxyphenol + H2O2
?
-
-
-
-
?
2,6-dimethoxyphenol + H2O2
?
-
-
-
-
?
2,6-dimethoxyphenol + H2O2
?
-
-
-
-
?
2,6-dimethoxyphenol + H2O2
?
-
-
-
-
?
2,6-dimethoxyphenol + H2O2
?
-
-
-
-
?
2,6-dimethoxyphenol + H2O2
?
-
-
-
-
?
2,6-dimethoxyphenol + H2O2
?
-
-
-
-
?
2,6-dimethoxyphenol + H2O2
?
Inocybe longicystis
-
-
-
-
?
2,6-dimethoxyphenol + H2O2
?
-
-
-
-
?
2,6-dimethoxyphenol + H2O2
?
-
-
-
-
?
2,6-dimethoxyphenol + H2O2
?
-
reaction in absence or in presence of Mn2+
-
-
?
2,6-dimethoxyphenol + H2O2
?
-
the highest relative activity for 2,6-dimethoxyphenol oxidation is observed in the presence of 10 mM malonate
-
-
?
2,6-dimethoxyphenol + H2O2
?
-
the highest relative activity for 2,6-dimethoxyphenol oxidation is observed in the presence of 10 mM malonate
-
-
?
2,6-dimethoxyphenol + H2O2
?
-
reaction in absence or in presence of Mn2+
-
-
?
2,6-dimethoxyphenol + H2O2
?
-
the highest relative activity for 2,6-dimethoxyphenol oxidation is observed in the presence of 10 mM malonate
-
-
?
2,6-dimethoxyphenol + H2O2
?
Lepiota naucina
-
-
-
-
?
2,6-dimethoxyphenol + H2O2
?
-
-
-
-
?
2,6-dimethoxyphenol + H2O2
?
-
-
-
-
?
2,6-dimethoxyphenol + H2O2
?
-
-
-
-
?
2,6-dimethoxyphenol + H2O2
?
-
-
-
-
?
2,6-dimethoxyphenol + H2O2
?
Leptonia lazunila
-
-
-
-
?
2,6-dimethoxyphenol + H2O2
?
Lyophyllum subglobisporium
-
-
-
-
?
2,6-dimethoxyphenol + H2O2
?
Lyophyllum subglobisporium ECN 100606
-
-
-
-
?
2,6-dimethoxyphenol + H2O2
?
-
-
-
-
?
2,6-dimethoxyphenol + H2O2
?
-
reaction in presence of Mn2+
-
-
?
2,6-dimethoxyphenol + H2O2
?
-
-
-
-
?
2,6-dimethoxyphenol + H2O2
?
-
-
-
-
?
2,6-dimethoxyphenol + H2O2
?
-
-
-
-
?
2,6-dimethoxyphenol + H2O2
?
-
-
-
-
?
2,6-dimethoxyphenol + H2O2
?
-
-
-
-
?
2,6-dimethoxyphenol + H2O2
?
-
-
-
-
?
2,6-dimethoxyphenol + H2O2
?
-
-
-
-
?
2,6-dimethoxyphenol + H2O2
?
-
-
-
-
?
2,6-dimethoxyphenol + H2O2
?
-
-
-
-
?
2,6-dimethoxyphenol + H2O2
?
-
-
-
-
?
2,6-dimethoxyphenol + H2O2
?
-
-
-
-
?
2,6-dimethoxyphenol + H2O2
?
-
-
-
-
?
2,6-dimethoxyphenol + H2O2
?
-
-
-
-
?
2,6-dimethoxyphenol + H2O2
?
-
-
-
-
?
2,6-dimethoxyphenol + Mn2+ + H2O2
coerulignone + Mn3+ + H2O
-
-
-
-
r
2,6-dimethoxyphenol + Mn2+ + H2O2
coerulignone + Mn3+ + H2O
-
-
-
-
r
4-(4-hydroxy-3-methoxy-phenyl)-2-butanone + H2O2
4-[6,2'-dihydroxy-5,3'-dimethoxy-5'-(3-oxo-butyl)-biphenyl]-butan-2-one + 4-(4-hydroxy-3-methoxyphenyl)-3-buten-2-one + 4-[6,2'-dihydroxy-5,3'-dimethoxy-5'-(3-oxo-butyl)-biphenyl]-3-buten-2-one + 3-(3-oxo-butyl)-hexa-2,4-dienedioic acid-1-methyl ester
-
3-(3-oxo-butyl)-hexa-2,4-dienedioic acid-1-methyl ester is the dominant product
-
-
?
4-(4-hydroxy-3-methoxy-phenyl)-2-butanone + H2O2
4-[6,2'-dihydroxy-5,3'-dimethoxy-5'-(3-oxo-butyl)-biphenyl]-butan-2-one + 4-(4-hydroxy-3-methoxyphenyl)-3-buten-2-one + 4-[6,2'-dihydroxy-5,3'-dimethoxy-5'-(3-oxo-butyl)-biphenyl]-3-buten-2-one + 3-(3-oxo-butyl)-hexa-2,4-dienedioic acid-1-methyl ester
-
3-(3-oxo-butyl)-hexa-2,4-dienedioic acid-1-methyl ester is the dominant product
-
-
?
4-(4-hydroxy-3-methoxy-phenyl)-2-butanone + H2O2
4-[6,2'-dihydroxy-5,3'-dimethoxy-5'-(3-oxo-butyl)-biphenyl]-butan-2-one + 4-(4-hydroxy-3-methoxyphenyl)-3-buten-2-one + 4-[6,2'-dihydroxy-5,3'-dimethoxy-5'-(3-oxo-butyl)-biphenyl]-3-buten-2-one + 3-(3-oxo-butyl)-hexa-2,4-dienedioic acid-1-methyl ester
-
-
-
-
?
bromophenol blue + H2O2
?
dye decolorization
-
-
?
bromophenol blue + H2O2
?
dye decolorization
-
-
?
bromophenol blue + H2O2
?
-
-
-
-
?
crystal violet + H2O2
?
dye decolorization
-
-
?
crystal violet + H2O2
?
dye decolorization
-
-
?
ferrocyanide + H+ + H2O2
ferricyanide + H2O
-
-
-
-
r
ferrocyanide + H+ + H2O2
ferricyanide + H2O
-
-
-
-
r
gallic acid + H2O2
?
-
-
-
?
gallic acid + H2O2
?
-
-
-
?
gallic acid + H2O2
?
-
-
-
?
gallic acid + H2O2
?
-
-
-
-
?
gallic acid + H2O2
?
-
-
-
?
gallic acid + H2O2
?
-
-
-
?
gallic acid + H2O2
?
-
-
-
?
guaiacol + 2 H+ + H2O2
oxidized guaiacol + 2 H2O
-
-
-
?
guaiacol + 2 H+ + H2O2
oxidized guaiacol + 2 H2O
-
-
-
?
guaiacol + 2 H+ + H2O2
oxidized guaiacol + 2 H2O
-
-
-
?
guaiacol + 2 H+ + H2O2
oxidized guaiacol + 2 H2O
-
-
-
?
guaiacol + ?
?
-
-
-
-
?
guaiacol + H2O2
?
-
-
-
-
?
guaiacol + H2O2
?
-
-
-
-
?
guaiacol + H2O2
?
-
-
-
-
?
guaiacol + H2O2
?
-
-
-
-
?
guaiacol + H2O2
?
-
-
-
-
?
guaiacol + H2O2
?
-
no oxidation in absence of Mn2+
-
-
?
guaiacol + H2O2
?
-
-
-
-
?
guaiacol + H2O2
?
-
no oxidation in absence of Mn2+
-
-
?
guaiacol + H2O2
?
-
-
-
-
?
guaiacol + H2O2
?
-
-
-
-
?
guaiacol + H2O2
?
-
-
-
-
?
guaiacol + H2O2
?
Lyophyllum subglobisporium
-
-
-
-
?
guaiacol + H2O2
?
Lyophyllum subglobisporium ECN 100606
-
-
-
-
?
guaiacol + H2O2
?
-
reaction in presence of Mn2+
-
-
?
guaiacol + H2O2
?
-
-
-
-
?
guaiacol + H2O2
?
-
-
-
-
?
guaiacol + H2O2
?
-
-
-
-
?
guaiacol + H2O2
?
-
-
-
-
?
guaiacol + H2O2
?
-
-
-
-
?
guaiacol + H2O2
?
-
-
-
-
?
guaiacol + H2O2
?
-
-
-
-
?
guaiacol + H2O2
?
-
-
-
-
?
guaiacol + H2O2
?
-
-
-
-
?
guaiacol + H2O2
?
-
-
-
-
?
H2O2 + 2,2'-azino-bis(3-ethyl)-benzothiazoline-6-sulfonic acid
H2O + ?
-
oxidized at a faster rate in presence of Mn(II) than in absence of Mn(II)
-
-
?
H2O2 + 2,2'-azino-bis(3-ethyl)-benzothiazoline-6-sulfonic acid
H2O + ?
-
oxidized at a faster rate in presence of Mn(II) than in absence of Mn(II)
-
-
?
H2O2 + 2,6-dimethoxyphenol
H2O + ?
-
oxidized at a faster rate in presence of Mn(II) than in absence of Mn(II)
-
-
?
H2O2 + 2,6-dimethoxyphenol
H2O + ?
-
oxidized at a faster rate in presence of Mn(II) than in absence of Mn(II)
-
-
?
H2O2 + guaiacol
H2O + ?
-
oxidized at a faster rate in presence of Mn(II) than in absence of Mn(II)
-
-
?
H2O2 + guaiacol
H2O + ?
-
oxidized at a faster rate in presence of Mn(II) than in absence of Mn(II)
-
-
?
H2O2 + Poly R-478
?
-
Mn2+ is required for reaction with Poly R-478 with MnP3
-
-
?
H2O2 + Poly R-478
?
-
MnP2 depolymerizes the polymeric azo dye,Poly R-478, regardless of the presence of Mn2+, to complete its catalytic cycle
-
-
?
Mn2+ + 2,6-dimethoxyphenol + H2O2
?
-
-
-
?
Mn2+ + 2,6-dimethoxyphenol + H2O2
?
-
activity assay
-
-
?
Mn2+ + guaiacol + H2O2
?
activity assay
-
-
?
Mn2+ + guaiacol + H2O2
?
activity assay
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
Mn3+ oxidizes 2,6-dimethoxyphenol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
Mn3+ oxidizes 2,6-dimethoxyphenol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Coriolus pruinosum
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Deuteromycotina sp.
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Deuteromycotina sp.
-
-
product Mn3+ possibly migrates into polymer molecules, such as lignin, nylon and melanin, and initiates nonspecific oxidation, Mn3+ oxidizes 2,6-dimethoxyphenol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Deuteromycotina sp.
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Deuteromycotina sp.
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
specifically oxidizes Mn2+
alpha-hydroxy acids, e.g. lactate, facilitate the dissociation of Mn3+ from enzyme, dicarboxylic acids facilitate the dissociation of Mn3+ from enzyme, Mn3+ oxidizes o-phenylenediamine and p-anisidine, Mn3+ oxidizes o-dianisidine, Mn3+ oxidizes amines, Mn3+ oxidizes a variety of phenols, Mn3+ oxidizes guaiacol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
single Mn2+ binding site in the vicinity of the heme
alpha-hydroxy acids, e.g. lactate, facilitate the dissociation of Mn3+ from enzyme, dicarboxylic acids facilitate the dissociation of Mn3+ from enzyme, Mn3+ oxidizes o-phenylenediamine and p-anisidine, Mn3+ oxidizes o-dianisidine, Mn3+ oxidizes amines, Mn3+ oxidizes a variety of phenols, Mn3+ oxidizes guaiacol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
oxidizes Mn2+ to Mn3+ in the presence of organic acid chelators
alpha-hydroxy acids, e.g. lactate, facilitate the dissociation of Mn3+ from enzyme, dicarboxylic acids facilitate the dissociation of Mn3+ from enzyme, Mn3+ oxidizes o-phenylenediamine and p-anisidine, Mn3+ oxidizes o-dianisidine, Mn3+ oxidizes amines, Mn3+ oxidizes a variety of phenols, Mn3+ oxidizes guaiacol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
the product Mn3+ is involved in the oxidative degradation of lignin in white-rot basidiomycetes, induced by Mn2+
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
Mn3+ oxidizes lignin
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
chelating organic acids facilitate the dissociation of Mn3+ from enzyme, Mn3+ oxidizes phenolic lignin model compounds
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
Mn3+ oxidizes vanillylacetone
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
Mn3+ oxidizes vanillylacetone, chelation of Mn3+ by organic acids stabilizes Mn3+ at a high redox potential
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
involved in lignin-degradation
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Merulius sp.
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
Mn3+ oxidizes vanillylacetone
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
Mn3+ oxidizes lignin
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
involved in lignin-degradation
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
Mn3+ oxidizes curcumin
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
Mn3+ oxidizes phenolic lignin model compounds
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
Mn3+ oxidizes phenolic lignin model compounds
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
Mn3+ oxidizes vanillylacetone
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
Mn3+ oxidizes vanillylacetone
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
Mn3+ oxidizes vanillylacetone
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
Mn3+ oxidizes lignin
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
in presence of Mn2+, H2O2 and glutathione MnP oxidizes by Mn3+ nonphenolic beta-aryl ether lignin model compounds, veratryl alcohol, anisyl alcohol, benzyl alcohol and thiols to thiyl radicals which abstracts a hydrogen from the substrate forming a benzylic radical, mechanism, glutathione can be replaced by dithiothreitol, dithioerythritol or cysteine
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
Mn3+ oxidizes 2,6-dimethoxyphenol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
Mn3+ oxidizes 2,6-dimethoxyphenol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
Mn3+ oxidizes o-dianisidine
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
Mn3+ acts as obligatory redox coupler, oxidizing various phenols, dyes and amines
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
Mn3+ oxidizes amines
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
Mn3+ oxidizes a variety of phenols, Mn3+ oxidizes methoxy benzenes: 1,2,4-tri-, 1,2,3,5-tetra-, 1,2,4,5-tetra-, pentamethoxybenzene, veratryl alcohol is oxidized by thiyl radicals derived from Mn3+ oxidation of glutathione, not directly by Mn3+
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
Mn3+ oxidizes guaiacol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
oxidation and cleavage of a phenolic lignin model dimer and its products, MnP catalyzes C-alpha-C-beta cleavages, C-alpha-oxidation and alkyl-aryl cleavages of phenolic syringyl type beta-1 lignin structures via Mn3+
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
unique binding and oxidation site for Mn2+, single Mn atom is hexacoordinate, with two water ligands and four carboxylate ligands from heme propionate 6 and amino acids Glu-35, Glu-39 and Asp-179
freely diffusible, enzyme-generated Mn(III)-organic-acid complex oxidizes phenolic substrates
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
unique binding and oxidation site for Mn2+, single Mn atom is hexacoordinate, with two water ligands and four carboxylate ligands from heme propionate 6 and amino acids Glu-35, Glu-39 and Asp-179
Mn3+ oxidizes phenolic lignin model compounds
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
unique binding and oxidation site for Mn2+, single Mn atom is hexacoordinate, with two water ligands and four carboxylate ligands from heme propionate 6 and amino acids Glu-35, Glu-39 and Asp-179
Mn3+ oxidizes lignin
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
unique binding and oxidation site for Mn2+, single Mn atom is hexacoordinate, with two water ligands and four carboxylate ligands from heme propionate 6 and amino acids Glu-35, Glu-39 and Asp-179
Mn3+ oxidizes lignin
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
unique binding and oxidation site for Mn2+, single Mn atom is hexacoordinate, with two water ligands and four carboxylate ligands from heme propionate 6 and amino acids Glu-35, Glu-39 and Asp-179
Mn3+ oxidizes lignin, Mn3+ oxidizes a variety of phenols
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
each catalytic cycle step is irreversible
alpha-hydroxy acids, e.g. lactate, facilitate the dissociation of Mn3+ from enzyme, Mn3+ oxidizes phenolic lignin model compounds, Mn3+ oxidizes vanillyl alcohol, Mn3+ oxidizes lignin, Mn3+-organic acid complexes oxidize terminal phenolic substrates in a second-order reaction, Mn3+ oxidizes thiols, Mn3+ acts as obligatory redox coupler, oxidizing various phenols, dyes and amines, the diffusible product is Mn3+, Mn3+ oxidizes amines, chelation of Mn3+ by organic acids stabilizes Mn3+ at a high redox potential
ir
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
specifically oxidizes Mn2+
product Mn3+ is a nonspecific oxidant which in turn oxidizes a variety of organic compounds, Mn3+ oxidizes phenolic lignin model compounds
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
specifically oxidizes Mn2+
Mn3+ complexed to lactate or other alpha-hydroxy acids acts as an obligatory oxidation intermediate in the oxidation of various dyes and lignin model compounds, Mn3+-lactate complex oxidizes all dyes oxidized by the enzyme in presence of Mn2+: NADH, pinacyanol, phenol red and poly B-411, the diffusible product is Mn3+
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
specifically oxidizes Mn2+
Mn3+ oxidizes a variety of phenols
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
specifically oxidizes Mn2+
chelation of Mn3+ by organic acids stabilizes Mn3+ at a high redox potential
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
in presence of H2O2 enzyme oxidizes Mn2+ significantly faster than all other substrates, main function of enzyme is oxidation of Mn2+ to Mn3+
Mn3+ complexed to lactate or other alpha-hydroxy acids acts as an obligatory oxidation intermediate in the oxidation of various dyes and lignin model compounds, Mn3+-lactate complex oxidizes all dyes oxidized by the enzyme in presence of Mn2+: NADH, pinacyanol, phenol red and poly B-411, the diffusible product is Mn3+, chelation of Mn3+ by organic acids stabilizes Mn3+ at a high redox potential
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
role for Arg-177 in promoting efficient Mn2+ binding and oxidation by MnP
freely diffusible, enzyme-generated Mn(III)-organic-acid complex oxidizes phenolic substrates, Mn3+ oxidizes lignin
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
completion of MnP catalytic cycle requires Mn2+
Mn3+ complex oxidizes a variety of organic substrates
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
completion of MnP catalytic cycle requires Mn2+
freely diffusible, enzyme-generated Mn(III)-organic-acid complex oxidizes phenolic substrates
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
completion of MnP catalytic cycle requires Mn2+
Mn3+ oxidizes phenolic lignin model compounds
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
completion of MnP catalytic cycle requires Mn2+
Mn3+ oxidizes phenolic lignin model compounds
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
completion of MnP catalytic cycle requires Mn2+
Mn3+ oxidizes vanillylacetone, Mn3+ oxidizes syringyl alcohol, syringyl aldehyde, syringic acid, syringaldazine, coniferyl alcohol, sinapic acid
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
completion of MnP catalytic cycle requires Mn2+
Mn3+ oxidizes vanillyl alcohol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
completion of MnP catalytic cycle requires Mn2+
Mn3+ oxidizes 2,6-dimethoxyphenol, Mn3+ oxidizes o-dianisidine, the diffusible product is Mn3+, Mn3+ oxidizes a variety of phenols
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
completion of MnP catalytic cycle requires Mn2+
chelation of Mn3+ by organic acids stabilizes Mn3+ at a high redox potential
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
completion of MnP catalytic cycle requires Mn2+
Mn3+ oxidizes guaiacol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
completion of MnP catalytic cycle requires Mn2+
Mn3+ oxidizes guaiacol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
oxidation of Mn2+ to Mn3+ at a redox potential of 1.5 V
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
absolute requirement of Mn2+ for enzymic activity, enzyme requires H2O2 as cosubstrate
freely diffusible, enzyme-generated Mn(III)-organic-acid complex oxidizes phenolic substrates, Mn3+ oxidizes phenolic lignin model compounds
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
absolute requirement of Mn2+ for enzymic activity, enzyme requires H2O2 as cosubstrate
Mn3+ oxidizes syringic acid, 4-hydroxy-3-methoxycinnamic acid, isoeugenol, ascorbate, Mn3+ oxidizes vanillyl alcohol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
absolute requirement of Mn2+ for enzymic activity, enzyme requires H2O2 as cosubstrate
Mn3+ oxidizes vanillyl alcohol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
absolute requirement of Mn2+ for enzymic activity, enzyme requires H2O2 as cosubstrate
Mn3+ oxidizes o-dianisidine, Mn3+ acts as obligatory redox coupler, oxidizing various phenols, dyes and amines, Mn3+ oxidizes p-cresol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
absolute requirement of Mn2+ for enzymic activity, enzyme requires H2O2 as cosubstrate
chelation of Mn3+ by organic acids stabilizes Mn3+ at a high redox potential
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
absolute requirement of Mn2+ for enzymic activity, enzyme requires H2O2 as cosubstrate
Mn3+ oxidizes guaiacol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
free divalent Mn is the substrate, not Mn2+-complexes
alpha-hydroxy acids, e.g. lactate, facilitate the dissociation of Mn3+ from enzyme, Mn3+ oxidizes phenolic lignin model compounds, Mn3+ oxidizes vanillyl alcohol, Mn3+ oxidizes lignin, Mn3+-organic acid complexes oxidize terminal phenolic substrates in a second-order reaction, Mn3+ oxidizes thiols, Mn3+ acts as obligatory redox coupler, oxidizing various phenols, dyes and amines, the diffusible product is Mn3+, Mn3+ oxidizes amines, chelation of Mn3+ by organic acids stabilizes Mn3+ at a high redox potential
ir
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Mn2+ is an obligatory substrate for MnP compound II, whereas compound I formation occurs with Mn2+, p-cresol and organic peroxides, e.g. peracetic acid, m-chloroperoxybenzoic acid and p-nitroperoxybenzoic acid
alpha-hydroxy acids, e.g. lactate, facilitate the dissociation of Mn3+ from enzyme, Mn3+ oxidizes phenolic lignin model compounds, Mn3+ acts as obligatory redox coupler, oxidizing various phenols, dyes and amines, Mn3+ oxidizes p-cresol, Mn3+ oxidizes amines, Mn3+ oxidizes a variety of phenols, chelation of Mn3+ by organic acids stabilizes Mn3+ at a high redox potential
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Mn2+ binds to a common site close to the delta-meso-carbon without blocking the approach of small molecules to the heme edge
Mn3+ oxidizes guaiacol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
oxidizes Mn2+ to Mn3+ in the presence of organic acid chelators
Mn3+-chelate-complexes catalyze decarboxylation and demeth(ox)ylation of aromatic substrates, Mn3+ oxidizes guaiacol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
role of manganese in organic compound oxidations by MnP is to serve as a one-electron transfer mediator
Mn3+ complex oxidizes a variety of organic substrates, Mn3+ oxidizes phenolic lignin model compounds, Mn3+-chelate-complexes catalyze decarboxylation and demeth(ox)ylation of aromatic substrates, Mn3+ oxidizes guaiacol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
little or no enzyme activity in absence of Mn2+
Mn3+ oxidizes vanillylacetone, Mn3+ oxidizes phenol red, Mn3+ oxidizes a variety of phenols, Mn3+ oxidizes guaiacol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
oxidizes Mn2+ in presence of H2O2 to a higher oxidation state, enzyme activity is dependent on Mn2+ acting as electron carriers
Mn3+ complex oxidizes a variety of organic substrates, Mn3+ oxidizes phenolic lignin model compounds, Mn3+ oxidizes vanillylacetone, Mn3+ oxidizes syringyl alcohol, syringyl aldehyde, syringic acid, syringaldazine, coniferyl alcohol, sinapic acid, Mn3+ oxidizes 2,6-dimethoxyphenol, Mn3+ oxidizes o-dianisidine, the diffusible product is Mn3+, Mn3+ oxidizes a variety of phenols, Mn3+ oxidizes guaiacol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
MnP isoenzymes serve different functions in lignin biodegradation, each may have a preferred substrate
the product Mn3+ is involved in the oxidative degradation of lignin in white-rot basidiomycetes, induced by Mn2+
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
involved in lignin-degradation
Mn3+ functions not as a primary oxidant of nonphenolic units in lignin, i.e. it plays another role in lignin-degradation than lignin peroxidase
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
involved in lignin-degradation
the product Mn3+ is involved in the oxidative degradation of lignin in white-rot basidiomycetes, induced by veratryl alcohol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
initial depolymerization of the lignin polymer
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Mn2+ is a component of woody plant tissues
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
important component of lignin degradation system
Mn3+ is stabilized by chelating agents, malonate is the most effective physiological chelator excreted by the fungus
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
important component of lignin degradation system
freely diffusible, enzyme-generated Mn(III)-organic-acid complex is an catalyst for the oxidative depolymerization of lignin in wood
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
important component of lignin degradation system
Mn3+ is produced under lignolytic conditions
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
involved in lignin-degradation, the mechanism enables the fungus to oxidize structures within woods which are inaccessible to enzymes
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
acts together with lignin peroxidase in lignin-degradation of white rot fungi
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
acts together with lignin peroxidase in lignin-degradation of white rot fungi
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
acts together with lignin peroxidase in lignin-degradation of white rot fungi
Mn3+ functions not as a primary oxidant of nonphenolic units in lignin, i.e. it plays another role in lignin-degradation than lignin peroxidase
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
in absence of H2O2 it may play a role in fungal peroxide production under ligninolytic conditions
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
little or no enzyme activity in absence of Mn2+
Mn3+ oxidizes vanillylacetone, Mn3+ oxidizes phenol red
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
Mn3+ oxidizes phenolic lignin model compounds, Mn3+ oxidizes vanillylacetone
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
Mn3+ oxidizes curcumin
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
Mn3+ oxidizes 2,6-dimethoxyphenol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
each catalytic cycle step is irreversible
alpha-hydroxy acids, e.g. lactate, facilitate the dissociation of Mn3+ from enzyme, Mn3+ oxidizes phenolic lignin model compounds
ir
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
completion of MnP catalytic cycle requires Mn2+
freely diffusible, enzyme-generated Mn(III)-organic-acid complex oxidizes phenolic substrates, Mn3+ oxidizes phenolic lignin model compounds, Mn3+ oxidizes vanillyl alcohol, chelation of Mn3+ by organic acids stabilizes Mn3+ at a high redox potential
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
completion of MnP catalytic cycle requires Mn2+
Mn3+ oxidizes guaiacol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
Mn2+ binds to a common site close to the delta-meso-carbon without blocking the approach of small molecules to the heme edge
Mn3+ oxidizes guaiacol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
Mn3+ oxidizes phenolic lignin model compounds, in presence of Mn2+, H2O2 and glutathione MnP oxidizes by Mn3+ nonphenolic beta-aryl ether lignin model compounds, veratryl alcohol, anisyl alcohol, benzyl alcohol and thiols to thiyl radicals which abstracts a hydrogen from the substrate forming a benzylic radical, mechanism, glutathione can be replaced by dithiothreitol, dithioerythritol or cysteine, Mn3+ acts as obligatory redox coupler, oxidizing various phenols, dyes and amines
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
important component of lignin degradation system
Mn3+ is produced under lignolytic conditions
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
unique binding and oxidation site for Mn2+, single Mn atom is hexacoordinate, with two water ligands and four carboxylate ligands from heme propionate 6 and amino acids Glu-35, Glu-39 and Asp-179
freely diffusible, enzyme-generated Mn(III)-organic-acid complex oxidizes phenolic substrates
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
unique binding and oxidation site for Mn2+, single Mn atom is hexacoordinate, with two water ligands and four carboxylate ligands from heme propionate 6 and amino acids Glu-35, Glu-39 and Asp-179
Mn3+ oxidizes lignin
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
unique binding and oxidation site for Mn2+, single Mn atom is hexacoordinate, with two water ligands and four carboxylate ligands from heme propionate 6 and amino acids Glu-35, Glu-39 and Asp-179
Mn3+ oxidizes phenolic lignin model compounds, Mn3+ oxidizes lignin, Mn3+ oxidizes a variety of phenols
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
oxidizes Mn2+ to Mn3+ in the presence of organic acid chelators
Mn3+-chelate-complexes catalyze decarboxylation and demeth(ox)ylation of aromatic substrates, Mn3+ oxidizes guaiacol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
role of manganese in organic compound oxidations by MnP is to serve as a one-electron transfer mediator
Mn3+ complex oxidizes a variety of organic substrates, Mn3+ oxidizes phenolic lignin model compounds, Mn3+-chelate-complexes catalyze decarboxylation and demeth(ox)ylation of aromatic substrates
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
Mn3+ oxidizes 2,6-dimethoxyphenol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
Phellinus trivialis
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
the product Mn3+ is involved in the oxidative degradation of lignin in white-rot basidiomycetes, induced by Mn2+
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
Mn3+ oxidizes lignin
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
completion of MnP catalytic cycle requires Mn2+
Mn3+ oxidizes vanillylacetone, Mn3+ oxidizes phenol red, Mn3+ oxidizes a variety of phenols, Mn3+ oxidizes several methoxylated and hydroxylated phenolic compounds
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
involved in lignin-degradation
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
Mn3+ oxidizes vanillylideneacetone, Mn3+ oxidizes 2,6-dimethoxyphenol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
Mn3+ oxidizes 2,6-dimethoxyphenol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
Mn3+ oxidizes phenol red, Mn3+ oxidizes a variety of phenols
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
preferential degradation of lignin in wheat straw
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
Mn3+ oxidizes 2,6-dimethoxyphenol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
Mn3+ oxidizes 2,6-dimethoxyphenol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
Mn3+ oxidizes 2,6-dimethoxyphenol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
Mn3+ oxidizes syringaldazine, Mn3+ oxidizes guaiacol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
oxidizes Mn2+ as the best substrate
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
preferential degradation of lignin in wheat straw
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
oxidizes Mn2+ as the best substrate
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
Mn3+ oxidizes 2,6-dimethoxyphenol
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
involved in lignin-degradation
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
important component of lignin degradation system
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
-
-
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
-
Mn3+ oxidizes lignin
?
Mn2+ + H+ + H2O2
Mn3+ + H2O
-
involved in lignin-degradation
-
-
?
Mn2+ + H2O2
Mn3+ + H2O
-
-
-
-
?
Mn2+ + H2O2
Mn3+ + H2O
-
-
-
-
?
Mn2+ + H2O2
Mn3+ + H2O
-
-
-
?
Mn2+ + H2O2
Mn3+ + H2O
-
-
-
-
?
Mn2+ + H2O2
Mn3+ + H2O
-
-
-
-
?
Mn2+ + H2O2
Mn3+ + H2O
-
-
-
-
?
Mn2+ + H2O2 + oxytetracycline
Mn3+ + ?
-
-
-
-
?
Mn2+ + H2O2 + oxytetracycline
Mn3+ + ?
-
-
-
-
?
Mn2+ + H2O2 + tetracycline
Mn3+ + ?
-
-
-
-
?
Mn2+ + H2O2 + tetracycline
Mn3+ + ?
-
-
-
-
?
o-dianisidine + H2O2
?
-
in absence or in presence of of Mn2+
-
-
?
o-dianisidine + H2O2
?
-
in absence or in presence of of Mn2+
-
-
?
phenol red + H2O2
?
-
-
-
-
?
phenol red + H2O2
?
-
-
-
-
?
phenol red + H2O2
?
-
-
-
-
?
phenol red + H2O2
?
-
-
-
-
?
phenol red + H2O2
?
-
-
-
-
?
phenol red + H2O2
?
-
-
-
-
?
phenol red + H2O2
?
-
-
-
-
?
phenol red + H2O2
?
-
-
-
-
?
phenol red + H2O2
?
-
-
-
-
?
phenol red + H2O2
?
-
-
-
-
?
phenol red + H2O2
?
-
-
-
-
?
phenol red + H2O2
?
-
-
-
-
?
phenol red + H2O2
?
-
-
-
-
?
phenol red + H2O2
?
-
-
-
-
?
phenol red + H2O2
?
-
-
-
-
?
phenol red + H2O2
?
-
-
-
-
?
phenol red + H2O2
?
-
-
-
-
?
phenol red + H2O2
?
-
-
-
-
?
phenol red + H2O2
?
-
-
-
-
?
phenol red + H2O2
?
-
-
-
-
?
phenol red + H2O2
?
-
-
-
-
?
phenol red + H2O2
?
-
-
-
-
?
phenol red + H2O2
?
Trametes zonata
-
-
-
-
?
phenol red + H2O2
?
Trametes zonata 540
-
-
-
-
?
pyrogallol + H2O2
?
-
-
-
-
?
pyrogallol + H2O2
?
-
-
-
-
?
pyrogallol + H2O2
?
-
-
-
-
?
Reactive Black 5 + 2 H+ + H2O2
oxidized Reactive Black 5 + 2 H2O
dye decolorization, substrate of A172W variants mutant enzymes
-
-
?
Reactive Black 5 + 2 H+ + H2O2
oxidized Reactive Black 5 + 2 H2O
dye decolorization, substrate of A172W variants mutant enzymes
-
-
?
Reactive Black 5 + H2O2
? + H2O
no substrate of wild-type
-
-
?
Reactive Black 5 + H2O2
? + H2O
no substrate of wild-type
-
-
?
Remazol Brilliant Blue R + H2O2
?
dye decolorization
-
-
?
Remazol Brilliant Blue R + H2O2
?
dye decolorization
-
-
?
vanillylacetone + H2O2
?
-
reaction in presence of Mn2+
-
-
?
vanillylacetone + H2O2
?
-
-
-
-
?
veratryl alcohol + H+ + H2O2
?
-
-
-
-
r
veratryl alcohol + H+ + H2O2
?
-
-
-
-
r
veratryl alcohol + H2O2
3,4-dimethoxybenzoic acid + 2 H2O
-
-
-
?
veratryl alcohol + H2O2
3,4-dimethoxybenzoic acid + 2 H2O
substrate of A172W variants mutant enzymes
-
-
?
veratryl alcohol + H2O2
? + 2 H2O
-
-
-
?
veratryl alcohol + H2O2
? + 2 H2O
-
-
-
?
veratryl alcohol + H2O2
? + H2O
-
-
-
-
?
veratryl alcohol + H2O2
? + H2O
-
reaction in absence of Mn2+
-
-
?
veratryl alcohol + H2O2 + H+
?
-
-
-
-
r
veratryl alcohol + H2O2 + H+
?
-
-
-
-
r
veratryl alcohol + H2O2 + H+
?
-
-
-
-
r
additional information
?
-
-
-
-
-
?
additional information
?
-
-
in absence of Mn2+ the enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
-
-
?
additional information
?
-
-
in absence of Mn2+ the enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
-
-
?
additional information
?
-
-
the enzyme is essential for lignin degradation
-
-
?
additional information
?
-
-
Mn2+-dependent and Mn2+-independent peroxidase activities, substrates: 2,6-dimethoxyphenol, 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate, guaiacol and veratryl alcohol
-
-
?
additional information
?
-
-
enzyme oxidizes 4-aminophenol and hydroquinone
-
-
?
additional information
?
-
-
enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
-
-
?
additional information
?
-
-
no activity with veratryl alcohol
-
-
?
additional information
?
-
-
no activity with veratryl alcohol
-
-
?
additional information
?
-
-
MnP oxidizes phenolic and nonphenolic aromatic compounds, e.g. phenol red and veratryl alcohol
-
-
?
additional information
?
-
-
enzyme oxidizes 2,6-dimethoxyphenol
-
-
?
additional information
?
-
-
in absence of Mn2+ enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate, o-phenylenediamine and phenol red, the former two are stimulated, the latter is inhibited by Mn2+, guaiacol and pyrocatechol are oxidized only in presence of Mn2+
-
-
?
additional information
?
-
-
the enzyme is essential for lignin degradation
-
-
?
additional information
?
-
-
catalyzes the oxidation of Mn(II) to Mn(III), which in turn can oxidize phenolic substrates
-
-
?
additional information
?
-
-
no activity with veratryl alcohol
-
-
?
additional information
?
-
-
in absence of Mn2+ enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate, o-phenylenediamine and phenol red, the former two are stimulated, the latter is inhibited by Mn2+, guaiacol and pyrocatechol are oxidized only in presence of Mn2+
-
-
?
additional information
?
-
-
Mn2+-dependent and Mn2+-independent peroxidase activities, substrates: 2,6-dimethoxyphenol, 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate, guaiacol and veratryl alcohol
-
-
?
additional information
?
-
-
enzyme oxidizes 4-aminophenol and hydroquinone
-
-
?
additional information
?
-
-
enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
-
-
?
additional information
?
-
-
enzyme oxidizes 2,6-dimethoxyphenol
-
-
?
additional information
?
-
-
Mn-mediated and Mn-independent activity on phenolic and non-phenolic aromatic substrates
-
-
?
additional information
?
-
-
Mn2+-independent peroxidase activity on 2,6-dimethoxyphenol and veratryl alcohol
-
-
?
additional information
?
-
-
MnP oxidizes phenolic and nonphenolic aromatic compounds, e.g. phenol red and veratryl alcohol
-
-
?
additional information
?
-
-
Mn-mediated and Mn-independent activity on phenolic and non-phenolic aromatic substrates
-
-
?
additional information
?
-
-
Mn2+-independent peroxidase activity on 2,6-dimethoxyphenol and veratryl alcohol
-
-
?
additional information
?
-
-
the enzyme is essential for lignin degradation
-
-
?
additional information
?
-
evaluation of the dye decolorization ability of the purified enzyme, MnP-BBP6, the enzyme is used to decolorize different types of synthetic dyes including RBBR, Congo red (CR), brilliant blue R (BBR), methyl orange (MO), bromophenol blue (BPB), and crystal violet (CV). Denim bleaching by the purified MnP-BBP6
-
-
-
additional information
?
-
isozyme MnP3 shows a broad substrate specificity
-
-
-
additional information
?
-
isozyme MnP3 shows a broad substrate specificity
-
-
-
additional information
?
-
evaluation of the dye decolorization ability of the purified enzyme, MnP-BBP6, the enzyme is used to decolorize different types of synthetic dyes including RBBR, Congo red (CR), brilliant blue R (BBR), methyl orange (MO), bromophenol blue (BPB), and crystal violet (CV). Denim bleaching by the purified MnP-BBP6
-
-
-
additional information
?
-
-
MnP oxidizes humic substances
-
-
?
additional information
?
-
Deuteromycotina sp.
-
-
-
-
?
additional information
?
-
Deuteromycotina sp.
-
structural properties
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
no oxidation of Co2+
-
-
?
additional information
?
-
-
enzyme oxidizes a variety of organic compounds in presence, but not in absence of Mn2+
-
-
?
additional information
?
-
-
catalytic cycle with oxidized intermediates MnP compound I and II
-
-
?
additional information
?
-
-
no activity with veratryl alcohol
-
-
?
additional information
?
-
-
no oxidation of Fe2+, Cu2+, Zn2+
-
-
?
additional information
?
-
-
no other metal can substitute Mn2+
-
-
?
additional information
?
-
-
enzyme oxidizes 2,6-dimethoxyphenol
-
-
?
additional information
?
-
-
no oxidation of Ni2+
-
-
?
additional information
?
-
-
dye decolorization
-
-
?
additional information
?
-
-
no oxidation of Co2+
-
-
?
additional information
?
-
-
enzyme oxidizes a variety of organic compounds in presence, but not in absence of Mn2+
-
-
?
additional information
?
-
-
catalytic cycle with oxidized intermediates MnP compound I and II
-
-
?
additional information
?
-
-
no activity with veratryl alcohol
-
-
?
additional information
?
-
-
no oxidation of Fe2+, Cu2+, Zn2+
-
-
?
additional information
?
-
-
the enzyme is essential for lignin degradation
-
-
?
additional information
?
-
-
MnP oxidizes polycyclic aromatic hydrocarbons
-
-
?
additional information
?
-
-
MnP oxidizes humic substances
-
-
?
additional information
?
-
-
MnP oxidizes chlorophenols and arsenic-containing warefare agents
-
-
?
additional information
?
-
-
MnP oxidizes nitroaromatic compounds
-
-
?
additional information
?
-
no activity with veratryl alcohol (VA)
-
-
-
additional information
?
-
-
no activity with veratryl alcohol (VA)
-
-
-
additional information
?
-
the oxidation of guaiacol mainly belongs to a series of polymeric reactions of radicals initiated by isozyme Il-MnP1,whether they are in the presence and absence of Mn2+ at either pH 4.0 or pH 7.4. Both wild-type Il-MnP1 and the variants exhibit negligible activity on veratryl alcohol oxidation in the absence of Mn2+
-
-
-
additional information
?
-
-
the oxidation of guaiacol mainly belongs to a series of polymeric reactions of radicals initiated by isozyme Il-MnP1,whether they are in the presence and absence of Mn2+ at either pH 4.0 or pH 7.4. Both wild-type Il-MnP1 and the variants exhibit negligible activity on veratryl alcohol oxidation in the absence of Mn2+
-
-
-
additional information
?
-
the oxidation of guaiacol mainly belongs to a series of polymeric reactions of radicals initiated by isozyme Il-MnP1,whether they are in the presence and absence of Mn2+ at either pH 4.0 or pH 7.4. Both wild-type Il-MnP1 and the variants exhibit negligible activity on veratryl alcohol oxidation in the absence of Mn2+
-
-
-
additional information
?
-
no activity with veratryl alcohol (VA)
-
-
-
additional information
?
-
the oxidation of guaiacol mainly belongs to a series of polymeric reactions of radicals initiated by isozyme Il-MnP1,whether they are in the presence and absence of Mn2+ at either pH 4.0 or pH 7.4. Both wild-type Il-MnP1 and the variants exhibit negligible activity on veratryl alcohol oxidation in the absence of Mn2+
-
-
-
additional information
?
-
-
enzyme oxidizes non-phenolic lignin-related compounds, including veratryl alcohol
-
-
?
additional information
?
-
-
enzyme is able to oxidatively depolymerize both dimeric lignin-model compounds and milled spruce-wood lignin
-
-
?
additional information
?
-
-
protein complex containing MnP, laccase and beta-glucosidase
-
-
?
additional information
?
-
-
enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
-
-
?
additional information
?
-
-
enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
-
-
?
additional information
?
-
-
no activity with veratryl alcohol
-
-
?
additional information
?
-
-
enzyme oxidizes 3,3,5,5-tetramethylbenzidine
-
-
?
additional information
?
-
-
enzyme oxidizes veratryl alcohol and o-tolidine
-
-
?
additional information
?
-
-
MnP oxidizes phenolic and nonphenolic aromatic compounds, e.g. phenol red and veratryl alcohol
-
-
?
additional information
?
-
-
in presence of H2O2 and Mn2+ the enzyme oxidizes lignin and lignin-model compounds
-
-
?
additional information
?
-
-
MnP oxidizes phenolic and nonphenolic aromatic compounds, e.g. phenol red and veratryl alcohol
-
-
?
additional information
?
-
the phenolic and non-phenolic lignin dimers guaiacylglycerol-beta-guaiacyl ether (Ge) and veratrylglycerol-beta-guaiacyl ether (Ve) are tested as substrates at pH 3.0-5.0. The phenolic lignin dimer Ge is barely oxidized by the wild-type enzyme (2% conversion), but after introduction of the A172W mutation around 33% can be degraded at pH 3.0 and pH 4.0, and around 15% at pH 5.0. All additional mutations (except for A269R) further increased the activity towards guaiacylglycerol-beta-guaiacyl ether at pH 3.0 and pH 4.0, with the A172W K168V mutant showing the highest conversion of up to 56% at pH 3.0. The more recalcitrant non-phenolic lignin dimer veratrylglycerol-beta-guaiacyl ether is oxidized only by the mutants, but not by the wild-type enzyme. The activity of the mutants is more similar to the substrate specificity of EC 1.11.1.14. The wild-type enzyme and the mutants are active with dyes: crystal violet, methyl orange, alizarin red S, indigo carmine, and remazol brilliant blue R, except for the poor activity of the wild-type enzyme with alizarin red S, overview. The mutants show similar tendencies, decolorization at pH 3.0 is stronger than that with wild-type enzyme. The wild-type MrMnP1 is able to convert ABTS, 2,6-DMP, and Mn2+, but not high-redox-potential substrates, such as Reactive Black 5 or veratryl alcohol
-
-
-
additional information
?
-
-
the phenolic and non-phenolic lignin dimers guaiacylglycerol-beta-guaiacyl ether (Ge) and veratrylglycerol-beta-guaiacyl ether (Ve) are tested as substrates at pH 3.0-5.0. The phenolic lignin dimer Ge is barely oxidized by the wild-type enzyme (2% conversion), but after introduction of the A172W mutation around 33% can be degraded at pH 3.0 and pH 4.0, and around 15% at pH 5.0. All additional mutations (except for A269R) further increased the activity towards guaiacylglycerol-beta-guaiacyl ether at pH 3.0 and pH 4.0, with the A172W K168V mutant showing the highest conversion of up to 56% at pH 3.0. The more recalcitrant non-phenolic lignin dimer veratrylglycerol-beta-guaiacyl ether is oxidized only by the mutants, but not by the wild-type enzyme. The activity of the mutants is more similar to the substrate specificity of EC 1.11.1.14. The wild-type enzyme and the mutants are active with dyes: crystal violet, methyl orange, alizarin red S, indigo carmine, and remazol brilliant blue R, except for the poor activity of the wild-type enzyme with alizarin red S, overview. The mutants show similar tendencies, decolorization at pH 3.0 is stronger than that with wild-type enzyme. The wild-type MrMnP1 is able to convert ABTS, 2,6-DMP, and Mn2+, but not high-redox-potential substrates, such as Reactive Black 5 or veratryl alcohol
-
-
-
additional information
?
-
the phenolic and non-phenolic lignin dimers guaiacylglycerol-beta-guaiacyl ether (Ge) and veratrylglycerol-beta-guaiacyl ether (Ve) are tested as substrates at pH 3.0-5.0. The phenolic lignin dimer Ge is barely oxidized by the wild-type enzyme (2% conversion), but after introduction of the A172W mutation around 33% can be degraded at pH 3.0 and pH 4.0, and around 15% at pH 5.0. All additional mutations (except for A269R) further increased the activity towards guaiacylglycerol-beta-guaiacyl ether at pH 3.0 and pH 4.0, with the A172W K168V mutant showing the highest conversion of up to 56% at pH 3.0. The more recalcitrant non-phenolic lignin dimer veratrylglycerol-beta-guaiacyl ether is oxidized only by the mutants, but not by the wild-type enzyme. The activity of the mutants is more similar to the substrate specificity of EC 1.11.1.14. The wild-type enzyme and the mutants are active with dyes: crystal violet, methyl orange, alizarin red S, indigo carmine, and remazol brilliant blue R, except for the poor activity of the wild-type enzyme with alizarin red S, overview. The mutants show similar tendencies, decolorization at pH 3.0 is stronger than that with wild-type enzyme. The wild-type MrMnP1 is able to convert ABTS, 2,6-DMP, and Mn2+, but not high-redox-potential substrates, such as Reactive Black 5 or veratryl alcohol
-
-
-
additional information
?
-
-
no activity with veratryl alcohol
-
-
?
additional information
?
-
-
MnP oxidizes polycyclic aromatic hydrocarbons
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
no oxidation of Co2+
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-
?
additional information
?
-
-
MnP oxidizes polycyclic aromatic hydrocarbons
-
-
?
additional information
?
-
-
catalytic cycle of enzyme, oxidation states: native enzyme via compound I via compound II to native enzyme, Mn2+ and phenols reduce MnP compound I to compound II, but only Mn2+ is a substrate for MnP compound II, Mn(II)/Mn(III) redox couple enables enzyme to rapidly oxidize terminal phenolic substrates
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-
?
additional information
?
-
-
catalytic cycle of enzyme, oxidation states: native enzyme via compound I via compound II to native enzyme, Mn2+ and phenols reduce MnP compound I to compound II, but only Mn2+ is a substrate for MnP compound II, Mn(II)/Mn(III) redox couple enables enzyme to rapidly oxidize terminal phenolic substrates
-
-
?
additional information
?
-
-
Mn2+-independent peroxidase activity on 2,6-dimethoxyphenol and veratryl alcohol
-
-
?
additional information
?
-
-
Mn2+-independent peroxidase activity on 2,6-dimethoxyphenol and veratryl alcohol
-
-
?
additional information
?
-
-
structural properties
-
-
?
additional information
?
-
-
structural properties
-
-
?
additional information
?
-
-
structural properties
-
-
?
additional information
?
-
-
structural properties
-
-
?
additional information
?
-
structural properties
-
-
?
additional information
?
-
-
structural properties
-
-
?
additional information
?
-
-
in absence of H2O2 the enzyme shows Mn-dependent oxidase activity against glutathione, dithiothreitol and dihydroxymaleic acid, forming H2O2 at the expense of oxygen
-
-
?
additional information
?
-
-
in absence of H2O2 the enzyme shows Mn-dependent oxidase activity against glutathione, dithiothreitol and dihydroxymaleic acid, forming H2O2 at the expense of oxygen
-
-
?
additional information
?
-
-
primary reaction product of peroxidation with H2O2 is enzyme compound I, formation of compound II from I follows second-order kinetic
-
-
?
additional information
?
-
-
enzyme oxidizes a variety of organic compounds in presence, but not in absence of Mn2+
-
-
?
additional information
?
-
-
enzyme oxidizes a variety of organic compounds in presence, but not in absence of Mn2+
-
-
?
additional information
?
-
-
enzyme oxidizes a variety of organic compounds in presence, but not in absence of Mn2+
-
-
?
additional information
?
-
-
in absence of Mn2+ the enzyme oxidizes pinacyanol as most easily oxidized dye at 1.7% of the rate of the Mn2+ oxidation
-
-
?
additional information
?
-
-
enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
-
-
?
additional information
?
-
-
enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
-
-
?
additional information
?
-
-
enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
-
-
?
additional information
?
-
-
enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
-
-
?
additional information
?
-
enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
-
-
?
additional information
?
-
-
enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
-
-
?
additional information
?
-
-
in absence of H2O2 the enzyme oxidizes Mn-dependently NADH to NAD+, generating H2O2 for oxidizing other substrates
-
-
?
additional information
?
-
-
in absence of H2O2 the enzyme oxidizes Mn-dependently NADH to NAD+, generating H2O2 for oxidizing other substrates
-
-
?
additional information
?
-
-
in presence of H2O2 and Mn2+ the enzyme oxidizes a variety of phenolic compounds, especially vinyl and syringyl side-chain substituted substrates
-
-
?
additional information
?
-
-
in presence of H2O2 and Mn2+ the enzyme oxidizes a variety of phenolic compounds, especially vinyl and syringyl side-chain substituted substrates
-
-
?
additional information
?
-
-
catalytic cycle with oxidized intermediates MnP compound I and II
-
-
?
additional information
?
-
-
catalytic cycle with oxidized intermediates MnP compound I and II
-
-
?
additional information
?
-
-
catalytic cycle with oxidized intermediates MnP compound I and II
-
-
?
additional information
?
-
-
catalytic cycle with oxidized intermediates MnP compound I and II
-
-
?
additional information
?
-
-
catalytic cycle with oxidized intermediates MnP compound I and II
-
-
?
additional information
?
-
-
catalytic cycle with oxidized intermediates MnP compound I and II
-
-
?
additional information
?
-
-
no activity with veratryl alcohol
-
-
?
additional information
?
-
-
catalytic cycle: MnP is oxidized by H2O2 to compound I, Mn2+, ferrocyanide or phenols reduce compound I to compound II, which is reduced to the ferric state by Mn2+ or ferrocyanide, but not by phenols, Mn2+ completes the cycle, substrates are oxidized via delta-meso heme edge of the enzyme, model of the active site
-
-
?
additional information
?
-
-
enzyme oxidizes ferrocyanide
-
-
?
additional information
?
-
-
enzyme oxidizes ferrocyanide
-
-
?
additional information
?
-
-
enzyme oxidizes ferrocyanide
-
-
?
additional information
?
-
-
enzyme oxidizes ferrocyanide
-
-
?
additional information
?
-
-
large substrates have no ready access to the catalytic center
-
-
?
additional information
?
-
-
large substrates have no ready access to the catalytic center
-
-
?
additional information
?
-
-
presence of proximal and distal histidines at the active center
-
-
?
additional information
?
-
-
Mn2+-dependent oxidation of 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
-
-
?
additional information
?
-
-
Mn2+-independent oxidase activity on NAD(P)H
-
-
?
additional information
?
-
-
in absence of H2O2 the enzyme oxidizes Mn-dependently NADPH+ to NADP+
-
-
?
additional information
?
-
-
in absence of H2O2 the enzyme oxidizes Mn-dependently NADPH+ to NADP+
-
-
?
additional information
?
-
-
in absence of H2O2 the enzyme oxidizes Mn-dependently NADPH+ to NADP+
-
-
?
additional information
?
-
-
in absence of H2O2 the enzyme oxidizes Mn-dependently NADPH+ to NADP+
-
-
?
additional information
?
-
-
enzyme oxidizes phenol red
-
-
?
additional information
?
-
-
enzyme oxidizes phenol red
-
-
?
additional information
?
-
-
enzyme oxidizes phenol red
-
-
?
additional information
?
-
-
enzyme oxidizes bromide
-
-
?
additional information
?
-
-
no other metal can substitute Mn2+
-
-
?
additional information
?
-
-
Mn2+-independent oxidation of small phenolic compounds, such as guaiacol and dimethoxyphenol, rates are greatly reduced compared with the Mn-mediated reaction
-
-
?
additional information
?
-
-
MnP oxidizes nitroaromatic compounds
-
-
?
additional information
?
-
-
enzyme oxidizes 2,6-dimethoxyphenol
-
-
?
additional information
?
-
-
enzyme oxidizes the polymeric dyes poly R-481 and poly B-411
-
-
?
additional information
?
-
-
in presence of Mn2+ enzyme oxidizes various organic compounds
-
-
?
additional information
?
-
-
in presence of Mn2+ enzyme oxidizes various organic compounds
-
-
?
additional information
?
-
-
in presence of Mn2+ enzyme oxidizes various organic compounds
-
-
?
additional information
?
-
-
in presence of Mn2+ enzyme oxidizes various organic compounds
-
-
?
additional information
?
-
-
no oxidation of Ni2+
-
-
?
additional information
?
-
-
no oxidation of Ni2+
-
-
?
additional information
?
-
-
in absence of H2O2 the enzyme oxidizes Mn-dependently NADH to NAD+
-
-
?
additional information
?
-
-
manganese peroxidase (MnP) is applied to induce the in vitro oxidation of the broad-spectrum antibiotic sulfamethoxazole (SMX). 87.04% of the SMX is transformed following first-order kinetics (kobs = 0.438/h) within 6 h when 40 U/l of MnP is added. The reaction kinetics are investigated under different conditions, including pH, MnP activity, and H2O2 concentration. The active species Mn3+ is responsible for the oxidation of SMX, and the Mn3+ production rate is monitored to reveal the interaction among MnP, Mn3+, and SMX, computational analysis, overview. Possible oxidation pathways of SMX are proposed based on single-electron transfer mechanism, which primarily included the S-N bond cleavage, the C-S bond cleavage, and one electron loss without bond breakage. It is then transformed to hydrolysis, N-H oxidation, self-coupling, and carboxylic acid coupling products. SMX stepwise undergoes an N-H oxidation and eventually converts into nitroso benzene and a nitro benzene compound. In addition, the sulfamethoxazole cation radical can also turn into self-coupling products, such as SMX-dimer
-
-
-
additional information
?
-
-
enzyme oxidizes phenol red
-
-
?
additional information
?
-
-
in presence of Mn2+ enzyme oxidizes various organic compounds
-
-
?
additional information
?
-
-
in absence of H2O2 the enzyme shows Mn-dependent oxidase activity against glutathione, dithiothreitol and dihydroxymaleic acid, forming H2O2 at the expense of oxygen
-
-
?
additional information
?
-
-
in presence of H2O2 and Mn2+ the enzyme oxidizes a variety of phenolic compounds, especially vinyl and syringyl side-chain substituted substrates
-
-
?
additional information
?
-
-
in absence of H2O2 the enzyme oxidizes Mn-dependently NADPH+ to NADP+
-
-
?
additional information
?
-
-
in absence of H2O2 the enzyme oxidizes Mn-dependently NADH to NAD+
-
-
?
additional information
?
-
-
manganese peroxidase (MnP) is applied to induce the in vitro oxidation of the broad-spectrum antibiotic sulfamethoxazole (SMX). 87.04% of the SMX is transformed following first-order kinetics (kobs = 0.438/h) within 6 h when 40 U/l of MnP is added. The reaction kinetics are investigated under different conditions, including pH, MnP activity, and H2O2 concentration. The active species Mn3+ is responsible for the oxidation of SMX, and the Mn3+ production rate is monitored to reveal the interaction among MnP, Mn3+, and SMX, computational analysis, overview. Possible oxidation pathways of SMX are proposed based on single-electron transfer mechanism, which primarily included the S-N bond cleavage, the C-S bond cleavage, and one electron loss without bond breakage. It is then transformed to hydrolysis, N-H oxidation, self-coupling, and carboxylic acid coupling products. SMX stepwise undergoes an N-H oxidation and eventually converts into nitroso benzene and a nitro benzene compound. In addition, the sulfamethoxazole cation radical can also turn into self-coupling products, such as SMX-dimer
-
-
-
additional information
?
-
-
manganese peroxidase (MnP) is applied to induce the in vitro oxidation of the broad-spectrum antibiotic sulfamethoxazole (SMX). 87.04% of the SMX is transformed following first-order kinetics (kobs = 0.438/h) within 6 h when 40 U/l of MnP is added. The reaction kinetics are investigated under different conditions, including pH, MnP activity, and H2O2 concentration. The active species Mn3+ is responsible for the oxidation of SMX, and the Mn3+ production rate is monitored to reveal the interaction among MnP, Mn3+, and SMX, computational analysis, overview. Possible oxidation pathways of SMX are proposed based on single-electron transfer mechanism, which primarily included the S-N bond cleavage, the C-S bond cleavage, and one electron loss without bond breakage. It is then transformed to hydrolysis, N-H oxidation, self-coupling, and carboxylic acid coupling products. SMX stepwise undergoes an N-H oxidation and eventually converts into nitroso benzene and a nitro benzene compound. In addition, the sulfamethoxazole cation radical can also turn into self-coupling products, such as SMX-dimer
-
-
-
additional information
?
-
-
structural properties
-
-
?
additional information
?
-
structural properties
-
-
?
additional information
?
-
enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
-
-
?
additional information
?
-
-
catalytic cycle with oxidized intermediates MnP compound I and II
-
-
?
additional information
?
-
-
large substrates have no ready access to the catalytic center
-
-
?
additional information
?
-
-
enzyme oxidizes 2,6-dimethoxyphenol
-
-
?
additional information
?
-
-
presence of proximal and distal histidines at the active center
-
-
?
additional information
?
-
-
enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
-
-
?
additional information
?
-
-
catalytic cycle: MnP is oxidized by H2O2 to compound I, Mn2+, ferrocyanide or phenols reduce compound I to compound II, which is reduced to the ferric state by Mn2+ or ferrocyanide, but not by phenols, Mn2+ completes the cycle, substrates are oxidized via delta-meso heme edge of the enzyme, model of the active site
-
-
?
additional information
?
-
-
enzyme oxidizes ferrocyanide
-
-
?
additional information
?
-
-
enzyme oxidizes a variety of organic compounds in presence, but not in absence of Mn2+
-
-
?
additional information
?
-
-
enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
-
-
?
additional information
?
-
-
in absence of H2O2 the enzyme oxidizes Mn-dependently NADH to NAD+, generating H2O2 for oxidizing other substrates
-
-
?
additional information
?
-
-
in absence of H2O2 the enzyme oxidizes Mn-dependently NADPH+ to NADP+
-
-
?
additional information
?
-
-
no other metal can substitute Mn2+
-
-
?
additional information
?
-
-
structural properties
-
-
?
additional information
?
-
-
catalytic cycle with oxidized intermediates MnP compound I and II
-
-
?
additional information
?
-
-
enzyme oxidizes ferrocyanide
-
-
?
additional information
?
-
-
enzyme oxidizes bromide
-
-
?
additional information
?
-
-
catalytic cycle with oxidized intermediates MnP compound I and II
-
-
?
additional information
?
-
-
enzyme oxidizes ferrocyanide
-
-
?
additional information
?
-
-
catalytic cycle with oxidized intermediates MnP compound I and II
-
-
?
additional information
?
-
-
Mn2+-independent oxidation of small phenolic compounds, such as guaiacol and dimethoxyphenol, rates are greatly reduced compared with the Mn-mediated reaction
-
-
?
additional information
?
-
-
catalytic cycle with oxidized intermediates MnP compound I and II
-
-
?
additional information
?
-
-
enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
-
-
?
additional information
?
-
-
catalytic cycle with oxidized intermediates MnP compound I and II
-
-
?
additional information
?
-
-
Mn2+-independent peroxidase activity on 2,6-dimethoxyphenol and veratryl alcohol
-
-
?
additional information
?
-
-
enzyme oxidizes a variety of organic compounds in presence, but not in absence of Mn2+
-
-
?
additional information
?
-
-
no activity with veratryl alcohol
-
-
?
additional information
?
-
-
poor substrates: benzoate, benzaldehyde or benzyl alcohol
-
-
?
additional information
?
-
-
enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
-
-
?
additional information
?
-
-
in absence of H2O2 the enzyme oxidizes Mn-dependently NADH to NAD+, generating H2O2 for oxidizing other substrates
-
-
?
additional information
?
-
-
catalytic cycle with oxidized intermediates MnP compound I and II
-
-
?
additional information
?
-
-
no activity with veratryl alcohol
-
-
?
additional information
?
-
-
Mn-dependent oxidation of phenols requires superoxide anion and H2O2, phenolic hydroxyl group is essential
-
-
?
additional information
?
-
-
in absence of H2O2 the enzyme oxidizes Mn-dependently NADPH+ to NADP+
-
-
?
additional information
?
-
-
MnP oxidizes nitroaromatic compounds
-
-
?
additional information
?
-
-
in presence of Mn2+ enzyme oxidizes various organic compounds
-
-
?
additional information
?
-
-
poor substrates: benzoate, benzaldehyde or benzyl alcohol
-
-
?
additional information
?
-
-
enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
in absence of Mn2+ the enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
-
-
?
additional information
?
-
-
in absence of Mn2+ the enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
-
-
?
additional information
?
-
-
Mn2+-independent peroxidase activity on 2,6-dimethoxyphenol and veratryl alcohol
-
-
?
additional information
?
-
-
Mn2+-independent peroxidase activity on 2,6-dimethoxyphenol and veratryl alcohol
-
-
?
additional information
?
-
-
Mn2+-independent peroxidase activity on 2,6-dimethoxyphenol and veratryl alcohol
-
-
?
additional information
?
-
-
Mn2+-independent peroxidase activity against phenolic substrates, e.g. phenol red
-
-
?
additional information
?
-
-
Mn2+-dependent oxidation of 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
-
-
?
additional information
?
-
-
Mn2+-independent oxidase activity on NAD(P)H
-
-
?
additional information
?
-
-
Mn2+-independent oxidase activity on NAD(P)H
-
-
?
additional information
?
-
-
MnP oxidizes phenolic and nonphenolic aromatic compounds, e.g. phenol red and veratryl alcohol
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
in absence of Mn2+ the enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
-
-
?
additional information
?
-
-
in absence of Mn2+ the enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
-
-
?
additional information
?
-
-
Mn2+-independent peroxidase activity on 2,6-dimethoxyphenol and veratryl alcohol
-
-
?
additional information
?
-
-
Mn2+-independent peroxidase activity on 2,6-dimethoxyphenol and veratryl alcohol
-
-
?
additional information
?
-
-
Mn2+-independent peroxidase activity on 2,6-dimethoxyphenol and veratryl alcohol
-
-
?
additional information
?
-
-
enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
-
-
?
additional information
?
-
-
no activity with veratryl alcohol
-
-
?
additional information
?
-
-
no activity with veratryl alcohol
-
-
?
additional information
?
-
-
Mn2+-independent oxidase activity on NAD(P)H
-
-
?
additional information
?
-
-
Mn2+-independent oxidase activity on NAD(P)H
-
-
?
additional information
?
-
-
Mn2+-dependent and Mn2+-independent peroxidase activities when tested on the phenolic substrates 2,6-dimethoxyphenol, 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate, guaiacol and syringaldazine, more rapid oxidation in presence of Mn2+
-
-
?
additional information
?
-
-
enzyme oxidizes 2,6-dimethoxyphenol
-
-
?
additional information
?
-
-
direct oxidation of Rnase by MnP2
-
-
?
additional information
?
-
-
in absence of Mn2+ the enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
-
-
?
additional information
?
-
-
Mn2+-independent peroxidase activity on 2,6-dimethoxyphenol and veratryl alcohol
-
-
?
additional information
?
-
-
Mn2+-independent oxidase activity on NAD(P)H
-
-
?
additional information
?
-
-
in absence of Mn2+ the enzyme oxidizes 2,2-azino-di-3-ethylbenzothiazoline-6-sulfonate
-
-
?
additional information
?
-
-
Mn2+-independent peroxidase activity on 2,6-dimethoxyphenol and veratryl alcohol
-
-
?
additional information
?
-
-
Mn2+-independent oxidase activity on NAD(P)H
-
-
?
additional information
?
-
-
MnP activity is determined by monitoring the oxidation of 2,6-dimethoxyphenol (DMP) as the oxidation of Mn2+ to Mn3+ by following the formation of the Mn3+-tartrate complex at 469 nm
-
-
-
additional information
?
-
-
the enzyme efficiently decolorized azo dyes such as Congo Red, Orange G and Orange IV
-
-
?
additional information
?
-
-
the enzyme efficiently decolorized azo dyes such as Congo Red, Orange G and Orange IV
-
-
?
additional information
?
-
-
MnP oxidizes nitroaromatic compounds
-
-
?
additional information
?
-
-
the enzyme is essential for lignin degradation
-
-
?
additional information
?
-
-
the enzyme is essential for lignin degradation
-
-
?
additional information
?
-
-
the enzyme is essential for lignin degradation
-
-
?
additional information
?
-
-
MnP oxidizes synthetic melanoidine
-
-
?
additional information
?
-
-
the enzyme is essential for lignin degradation
-
-
?
additional information
?
-
-
lingnin containing agricultural waste, like almond shells, hazelnut husks, clover straw, sunflower stems and hazelnut cobs are used as substrate for submerged cultures
-
-
?
additional information
?
-
-
the enzyme is essential for lignin degradation
-
-
?
additional information
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no oxidation of veratryl alcohol
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additional information
?
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no oxidation of veratryl alcohol
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evolution
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DNA sequence comparisons and phylogenetic analysis and tree
evolution
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DNA sequence comparisons and phylogenetic analysis and tree
evolution
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DNA sequence comparisons and phylogenetic analysis and tree
evolution
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DNA sequence comparisons and phylogenetic analysis and tree
evolution
maganese peroxidases (MnPs) can be divided into groups of short, long, and extra-long MnPs. The length of long MnPs is 348-361 amino acids, extra-long MnPs are longer than 362 amino acids, and short MnPs are no longer than 348 amino acids. The long and extralong MnPs are characterized by a C-terminal tail that surrounds the main heme access channel, preventing oxidation of low-redox-potential substrates (e.g. ABTS, 2,6-DMP). MrMnP1 is 343 amino acids long and can be categorized as a short MnP
evolution
MGMnPs may have evolved to adapt to chloride-rich environments, e.g. mangrove forests
evolution
MnP124076 is the only short MnP found in Ceriporiopsis subvermispora, MnP157986 is an extralong MnP and has the longest amino acid sequence. MnP50297 and MnP117436 are an extralong MnP and a long MnP, respectively, and they are the most abundantly produced MnPs in each subfamily by Ceriporiopsis subvermispora grown in aspen wood-containing medium
evolution
the enzyme belongs to the class II fungal peroxidases (PODs)
evolution
the enzyme belongs to the ligninolytic peroxidase gene family, 13 MnP genes and five dye-decolorizing peroxidase (DyP) genes are present in the Irpex lacteus strain F17 genome, they represent two different families of heme peroxidases and are unrelated to the fungal class II peroxidases
evolution
-
the enzyme belongs to the ligninolytic peroxidase gene family, 13 MnP genes and five dye-decolorizing peroxidase (DyP) genes are present in the Irpex lacteus strain F17 genome, they represent two different families of heme peroxidases and are unrelated to the fungal class II peroxidases
-
evolution
-
the enzyme belongs to the class II fungal peroxidases (PODs)
-
evolution
-
maganese peroxidases (MnPs) can be divided into groups of short, long, and extra-long MnPs. The length of long MnPs is 348-361 amino acids, extra-long MnPs are longer than 362 amino acids, and short MnPs are no longer than 348 amino acids. The long and extralong MnPs are characterized by a C-terminal tail that surrounds the main heme access channel, preventing oxidation of low-redox-potential substrates (e.g. ABTS, 2,6-DMP). MrMnP1 is 343 amino acids long and can be categorized as a short MnP
-
evolution
-
MnP124076 is the only short MnP found in Ceriporiopsis subvermispora, MnP157986 is an extralong MnP and has the longest amino acid sequence. MnP50297 and MnP117436 are an extralong MnP and a long MnP, respectively, and they are the most abundantly produced MnPs in each subfamily by Ceriporiopsis subvermispora grown in aspen wood-containing medium
-
evolution
-
the enzyme belongs to the class II fungal peroxidases (PODs)
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physiological function
-
lignin-degrading enzyme
physiological function
-
a potential aerobic bacterial consortium is identified consisting of Klebsiella pneumoniae (KU726953), Salmonella enterica (KU726954), Enterobacter aerogenes (KU726955), Enterobacter cloaceae (KU726957) that show optimum production of maganese peroxidase (MnP) and laccase at 120 and 144 h of growth, respectively. The bacterial consortium causes decolourisation of Maillard reactions products (MRPs) up to 70% in presence of glucose (1%), peptone (0.1%) at optimum pH (8.1), temperature (37°C) and shaking speed (180 rpm) within 192 h of incubation, method optimization and evaluation, overview. The reduction of colour of sucrose glutamic acid-Maillard reaction products (SGA-MRPs) correlates with shifting of absorption peaks in UV-Vis spectrophotometry analysis. Further, the changing of functional group in FT-IR data shows appearance of new peaks and GC-MS analysis of degraded sample revealed the depolymerisation of complex MRPs. Maillard reactions products (MRPs) are a major colorant of distillery effluent. They are a major source of environmental pollution due to their complex structures and recalcitrant nature. The toxicity evaluation using seed of Phaseolus mungo L. reveals a reduction of toxicity of MRPs after bacterial treatment
physiological function
-
a potential aerobic bacterial consortium is identified consisting of Klebsiella pneumoniae (KU726953), Salmonella enterica (KU726954), Enterobacter aerogenes (KU726955), Enterobacter cloaceae (KU726957) that show optimum production of maganese peroxidase (MnP) and laccase at 120 and 144 h of growth, respectively. The bacterial consortium causes decolourisation of Maillard reactions products (MRPs) up to 70% in presence of glucose (1%), peptone (0.1%) at optimum pH (8.1), temperature (37°C) and shaking speed (180 rpm) within 192 h of incubation, method optimization and evaluation, overview. The reduction of colour of sucrose glutamic acid-Maillard reaction products (SGA-MRPs) correlates with shifting of absorption peaks in UV-Vis spectrophotometry analysis. Further, the changing of functional group in FT-IR data shows appearance of new peaks and GC-MS analysis of degraded sample revealed the depolymerisation of complex MRPs. Maillard reactions products (MRPs) are a major colorant of distillery effluent. They are a major source of environmental pollution due to their complex structures and recalcitrant nature. The toxicity evaluation using seed of Phaseolus mungo L. reveals a reduction of toxicity of MRPs after bacterial treatment
physiological function
-
a potential aerobic bacterial consortium is identified consisting of Klebsiella pneumoniae (KU726953), Salmonella enterica (KU726954), Enterobacter aerogenes (KU726955), Enterobacter cloaceae (KU726957) that show optimum production of maganese peroxidase (MnP) and laccase at 120 and 144 h of growth, respectively. The bacterial consortium causes decolourisation of Maillard reactions products (MRPs) up to 70% in presence of glucose (1%), peptone (0.1%) at optimum pH (8.1), temperature (37°C) and shaking speed (180 rpm) within 192 h of incubation, method optimization and evaluation, overview. The reduction of colour of sucrose glutamic acid-Maillard reaction products (SGA-MRPs) correlates with shifting of absorption peaks in UV-Vis spectrophotometry analysis. Further, the changing of functional group in FT-IR data shows appearance of new peaks and GC-MS analysis of degraded sample revealed the depolymerisation of complex MRPs. Maillard reactions products (MRPs) are a major colorant of distillery effluent. They are a major source of environmental pollution due to their complex structures and recalcitrant nature. The toxicity evaluation using seed of Phaseolus mungo L. reveals a reduction of toxicity of MRPs after bacterial treatment
physiological function
-
a potential aerobic bacterial consortium is identified consisting of Klebsiella pneumoniae (KU726953), Salmonella enterica (KU726954), Enterobacter aerogenes (KU726955), Enterobacter cloaceae (KU726957) that show optimum production of maganese peroxidase (MnP) and laccase at 120 and 144 h of growth, respectively. The bacterial consortium causes decolourisation of Maillard reactions products (MRPs) up to 70% in presence of glucose (1%), peptone (0.1%) at optimum pH (8.1), temperature (37°C) and shaking speed (180 rpm) within 192 h of incubation, method optimization and evaluation, overview. The reduction of colour of sucrose glutamic acid-Maillard reaction products (SGA-MRPs) correlates with shifting of absorption peaks in UV-Vis spectrophotometry analysis. Further, the changing of functional group in FT-IR data shows appearance of new peaks and GC-MS analysis of degraded sample revealed the depolymerisation of complex MRPs. Maillard reactions products (MRPs) are a major colorant of distillery effluent. They are a major source of environmental pollution due to their complex structures and recalcitrant nature. The toxicity evaluation using seed of Phaseolus mungo L. reveals a reduction of toxicity of MRPs after bacterial treatment
physiological function
class II fungal peroxidases (PODs), manganese peroxidases (MnPs) are named for their strongMn2+-dependent oxidative activity for an array of aromatic substrates, including phenols, nonphenols, and various industrial dyes
physiological function
-
enzyme MnP generates Mn3+ (act as a diffusible charge transfer mediators) which can oxidize a large amount of phenolic substrates such as simple phenols, amines, dyes as well as phenolic lignin model compounds. In contrast to laccase, MnP is not capable of oxidizing the more recalcitrant nonphenolic compounds
physiological function
manganese peroxidase (MnP) is an extracellular glycosylated heme protein produced by various basidiomycetous fungi. It requires hydrogen peroxide as an oxidant to function. In the catalytic cycle of MnP, Mn2+ is oxidized into Mn3+. A complex of Mn3+ and organic acid with low molecular weight is subsequently formed and acts as a diffusible redox-mediator to attack phenolic lignin structures and break the aromatic rings of lignin polymers. The recombinant isozyme MnP3 from Cerrena unicolor strain BBP6 has strong decolorizing activity on a variety of dyes and it is efficient in denim bleaching. It is also able to degrade fluorene and phenanthrene effectively. Due to its broad substrate specificity, MnP is capable of transforming many structurally different pollutants such as synthetic dyes, PAHs and pesticides
physiological function
-
manganese peroxidase (MnP) is the most common lignin-degrading enzyme produced by white-rot basidiomycetes fungi. It can catalyze Mn2+ into Mn3+ by the addition of H2O2 or organic peroxide, and it can mediate the oxidation of a substrate
physiological function
-
manganese peroxidase is a key contributor in the microbial ligninolytic system. It mainly oxidizes Mn2+ ions that remain present in wood and soils, into more reactive Mn3+ form, stabilized by fungal chelators like oxalic acids. Mn3+ acts as a diffusible redox intermediate, a low molecular weight compound, which breaks phenolic lignin and produces free radicals that have a tendency to disintegrate involuntarily
physiological function
-
manganese peroxidase is a key contributor in the microbial ligninolytic system. It mainly oxidizes Mn2+ ions that remain present in wood and soils, into more reactive Mn3+ form, stabilized by fungal chelators like oxalic acids. Mn3+ acts as a diffusible redox intermediate, a low molecular weight compound, which breaks phenolic lignin and produces free radicals that have a tendency to disintegrate involuntarily
physiological function
-
manganese peroxidase is a key contributor in the microbial ligninolytic system. It mainly oxidizes Mn2+ ions that remain present in wood and soils, into more reactive Mn3+ form, stabilized by fungal chelators like oxalic acids. Mn3+ acts as a diffusible redox intermediate, a low molecular weight compound, which breaks phenolic lignin and produces free radicals that have a tendency to disintegrate involuntarily
physiological function
-
manganese peroxidase is a key contributor in the microbial ligninolytic system. It mainly oxidizes Mn2+ ions that remain present in wood and soils, into more reactive Mn3+ form, stabilized by fungal chelators like oxalic acids. Mn3+ acts as a diffusible redox intermediate, a low molecular weight compound, which breaks phenolic lignin and produces free radicals that have a tendency to disintegrate involuntarily
physiological function
manganese peroxidase is a key contributor in the microbial ligninolytic system. It mainly oxidizes Mn2+ ions that remain present in wood and soils, into more reactive Mn3+ form, stabilized by fungal chelators like oxalic acids. Mn3+ acts as a diffusible redox intermediate, a low molecular weight compound, which breaks phenolic lignin and produces free radicals that have a tendency to disintegrate involuntarily
physiological function
manganese peroxidase is a key contributor in the microbial ligninolytic system. It mainly oxidizes Mn2+ ions that remain present in wood and soils, into more reactive Mn3+ form, stabilized by fungal chelators like oxalic acids. Mn3+ acts as a diffusible redox intermediate, a low molecular weight compound, which breaks phenolic lignin and produces free radicals that have a tendency to disintegrate involuntarily
physiological function
-
manganese peroxidase is a key contributor in the microbial ligninolytic system. It mainly oxidizes Mn2+ ions that remain present in wood and soils, into more reactive Mn3+ form, stabilized by fungal chelators like oxalic acids. Mn3+ acts as a diffusible redox intermediate, a low molecular weight compound, which breaks phenolic lignin and produces free radicals that have a tendency to disintegrate involuntarily
physiological function
-
manganese peroxidase is a key contributor in the microbial ligninolytic system. It mainly oxidizes Mn2+ ions that remain present in wood and soils, into more reactive Mn3+ form, stabilized by fungal chelators like oxalic acids. Mn3+ acts as a diffusible redox intermediate, a low molecular weight compound, which breaks phenolic lignin and produces free radicals that have a tendency to disintegrate involuntarily
physiological function
-
manganese peroxidase is a key contributor in the microbial ligninolytic system. It mainly oxidizes Mn2+ ions that remain present in wood and soils, into more reactive Mn3+ form, stabilized by fungal chelators like oxalic acids. Mn3+ acts as a diffusible redox intermediate, a low molecular weight compound, which breaks phenolic lignin and produces free radicals that have a tendency to disintegrate involuntarily
physiological function
manganese peroxidase is a key contributor in the microbial ligninolytic system. It mainly oxidizes Mn2+ ions that remain present in wood and soils, into more reactive Mn3+ form, stabilized by fungal chelators like oxalic acids. Mn3+ acts as a diffusible redox intermediate, a low molecular weight compound, which breaks phenolic lignin and produces free radicals that have a tendency to disintegrate involuntarily
physiological function
manganese peroxidase is a key contributor in the microbial ligninolytic system. It mainly oxidizes Mn2+ ions that remain present in wood and soils, into more reactive Mn3+ form, stabilized by fungal chelators like oxalic acids. Mn3+ acts as a diffusible redox intermediate, a low molecular weight compound, which breaks phenolic lignin and produces free radicals that have a tendency to disintegrate involuntarily
physiological function
manganese peroxidase is a key contributor in the microbial ligninolytic system. It mainly oxidizes Mn2+ ions that remain present in wood and soils, into more reactive Mn3+ form, stabilized by fungal chelators like oxalic acids. Mn3+ acts as a diffusible redox intermediate, a low molecular weight compound, which breaks phenolic lignin and produces free radicals that have a tendency to disintegrate involuntarily
physiological function
manganese peroxidase is a key contributor in the microbial ligninolytic system. It mainly oxidizes Mn2+ ions that remain present in wood and soils, into more reactive Mn3+ form, stabilized by fungal chelators like oxalic acids. Mn3+ acts as a diffusible redox intermediate, a low molecular weight compound, which breaks phenolic lignin and produces free radicals that have a tendency to disintegrate involuntarily
physiological function
-
manganese peroxidase is a key contributor in the microbial ligninolytic system. It mainly oxidizes Mn2+ ions that remain present in wood and soils, into more reactive Mn3+ form, stabilized by fungal chelators like oxalic acids. Mn3+ acts as a diffusible redox intermediate, a low molecular weight compound, which breaks phenolic lignin and produces free radicals that have a tendency to disintegrate involuntarily
physiological function
-
the crude manganese peroxidase from Bacillus velezensis strain Al-Dhabi 140 shows an optimum degradation process and maximum removal efficacy of 87 mg/l at tetracycline concentration 143.75 mg/l, pH 6.9, and 8.04% inoculum
physiological function
the manganese peroxidase of Irpex lacteus strain 17 is able to degrade recalcitrant aromatic pollutants
physiological function
-
manganese peroxidase is a key contributor in the microbial ligninolytic system. It mainly oxidizes Mn2+ ions that remain present in wood and soils, into more reactive Mn3+ form, stabilized by fungal chelators like oxalic acids. Mn3+ acts as a diffusible redox intermediate, a low molecular weight compound, which breaks phenolic lignin and produces free radicals that have a tendency to disintegrate involuntarily
-
physiological function
-
lignin-degrading enzyme
-
physiological function
Bacillus velezensis Al-Dhabi 140
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the crude manganese peroxidase from Bacillus velezensis strain Al-Dhabi 140 shows an optimum degradation process and maximum removal efficacy of 87 mg/l at tetracycline concentration 143.75 mg/l, pH 6.9, and 8.04% inoculum
-
physiological function
-
the manganese peroxidase of Irpex lacteus strain 17 is able to degrade recalcitrant aromatic pollutants
-
physiological function
-
class II fungal peroxidases (PODs), manganese peroxidases (MnPs) are named for their strongMn2+-dependent oxidative activity for an array of aromatic substrates, including phenols, nonphenols, and various industrial dyes
-
physiological function
-
manganese peroxidase is a key contributor in the microbial ligninolytic system. It mainly oxidizes Mn2+ ions that remain present in wood and soils, into more reactive Mn3+ form, stabilized by fungal chelators like oxalic acids. Mn3+ acts as a diffusible redox intermediate, a low molecular weight compound, which breaks phenolic lignin and produces free radicals that have a tendency to disintegrate involuntarily
-
physiological function
-
manganese peroxidase is a key contributor in the microbial ligninolytic system. It mainly oxidizes Mn2+ ions that remain present in wood and soils, into more reactive Mn3+ form, stabilized by fungal chelators like oxalic acids. Mn3+ acts as a diffusible redox intermediate, a low molecular weight compound, which breaks phenolic lignin and produces free radicals that have a tendency to disintegrate involuntarily
-
physiological function
-
manganese peroxidase is a key contributor in the microbial ligninolytic system. It mainly oxidizes Mn2+ ions that remain present in wood and soils, into more reactive Mn3+ form, stabilized by fungal chelators like oxalic acids. Mn3+ acts as a diffusible redox intermediate, a low molecular weight compound, which breaks phenolic lignin and produces free radicals that have a tendency to disintegrate involuntarily
-
physiological function
-
manganese peroxidase is a key contributor in the microbial ligninolytic system. It mainly oxidizes Mn2+ ions that remain present in wood and soils, into more reactive Mn3+ form, stabilized by fungal chelators like oxalic acids. Mn3+ acts as a diffusible redox intermediate, a low molecular weight compound, which breaks phenolic lignin and produces free radicals that have a tendency to disintegrate involuntarily
-
physiological function
-
manganese peroxidase (MnP) is the most common lignin-degrading enzyme produced by white-rot basidiomycetes fungi. It can catalyze Mn2+ into Mn3+ by the addition of H2O2 or organic peroxide, and it can mediate the oxidation of a substrate
-
physiological function
-
class II fungal peroxidases (PODs), manganese peroxidases (MnPs) are named for their strongMn2+-dependent oxidative activity for an array of aromatic substrates, including phenols, nonphenols, and various industrial dyes
-
physiological function
-
manganese peroxidase (MnP) is an extracellular glycosylated heme protein produced by various basidiomycetous fungi. It requires hydrogen peroxide as an oxidant to function. In the catalytic cycle of MnP, Mn2+ is oxidized into Mn3+. A complex of Mn3+ and organic acid with low molecular weight is subsequently formed and acts as a diffusible redox-mediator to attack phenolic lignin structures and break the aromatic rings of lignin polymers. The recombinant isozyme MnP3 from Cerrena unicolor strain BBP6 has strong decolorizing activity on a variety of dyes and it is efficient in denim bleaching. It is also able to degrade fluorene and phenanthrene effectively. Due to its broad substrate specificity, MnP is capable of transforming many structurally different pollutants such as synthetic dyes, PAHs and pesticides
-
physiological function
-
manganese peroxidase is a key contributor in the microbial ligninolytic system. It mainly oxidizes Mn2+ ions that remain present in wood and soils, into more reactive Mn3+ form, stabilized by fungal chelators like oxalic acids. Mn3+ acts as a diffusible redox intermediate, a low molecular weight compound, which breaks phenolic lignin and produces free radicals that have a tendency to disintegrate involuntarily
-
physiological function
-
manganese peroxidase (MnP) is the most common lignin-degrading enzyme produced by white-rot basidiomycetes fungi. It can catalyze Mn2+ into Mn3+ by the addition of H2O2 or organic peroxide, and it can mediate the oxidation of a substrate
-
additional information
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GS-MS analysis of organic compounds and products in the ethyl acetate extracted untreated and bacterially-treated sucrose glutamic acid-Maillard reaction products (SGA-MRPs) solution, overview
additional information
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GS-MS analysis of organic compounds and products in the ethyl acetate extracted untreated and bacterially-treated sucrose glutamic acid-Maillard reaction products (SGA-MRPs) solution, overview
additional information
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GS-MS analysis of organic compounds and products in the ethyl acetate extracted untreated and bacterially-treated sucrose glutamic acid-Maillard reaction products (SGA-MRPs) solution, overview
additional information
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GS-MS analysis of organic compounds and products in the ethyl acetate extracted untreated and bacterially-treated sucrose glutamic acid-Maillard reaction products (SGA-MRPs) solution, overview
additional information
role of Glu166 in the Mn2+-independent activity
additional information
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role of Glu166 in the Mn2+-independent activity
additional information
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screening and tetracycline degrading efficiency of the five bacteria isolated from the municipal soil sludge, overview. The strain termed Al-Dhabi 140 from Bacillus velezensis shows the highest activity
additional information
the catalytic tryptophan 172 is considered to be essential for oxidizing substrates with a high redox potential
additional information
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the catalytic tryptophan 172 is considered to be essential for oxidizing substrates with a high redox potential
additional information
Bacillus velezensis Al-Dhabi 140
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screening and tetracycline degrading efficiency of the five bacteria isolated from the municipal soil sludge, overview. The strain termed Al-Dhabi 140 from Bacillus velezensis shows the highest activity
-
additional information
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role of Glu166 in the Mn2+-independent activity
-
additional information
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the catalytic tryptophan 172 is considered to be essential for oxidizing substrates with a high redox potential
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additional information
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role of Glu166 in the Mn2+-independent activity
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S168W
mutation introduced to confer Vversatile peroxidase-type activity, EC 1.11.1.16, on aromatic substrates and dyes. Variant conserves the high catalytic efficiency of isoform MnP6 oxidizing Mn2+ and gains the ability to oxidize veratryl alcohol as well as reactive black 5
T162S/S168W/F258E/F262M/F268K/Q271N/S272R/S275G
mutation introduced to confer Vversatile peroxidase-type activity, EC 1.11.1.16, on aromatic substrates and dyes. Variant conserves the high catalytic efficiency of isoform MnP6 oxidizing Mn2+ and gains the ability to oxidize veratryl alcohol as well as reactive black 5
S168W
-
mutation introduced to confer Vversatile peroxidase-type activity, EC 1.11.1.16, on aromatic substrates and dyes. Variant conserves the high catalytic efficiency of isoform MnP6 oxidizing Mn2+ and gains the ability to oxidize veratryl alcohol as well as reactive black 5
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T162S/S168W/F258E/F262M/F268K/Q271N/S272R/S275G
-
mutation introduced to confer Vversatile peroxidase-type activity, EC 1.11.1.16, on aromatic substrates and dyes. Variant conserves the high catalytic efficiency of isoform MnP6 oxidizing Mn2+ and gains the ability to oxidize veratryl alcohol as well as reactive black 5
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E166D
site-directed mutagenesis, the E166D mutant shows no obvious improvement to Mn2+-independent oxidative activity of Il-MnP1
E166G
site-directed mutagenesis, the mutant shows highly improved Mn2+-independent oxidative activity, as compared to the wild-type enzyme, with 170fold increased Kcat/Km value. Mutant E166G exhibits 27, 17, 75, 14, and 29fold increase to Mn2+-independent oxidative activity of Il-MnP1 for the phenolic substrates (DMP, guaiacol, catechol, HQ) and the nonphenolic substrate (ABTS), respectively, compared to wild-type
E166Q
site-directed mutagenesis, the mutant shows highly improved Mn2+-independent oxidative activity, as compared to the wild-type enzyme, with 34fold increased Kcat/Km value. The E166Q mutant displays a 5fold increase to the oxidative activity of Il-MnP1 for all the substrates compared to wild-type Il-MnP1
E166D
-
site-directed mutagenesis, the E166D mutant shows no obvious improvement to Mn2+-independent oxidative activity of Il-MnP1
-
E166G
-
site-directed mutagenesis, the mutant shows highly improved Mn2+-independent oxidative activity, as compared to the wild-type enzyme, with 170fold increased Kcat/Km value. Mutant E166G exhibits 27, 17, 75, 14, and 29fold increase to Mn2+-independent oxidative activity of Il-MnP1 for the phenolic substrates (DMP, guaiacol, catechol, HQ) and the nonphenolic substrate (ABTS), respectively, compared to wild-type
-
E166Q
-
site-directed mutagenesis, the mutant shows highly improved Mn2+-independent oxidative activity, as compared to the wild-type enzyme, with 34fold increased Kcat/Km value. The E166Q mutant displays a 5fold increase to the oxidative activity of Il-MnP1 for all the substrates compared to wild-type Il-MnP1
-
E166D
-
site-directed mutagenesis, the E166D mutant shows no obvious improvement to Mn2+-independent oxidative activity of Il-MnP1
-
E166G
-
site-directed mutagenesis, the mutant shows highly improved Mn2+-independent oxidative activity, as compared to the wild-type enzyme, with 170fold increased Kcat/Km value. Mutant E166G exhibits 27, 17, 75, 14, and 29fold increase to Mn2+-independent oxidative activity of Il-MnP1 for the phenolic substrates (DMP, guaiacol, catechol, HQ) and the nonphenolic substrate (ABTS), respectively, compared to wild-type
-
E166Q
-
site-directed mutagenesis, the mutant shows highly improved Mn2+-independent oxidative activity, as compared to the wild-type enzyme, with 34fold increased Kcat/Km value. The E166Q mutant displays a 5fold increase to the oxidative activity of Il-MnP1 for all the substrates compared to wild-type Il-MnP1
-
A172W
site-directed mutagenesis, the mutant shows decreased stability compared to the wild-type enzyme in Britton Robinson buffer at pH 3-7 for 24 h measured with 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) as a substrate. The mutant shows increased kcat values for all substrates compared to wild-type. The mutant is active with lignin dimers, veratryl alcohol, and the azo dye Reactive Black 5 in contrast to the wild-type enzyme
A172W/A269R
site-directed mutagenesis, the mutant shows decreased stability compared to the wild-type enzyme in Britton Robinson buffer at pH 3-7 for 24 h measured with 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) as a substrate. The mutant does not show altered kcat values for all substrates compared to wild-type. The mutant is active with lignin dimers, veratryl alcohol, and the azo dye Reactive Black 5 in contrast to the wild-type enzyme
A172W/A273T
site-directed mutagenesis, the mutant shows decreased stability compared to the wild-type enzyme in Britton Robinson buffer at pH 3-7 for 24 h measured with 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) as a substrate. The mutant shows increased kcat values for all substrates compared to wild-type. The mutant is active with lignin dimers, veratryl alcohol, and the azo dye Reactive Black 5 in contrast to the wild-type enzyme
A172W/F259M
site-directed mutagenesis, the mutant shows decreased stability compared to the wild-type enzyme in Britton Robinson buffer at pH 3-7 for 24 h measured with 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) as a substrate. The mutant shows increased kcat values for all substrates compared to wild-type. The mutant is active with lignin dimers, veratryl alcohol, and the azo dye Reactive Black 5 in contrast to the wild-type enzyme
A172W/I171V
site-directed mutagenesis, the mutant shows decreased stability compared to the wild-type enzyme in Britton Robinson buffer at pH 3-7 for 24 h measured with 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) as a substrate. The mutant shows increased kcat values for all substrates compared to wild-type. The mutant is active with lignin dimers, veratryl alcohol, and the azo dye Reactive Black 5 in contrast to the wild-type enzyme
A172W/K168V
site-directed mutagenesis, the mutant shows increased stability compared to the wild-type enzyme in Britton Robinson buffer at pH 3-7 for 24 h measured with 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) as a substrate. The mutant shows increased kcat values for all substrates compared to wild-type. The mutant is active with lignin dimers, veratryl alcohol, and the azo dye Reactive Black 5 in contrast to the wild-type enzyme
A172W
-
site-directed mutagenesis, the mutant shows decreased stability compared to the wild-type enzyme in Britton Robinson buffer at pH 3-7 for 24 h measured with 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) as a substrate. The mutant shows increased kcat values for all substrates compared to wild-type. The mutant is active with lignin dimers, veratryl alcohol, and the azo dye Reactive Black 5 in contrast to the wild-type enzyme
-
A172W/F259M
-
site-directed mutagenesis, the mutant shows decreased stability compared to the wild-type enzyme in Britton Robinson buffer at pH 3-7 for 24 h measured with 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) as a substrate. The mutant shows increased kcat values for all substrates compared to wild-type. The mutant is active with lignin dimers, veratryl alcohol, and the azo dye Reactive Black 5 in contrast to the wild-type enzyme
-
A172W/I171V
-
site-directed mutagenesis, the mutant shows decreased stability compared to the wild-type enzyme in Britton Robinson buffer at pH 3-7 for 24 h measured with 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) as a substrate. The mutant shows increased kcat values for all substrates compared to wild-type. The mutant is active with lignin dimers, veratryl alcohol, and the azo dye Reactive Black 5 in contrast to the wild-type enzyme
-
A172W/K168V
-
site-directed mutagenesis, the mutant shows increased stability compared to the wild-type enzyme in Britton Robinson buffer at pH 3-7 for 24 h measured with 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) as a substrate. The mutant shows increased kcat values for all substrates compared to wild-type. The mutant is active with lignin dimers, veratryl alcohol, and the azo dye Reactive Black 5 in contrast to the wild-type enzyme
-
A48C/A63C
-
A48C and A63C double mutant with an engineered disulfide bond near the distal calcium binding site to restrict the movement of helix B upon loss of calcium and to stabilize against this loss, thermal and pH-stability is improved compared with that of native and recombinant MnP, thermally treated enzyme contains one calcium and retains a percentage of its activity
F190A
-
mutant MnP: apparent Km-value for ferrocyanide oxidation is 1/8 of that for wild-type MnP and kcat is 4fold greater than that for wild-type enzyme, mutant enzyme is significantly destabilized to thermal denaturation, unstable at 37°C, rates of spontaneous reduction of the oxidized intermediates, compound I and II, are dramatically increased compared with those for the wild-type MnP
F190I
-
mutant enzyme is significantly destabilized to thermal denaturation, unstable at 37°C, rates of spontaneous reduction of the oxidized intermediates, compound I and II, are 2fold greater than those for the wild-type MnP
F190L
-
rates of spontaneous reduction of the oxidized intermediates, compound I and II, are 2fold greater than those for the wild-type MnP
F190Y
-
engineered mutant
M273L
mutant with high H2O2 resistance, i.e. 4.1fold higher than that of wild-type, Met-273 is located near the active site pocket and is converted to a non-oxidizable Leu
N131D
mutant displays a similar catalysis pattern to that of wild-type enzyme, Asn131 is the only potential glycosylation site
N81S
mutant enzyme is not inhibited by 1 mM H2O2, H2O2-dependency is 5.5fold higher than that of wild-type, engineering of Asn-81, which might have conformational changes due to the environment of the pocket, to a non-bulky and non-oxidizable Ser
R177A
-
mutant with reduced binding efficiency for Mn2+: disruption in the salt-bridge between Arg-177 and the Mn2+ binding ligand Glu-35
R177D
-
mutant with decreased electron-transfer rate and reduced binding efficiency for Mn2+: disruption in the salt-bridge between Arg-177 and the Mn2+ binding ligand Glu-35, higher redox potential for the enzyme-bound Mn2+
R177E
-
mutant with decreased electron-transfer rate and reduced binding efficiency for Mn2+: disruption in the salt-bridge between Arg-177 and the Mn2+ binding ligand Glu-35, higher redox potential for the enzyme-bound Mn2+
R177K
-
mutant with reduced binding efficiency for Mn2+: disruption in the salt-bridge between Arg-177 and the Mn2+ binding ligand Glu-35
R177N
-
mutant with decreased electron-transfer rate and reduced binding efficiency for Mn2+: disruption in the salt-bridge between Arg-177 and the Mn2+ binding ligand Glu-35, higher redox potential for the enzyme-bound Mn2+
R177Q
-
mutant with decreased electron-transfer rate and reduced binding efficiency for Mn2+: disruption in the salt-bridge between Arg-177 and the Mn2+ binding ligand Glu-35, higher redox potential for the enzyme-bound Mn2+
R42A
mutant displays a similar catalysis pattern to that of wild-type enzyme, Arg42 is forming the peroxide binding pocket
S168W
-
mutant can oxidize both Mn2+ and typical lignin peroxidase substrates such as veratryl alcohol
M237L
-
engineered mutant
-
M273L
-
mutant with high H2O2 resistance, i.e. 4.1fold higher than that of wild-type, Met-273 is located near the active site pocket and is converted to a non-oxidizable Leu
-
M67L
-
engineered mutant
-
N81S
-
mutant enzyme is not inhibited by 1 mM H2O2, H2O2-dependency is 5.5fold higher than that of wild-type, engineering of Asn-81, which might have conformational changes due to the environment of the pocket, to a non-bulky and non-oxidizable Ser
-
F190A
-
mutant MnP: apparent Km-value for ferrocyanide oxidation is 1/8 of that for wild-type MnP and kcat is 4fold greater than that for wild-type enzyme, mutant enzyme is significantly destabilized to thermal denaturation, unstable at 37°C, rates of spontaneous reduction of the oxidized intermediates, compound I and II, are dramatically increased compared with those for the wild-type MnP
-
F190I
-
mutant enzyme is significantly destabilized to thermal denaturation, unstable at 37°C, rates of spontaneous reduction of the oxidized intermediates, compound I and II, are 2fold greater than those for the wild-type MnP
-
F190L
-
rates of spontaneous reduction of the oxidized intermediates, compound I and II, are 2fold greater than those for the wild-type MnP
-
F190Y
-
engineered mutant
-
R177A
-
mutant with reduced binding efficiency for Mn2+: disruption in the salt-bridge between Arg-177 and the Mn2+ binding ligand Glu-35
-
R177D
-
mutant with decreased electron-transfer rate and reduced binding efficiency for Mn2+: disruption in the salt-bridge between Arg-177 and the Mn2+ binding ligand Glu-35, higher redox potential for the enzyme-bound Mn2+
-
R177E
-
mutant with decreased electron-transfer rate and reduced binding efficiency for Mn2+: disruption in the salt-bridge between Arg-177 and the Mn2+ binding ligand Glu-35, higher redox potential for the enzyme-bound Mn2+
-
R177K
-
mutant with reduced binding efficiency for Mn2+: disruption in the salt-bridge between Arg-177 and the Mn2+ binding ligand Glu-35
-
R177N
-
mutant with decreased electron-transfer rate and reduced binding efficiency for Mn2+: disruption in the salt-bridge between Arg-177 and the Mn2+ binding ligand Glu-35, higher redox potential for the enzyme-bound Mn2+
-
additional information
-
usage of a fibrous bed reactor to culture of Bacilllus velezensis strain Al-Dhabi 140 on fibrous matrix to transform tetracycline in synthetic wastewater. The transformed product of tetracycline from the fibrous bed reactor is evident by the activity of ligninolytic enzymes produced by Bacillus velezensis strain Al-Dhabi 140 in reactor. Decrease in antibacterial potency by tetracycline degradation is obtained after 10 days. The zone of inhibition is 24 mm at day 1 and 9 mm at day 10
additional information
Bacillus velezensis Al-Dhabi 140
-
usage of a fibrous bed reactor to culture of Bacilllus velezensis strain Al-Dhabi 140 on fibrous matrix to transform tetracycline in synthetic wastewater. The transformed product of tetracycline from the fibrous bed reactor is evident by the activity of ligninolytic enzymes produced by Bacillus velezensis strain Al-Dhabi 140 in reactor. Decrease in antibacterial potency by tetracycline degradation is obtained after 10 days. The zone of inhibition is 24 mm at day 1 and 9 mm at day 10
-
additional information
four MnPs from three MnP 88 subfamilies (extralong, long, and short MnPs) in Ceriporiopsis subvermispora are selected as model proteins for developing a universal method for MnP production, overview
additional information
four MnPs from three MnP 88 subfamilies (extralong, long, and short MnPs) in Ceriporiopsis subvermispora are selected as model proteins for developing a universal method for MnP production, overview
additional information
four MnPs from three MnP 88 subfamilies (extralong, long, and short MnPs) in Ceriporiopsis subvermispora are selected as model proteins for developing a universal method for MnP production, overview
additional information
-
four MnPs from three MnP 88 subfamilies (extralong, long, and short MnPs) in Ceriporiopsis subvermispora are selected as model proteins for developing a universal method for MnP production, overview
-
additional information
both wild-type Il-MnP1 and the variants exhibit negligible activity on veratryl alcohol oxidation in the absence of Mn2+
additional information
-
both wild-type Il-MnP1 and the variants exhibit negligible activity on veratryl alcohol oxidation in the absence of Mn2+
additional information
-
both wild-type Il-MnP1 and the variants exhibit negligible activity on veratryl alcohol oxidation in the absence of Mn2+
-
additional information
-
both wild-type Il-MnP1 and the variants exhibit negligible activity on veratryl alcohol oxidation in the absence of Mn2+
-
additional information
-
MnP production from NITW715076_2, NITW715076_1, and NITW715076 isolates
additional information
to extend the substrate spectrum of MrMnP1, catalytic tryptophan 172 is introduced at the enzyme surface. Properties of Moniliophthora roreri MrMnP1 manganese peroxidase enzyme are shifted towards those of a versatile peroxidase, comparison with the versatile peroxidase from Pleurotus eryngii (UniProt ID Q9UR19). The resulting mutants demonstrate additional activities towards high-redox-potential substrates, such as lignin dimers, veratryl alcohol, and the azo dye Reactive Black 5. The phenolic and non-phenolic lignin dimers guaiacylglycerol-beta-guaiacyl ether (Ge) and veratrylglycerol-beta-guaiacyl ether (Ve) are tested as substrates at pH 3.0-5.0. The phenolic lignin dimer Ge is barely oxidized by the wild-type enzyme (2% conversion), but after introduction of the A172W mutation around 33% can be degraded at pH 3.0 and pH 4.0, and around 15% at pH 5.0. All additional mutations (except for A269R) further increased the activity towards guaiacylglycerol-beta-guaiacyl ether at pH 3.0 and pH 4.0, with the A172W/K168V mutant showing the highest conversion of up to 56% at pH 3.0. The more recalcitrant non-phenolic lignin dimer veratrylglycerol-beta-guaiacyl ether is oxidized only by the mutants, but not by the wild-type enzyme. The activity of the mutants is more similar to the substrate specificity of EC 1.11.1.14. The wild-type enzyme and the mutants are active with dyes: crystal violet, methyl orange, alizarin red S, Indigo carmine, and remazol brilliant blue R, except for the poor activity of the wild-type enzyme with alizarin red S, overview. The mutants showed similar tendencies, decolorization at pH 3.0 is stronger than that with wild-type enzyme
additional information
-
to extend the substrate spectrum of MrMnP1, catalytic tryptophan 172 is introduced at the enzyme surface. Properties of Moniliophthora roreri MrMnP1 manganese peroxidase enzyme are shifted towards those of a versatile peroxidase, comparison with the versatile peroxidase from Pleurotus eryngii (UniProt ID Q9UR19). The resulting mutants demonstrate additional activities towards high-redox-potential substrates, such as lignin dimers, veratryl alcohol, and the azo dye Reactive Black 5. The phenolic and non-phenolic lignin dimers guaiacylglycerol-beta-guaiacyl ether (Ge) and veratrylglycerol-beta-guaiacyl ether (Ve) are tested as substrates at pH 3.0-5.0. The phenolic lignin dimer Ge is barely oxidized by the wild-type enzyme (2% conversion), but after introduction of the A172W mutation around 33% can be degraded at pH 3.0 and pH 4.0, and around 15% at pH 5.0. All additional mutations (except for A269R) further increased the activity towards guaiacylglycerol-beta-guaiacyl ether at pH 3.0 and pH 4.0, with the A172W/K168V mutant showing the highest conversion of up to 56% at pH 3.0. The more recalcitrant non-phenolic lignin dimer veratrylglycerol-beta-guaiacyl ether is oxidized only by the mutants, but not by the wild-type enzyme. The activity of the mutants is more similar to the substrate specificity of EC 1.11.1.14. The wild-type enzyme and the mutants are active with dyes: crystal violet, methyl orange, alizarin red S, Indigo carmine, and remazol brilliant blue R, except for the poor activity of the wild-type enzyme with alizarin red S, overview. The mutants showed similar tendencies, decolorization at pH 3.0 is stronger than that with wild-type enzyme
additional information
-
to extend the substrate spectrum of MrMnP1, catalytic tryptophan 172 is introduced at the enzyme surface. Properties of Moniliophthora roreri MrMnP1 manganese peroxidase enzyme are shifted towards those of a versatile peroxidase, comparison with the versatile peroxidase from Pleurotus eryngii (UniProt ID Q9UR19). The resulting mutants demonstrate additional activities towards high-redox-potential substrates, such as lignin dimers, veratryl alcohol, and the azo dye Reactive Black 5. The phenolic and non-phenolic lignin dimers guaiacylglycerol-beta-guaiacyl ether (Ge) and veratrylglycerol-beta-guaiacyl ether (Ve) are tested as substrates at pH 3.0-5.0. The phenolic lignin dimer Ge is barely oxidized by the wild-type enzyme (2% conversion), but after introduction of the A172W mutation around 33% can be degraded at pH 3.0 and pH 4.0, and around 15% at pH 5.0. All additional mutations (except for A269R) further increased the activity towards guaiacylglycerol-beta-guaiacyl ether at pH 3.0 and pH 4.0, with the A172W/K168V mutant showing the highest conversion of up to 56% at pH 3.0. The more recalcitrant non-phenolic lignin dimer veratrylglycerol-beta-guaiacyl ether is oxidized only by the mutants, but not by the wild-type enzyme. The activity of the mutants is more similar to the substrate specificity of EC 1.11.1.14. The wild-type enzyme and the mutants are active with dyes: crystal violet, methyl orange, alizarin red S, Indigo carmine, and remazol brilliant blue R, except for the poor activity of the wild-type enzyme with alizarin red S, overview. The mutants showed similar tendencies, decolorization at pH 3.0 is stronger than that with wild-type enzyme
-
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biotechnology
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biotechnological applications require large amounts of low-cost enzymes, one of the appropriate approaches for this is to utilize the potential of lignocellulosic wastes, some of which may contain significant concentrations of soluble carbohydrates and inducers of enzyme synthesis, ensuring efficient production of ligninolytic enzymes
biofuel production
-
applications of recombinant enzyme in the pulp and paper industry and in the processing of lignocellulosic materials for ethanol and biofuels production
biofuel production
-
bioethanol production, the enzymes laccase and manganese peroxidase from Klebsiella pneumoniae are employed for ethanol production from rice and wheat bran biomass which shows 39.29% improved production compared to control, evaluation
biofuel production
-
microbial MnPs can convert lignin into biomass so that the sugar can be converted into biofuels
biofuel production
-
microbial MnPs can convert lignin into biomass so that the sugar can be converted into biofuels
biofuel production
-
microbial MnPs can convert lignin into biomass so that the sugar can be converted into biofuels
biofuel production
-
microbial MnPs can convert lignin into biomass so that the sugar can be converted into biofuels
biofuel production
microbial MnPs can convert lignin into biomass so that the sugar can be converted into biofuels
biofuel production
microbial MnPs can convert lignin into biomass so that the sugar can be converted into biofuels
biofuel production
-
microbial MnPs can convert lignin into biomass so that the sugar can be converted into biofuels
biofuel production
-
microbial MnPs can convert lignin into biomass so that the sugar can be converted into biofuels
biofuel production
-
microbial MnPs can convert lignin into biomass so that the sugar can be converted into biofuels
biofuel production
microbial MnPs can convert lignin into biomass so that the sugar can be converted into biofuels
biofuel production
microbial MnPs can convert lignin into biomass so that the sugar can be converted into biofuels
biofuel production
microbial MnPs can convert lignin into biomass so that the sugar can be converted into biofuels
biofuel production
microbial MnPs can convert lignin into biomass so that the sugar can be converted into biofuels
biofuel production
-
microbial MnPs can convert lignin into biomass so that the sugar can be converted into biofuels
biofuel production
-
microbial MnPs can convert lignin into biomass so that the sugar can be converted into biofuels
-
biofuel production
-
microbial MnPs can convert lignin into biomass so that the sugar can be converted into biofuels
-
biofuel production
-
microbial MnPs can convert lignin into biomass so that the sugar can be converted into biofuels
-
biofuel production
-
microbial MnPs can convert lignin into biomass so that the sugar can be converted into biofuels
-
biofuel production
-
microbial MnPs can convert lignin into biomass so that the sugar can be converted into biofuels
-
biofuel production
-
microbial MnPs can convert lignin into biomass so that the sugar can be converted into biofuels
-
degradation
-
biomimmetic decrosslinking with enzyme or metal complex-catalyzed reactions will enable the development of new devulcanizing strategies for the safe disposal and recycling of waste vulcanized rubber products
degradation
lingnin-degrading enzymes possess oxidative activity against phenolic compoundss, which can be used for bioremediation, biobleaching, and biofuel production
degradation
Mn peroxidases are of much interest biotechnologically because of their potentially applications in bioremdeial waste treatment and in catalyzing difficult chemical transfromations
degradation
-
various aspects of the biotechnological uses of these fungi have been studied regarding the nonspecific ligninolytic system of white-red fungi such as the degradation of industrial textile dye effluents and various xenobiotics
degradation
-
enzyme is able to detoxify aflatoxin B1. Maximum elimination of 86.0% of aflatoxin B1 is observed after 48 h in a reaction mixture containing 5 nkat of enzyme, and the addition of Tween 80 enhances elimination. The treatment of aflatoxin B1 by 20 nkat MnP reduces the mutagenic activity by 69.2%. Analysis suggests that aflatoxin B1 is first oxidized to aflatoxin B1-8,9-epoxide and then hydrolyzed to aflatoxin B1-8,9-dihydrodiol
degradation
-
crude enzyme is able to degrade the antibiotics tetracycline and oxytetracycline. 72.5% of 50 mg/l of tetracycline and 84.3% of 50 mg/l oxytetracycline is degraded by 40 U/l of amnganese peroxidase, within 4 h. With the pH at 3.0-4.8, the temperature at 37-40°C, the Mn2+ concentration between 0.1 and 0.4 mM, the H2O2 concentration of 0.2 mM, and the enzyme-substrate ratio above 2.0 U/mg, the degradation rate reaches the highest
degradation
-
fibrous bed culture of Bacillus velezensis strain Al-Dhabi 140 might be an efficient strain for tetracycline removal from artificial wastewater, even from natural wastewater
degradation
Bacillus velezensis Al-Dhabi 140
-
fibrous bed culture of Bacillus velezensis strain Al-Dhabi 140 might be an efficient strain for tetracycline removal from artificial wastewater, even from natural wastewater
-
degradation
-
crude enzyme is able to degrade the antibiotics tetracycline and oxytetracycline. 72.5% of 50 mg/l of tetracycline and 84.3% of 50 mg/l oxytetracycline is degraded by 40 U/l of amnganese peroxidase, within 4 h. With the pH at 3.0-4.8, the temperature at 37-40°C, the Mn2+ concentration between 0.1 and 0.4 mM, the H2O2 concentration of 0.2 mM, and the enzyme-substrate ratio above 2.0 U/mg, the degradation rate reaches the highest
-
degradation
-
enzyme is able to detoxify aflatoxin B1. Maximum elimination of 86.0% of aflatoxin B1 is observed after 48 h in a reaction mixture containing 5 nkat of enzyme, and the addition of Tween 80 enhances elimination. The treatment of aflatoxin B1 by 20 nkat MnP reduces the mutagenic activity by 69.2%. Analysis suggests that aflatoxin B1 is first oxidized to aflatoxin B1-8,9-epoxide and then hydrolyzed to aflatoxin B1-8,9-dihydrodiol
-
degradation
-
lingnin-degrading enzymes possess oxidative activity against phenolic compoundss, which can be used for bioremediation, biobleaching, and biofuel production
-
environmental protection
-
-
environmental protection
-
thiol-mediated degradation of dimeric model compounds and of polymeric lignin by MnP has potential applications in the degradation of industrial lignins
environmental protection
-
key enzyme for degradation of environmentally persistent xenobiotics such as pentachlorophenol and dioxins
environmental protection
Deuteromycotina sp.
-
degradation of recalcitrant high-molecular-mass compounds, such as nylon and melanin, degradation of xenobiotic compounds, bioremediation, decolorization of wastewater
environmental protection
-
polycyclic aromatic hydrocarbon degradation
environmental protection
-
mediated system of degradation is potentially valuable for degradation of synthetic polymers and of environmental pollutants
environmental protection
mediated system of degradation is potentially valuable for degradation of synthetic polymers and of environmental pollutants
environmental protection
-
degradation of recalcitrant pollutants
environmental protection
as to denim bleaching, sodium hypochlorite treatment is primarily used and this gives rise to problems such as chemical injuries, denim yellowness and reduced denim strength. To ensure the low-cost and ecofriendly advantages, denim biobleaching using oxidizing enzymes such as manganese peroxidases (MnPs) and laccases is an ideal alternative. In the presence of MnPs, denim bleaching by laccases is greatly enhanced. Usage of recombinant white-rot fungi MnP in denim bleaching and PAH degradation
environmental protection
-
fibrous bed culture of Bacillus velezensis strain Al-Dhabi 140 might be an efficient strain for tetracycline removal from artificial wastewater, even from natural wastewater
environmental protection
-
manganese peroxidases have a potential for degradation of many xenobiotic compounds and produce polymeric products formulated them into valuable tools for bioremediation purposes
environmental protection
-
manganese peroxidases have a potential for degradation of many xenobiotic compounds and produce polymeric products formulated them into valuable tools for bioremediation purposes
environmental protection
-
manganese peroxidases have a potential for degradation of many xenobiotic compounds and produce polymeric products formulated them into valuable tools for bioremediation purposes
environmental protection
-
manganese peroxidases have a potential for degradation of many xenobiotic compounds and produce polymeric products formulated them into valuable tools for bioremediation purposes
environmental protection
manganese peroxidases have a potential for degradation of many xenobiotic compounds and produce polymeric products formulated them into valuable tools for bioremediation purposes
environmental protection
manganese peroxidases have a potential for degradation of many xenobiotic compounds and produce polymeric products formulated them into valuable tools for bioremediation purposes
environmental protection
-
manganese peroxidases have a potential for degradation of many xenobiotic compounds and produce polymeric products formulated them into valuable tools for bioremediation purposes
environmental protection
-
manganese peroxidases have a potential for degradation of many xenobiotic compounds and produce polymeric products formulated them into valuable tools for bioremediation purposes
environmental protection
-
manganese peroxidases have a potential for degradation of many xenobiotic compounds and produce polymeric products formulated them into valuable tools for bioremediation purposes
environmental protection
manganese peroxidases have a potential for degradation of many xenobiotic compounds and produce polymeric products formulated them into valuable tools for bioremediation purposes
environmental protection
manganese peroxidases have a potential for degradation of many xenobiotic compounds and produce polymeric products formulated them into valuable tools for bioremediation purposes
environmental protection
manganese peroxidases have a potential for degradation of many xenobiotic compounds and produce polymeric products formulated them into valuable tools for bioremediation purposes
environmental protection
manganese peroxidases have a potential for degradation of many xenobiotic compounds and produce polymeric products formulated them into valuable tools for bioremediation purposes
environmental protection
-
manganese peroxidases have a potential for degradation of many xenobiotic compounds and produce polymeric products formulated them into valuable tools for bioremediation purposes
environmental protection
-
the enzyme can degrade sulfamethoxazole (SMX), a broad-spectrum antibiotic (one non-phenolic compound) that has been widely used as a growth promoter in the breeding industry. SMX has been widely detected in effluents, soils, and surface waters in China. SMX is a persistent and polar organic compound in effluent with a half-life time of 17.8 days. More seriously, the SMX in aquatic environments may accelerate the spread of sul genes (antibiotic resistance genes (ARGs)) in microbial populations, and this would have detrimental effects on the ecosystem balance
environmental protection
-
manganese peroxidases have a potential for degradation of many xenobiotic compounds and produce polymeric products formulated them into valuable tools for bioremediation purposes
-
environmental protection
Bacillus velezensis Al-Dhabi 140
-
fibrous bed culture of Bacillus velezensis strain Al-Dhabi 140 might be an efficient strain for tetracycline removal from artificial wastewater, even from natural wastewater
-
environmental protection
-
manganese peroxidases have a potential for degradation of many xenobiotic compounds and produce polymeric products formulated them into valuable tools for bioremediation purposes
-
environmental protection
-
manganese peroxidases have a potential for degradation of many xenobiotic compounds and produce polymeric products formulated them into valuable tools for bioremediation purposes
-
environmental protection
-
manganese peroxidases have a potential for degradation of many xenobiotic compounds and produce polymeric products formulated them into valuable tools for bioremediation purposes
-
environmental protection
-
thiol-mediated degradation of dimeric model compounds and of polymeric lignin by MnP has potential applications in the degradation of industrial lignins
-
environmental protection
-
manganese peroxidases have a potential for degradation of many xenobiotic compounds and produce polymeric products formulated them into valuable tools for bioremediation purposes
-
environmental protection
-
polycyclic aromatic hydrocarbon degradation
-
environmental protection
-
the enzyme can degrade sulfamethoxazole (SMX), a broad-spectrum antibiotic (one non-phenolic compound) that has been widely used as a growth promoter in the breeding industry. SMX has been widely detected in effluents, soils, and surface waters in China. SMX is a persistent and polar organic compound in effluent with a half-life time of 17.8 days. More seriously, the SMX in aquatic environments may accelerate the spread of sul genes (antibiotic resistance genes (ARGs)) in microbial populations, and this would have detrimental effects on the ecosystem balance
-
environmental protection
-
mediated system of degradation is potentially valuable for degradation of synthetic polymers and of environmental pollutants
-
environmental protection
-
-
-
environmental protection
-
as to denim bleaching, sodium hypochlorite treatment is primarily used and this gives rise to problems such as chemical injuries, denim yellowness and reduced denim strength. To ensure the low-cost and ecofriendly advantages, denim biobleaching using oxidizing enzymes such as manganese peroxidases (MnPs) and laccases is an ideal alternative. In the presence of MnPs, denim bleaching by laccases is greatly enhanced. Usage of recombinant white-rot fungi MnP in denim bleaching and PAH degradation
-
environmental protection
-
manganese peroxidases have a potential for degradation of many xenobiotic compounds and produce polymeric products formulated them into valuable tools for bioremediation purposes
-
environmental protection
-
degradation of recalcitrant pollutants
-
environmental protection
-
the enzyme can degrade sulfamethoxazole (SMX), a broad-spectrum antibiotic (one non-phenolic compound) that has been widely used as a growth promoter in the breeding industry. SMX has been widely detected in effluents, soils, and surface waters in China. SMX is a persistent and polar organic compound in effluent with a half-life time of 17.8 days. More seriously, the SMX in aquatic environments may accelerate the spread of sul genes (antibiotic resistance genes (ARGs)) in microbial populations, and this would have detrimental effects on the ecosystem balance
-
industry
-
the ligninolytic enzymes of Basidiomycete are of fundamental importance for the efficient bioconversion of plant residues and they are prospective for the various biotechnological applications in pulp and paper, food, textile and dye industries, bioremediation, cosmetics, analytic biochemistry, and many others
industry
-
the ligninolytic enzymes of Basidiomycete are of fundamental importance for the efficient bioconversion of plant residues and they are prospective for the various biotechnological applications in pulp and paper, food, textile and dye industries, bioremediation, cosmetics, analytic biochemistry, and many others
industry
-
the ligninolytic enzymes of Basidiomycete are of fundamental importance for the efficient bioconversion of plant residues and they are prospective for the various biotechnological applications in pulp and paper, food, textile and dye industries, bioremediation, cosmetics, analytic biochemistry, and many others
industry
-
the ligninolytic enzymes of Basidiomycete are of fundamental importance for the efficient bioconversion of plant residues and they are prospective for the various biotechnological applications in pulp and paper, food, textile and dye industries, bioremediation, cosmetics, analytic biochemistry, and many others
industry
-
the ligninolytic enzymes of Basidiomycete are of fundamental importance for the efficient bioconversion of plant residues and they are prospective for the various biotechnological applications in pulp and paper, food, textile and dye industries, bioremediation, cosmetics, analytic biochemistry, and many others
industry
-
the ligninolytic enzymes of Basidiomycete are of fundamental importance for the efficient bioconversion of plant residues and they are prospective for the various biotechnological applications in pulp and paper, food, textile and dye industries, bioremediation, cosmetics, analytic biochemistry, and many others
industry
-
the ligninolytic enzymes of Basidiomycete are of fundamental importance for the efficient bioconversion of plant residues and they are prospective for the various biotechnological applications in pulp and paper, food, textile and dye industries, bioremediation, cosmetics, analytic biochemistry, and many others
industry
-
the ligninolytic enzymes of Basidiomycete are of fundamental importance for the efficient bioconversion of plant residues and they are prospective for the various biotechnological applications in pulp and paper, food, textile and dye industries, bioremediation, cosmetics, analytic biochemistry, and many others
industry
-
the ligninolytic enzymes of Basidiomycete are of fundamental importance for the efficient bioconversion of plant residues and they are prospective for the various biotechnological applications in pulp and paper, food, textile and dye industries, bioremediation, cosmetics, analytic biochemistry, and many others
nutrition
-
biotechnological applications related to animal feeding
nutrition
-
biotechnological applications related to animal feeding
nutrition
-
biotechnological applications related to animal feeding
-
paper production
-
-
paper production
Deuteromycotina sp.
-
biobleaching of kraft pulp
paper production
-
preferential degradation of lignin in wheat straw, an important property for biotechnological applications related to pulp and paper industry
paper production
-
preferential degradation of lignin in wheat straw, an important property for biotechnological applications related to pulp and paper industry
paper production
-
bleaching of paper pulp
paper production
-
bleaching of paper pulp
paper production
-
mediated system of degradation is potentially valuable for pulp and paper industries
paper production
mediated system of degradation is potentially valuable for pulp and paper industries
paper production
-
applications of recombinant enzyme in the pulp and paper industry and in the processing of lignocellulosic materials for ethanol and biofuels production
paper production
-
manganese peroxidase produced by the white-rot fungus Bjerkandera sp. strain BOS55 is used for lignin oxidation and bleaching of eucalyptus oxygen delignified kraft pulp
paper production
-
manganese peroxidase produced by the white-rot fungus Bjerkandera sp. strain BOS55 is used for lignin oxidation and bleaching of eucalyptus oxygen delignified kraft pulp
-
paper production
-
bleaching of paper pulp
-
paper production
-
preferential degradation of lignin in wheat straw, an important property for biotechnological applications related to pulp and paper industry
-
paper production
-
mediated system of degradation is potentially valuable for pulp and paper industries
-
paper production
-
bleaching of paper pulp
-
synthesis
-
expression of active manganese peroxidase in an Escherichia coli cell-free protein synthesis system, and optimization of reaction conditions such as the concentrations of hemin, calcium ions, and disulfide bond isomerase. Cell-free synthesized manganese peroxidase purified using the hemagglutinin tag shows higher specific activity than the commercial wild-type enzyme
synthesis
-
the enzymes laccase and manganese peroxidase from Klebsiella pneumoniae are employed for ethanol production from rice and wheat bran biomass which shows 39.29% improved production compared to control, evaluation
additional information
maganese peroxidase (MnP) has a great application potential and ample opportunities in diverse area, such as alcohol, pulp and paper, biofuel, agriculture, cosmetic, textile, and food industries detailed overview
additional information
-
maganese peroxidase (MnP) has a great application potential and ample opportunities in diverse area, such as alcohol, pulp and paper, biofuel, agriculture, cosmetic, textile, and food industries, detailed overview
additional information
-
maganese peroxidase (MnP) has a great application potential and ample opportunities in diverse area, such as alcohol, pulp and paper, biofuel, agriculture, cosmetic, textile, and food industries, detailed overview
additional information
-
maganese peroxidase (MnP) has a great application potential and ample opportunities in diverse area, such as alcohol, pulp and paper, biofuel, agriculture, cosmetic, textile, and food industries, detailed overview
additional information
-
maganese peroxidase (MnP) has a great application potential and ample opportunities in diverse area, such as alcohol, pulp and paper, biofuel, agriculture, cosmetic, textile, and food industries, detailed overview
additional information
maganese peroxidase (MnP) has a great application potential and ample opportunities in diverse area, such as alcohol, pulp and paper, biofuel, agriculture, cosmetic, textile, and food industries, detailed overview
additional information
maganese peroxidase (MnP) has a great application potential and ample opportunities in diverse area, such as alcohol, pulp and paper, biofuel, agriculture, cosmetic, textile, and food industries, detailed overview
additional information
-
maganese peroxidase (MnP) has a great application potential and ample opportunities in diverse area, such as alcohol, pulp and paper, biofuel, agriculture, cosmetic, textile, and food industries, detailed overview
additional information
maganese peroxidase (MnP) has a great application potential and ample opportunities in diverse area, such as alcohol, pulp and paper, biofuel, agriculture, cosmetic, textile, and food industries, detailed overview
additional information
-
maganese peroxidase (MnP) has a great application potential and ample opportunities in diverse area, such as alcohol, pulp and paper, biofuel, agriculture, cosmetic, textile, and food industries, detailed overview
additional information
-
maganese peroxidase (MnP) has a great application potential and ample opportunities in diverse area, such as alcohol, pulp and paper, biofuel, agriculture, cosmetic, textile, and food industries, detailed overview
additional information
-
maganese peroxidase (MnP) has a great application potential and ample opportunities in diverse area, such as alcohol, pulp and paper, biofuel, agriculture, cosmetic, textile, and food industries, detailed overview
additional information
maganese peroxidase (MnP) has a great application potential and ample opportunities in diverse area, such as alcohol, pulp and paper, biofuel, agriculture, cosmetic, textile, and food industries, detailed overview
additional information
maganese peroxidase (MnP) has a great application potential and ample opportunities in diverse area, such as alcohol, pulp and paper, biofuel, agriculture, cosmetic, textile, and food industries, detailed overview
additional information
maganese peroxidase (MnP) has a great application potential and ample opportunities in diverse area, such as alcohol, pulp and paper, biofuel, agriculture, cosmetic, textile, and food industries, detailed overview
additional information
-
maganese peroxidase (MnP) has a great application potential and ample opportunities in diverse area, such as alcohol, pulp and paper, biofuel, agriculture, cosmetic, textile, and food industries, detailed overview
additional information
-
maganese peroxidase (MnP) has a great application potential and ample opportunities in diverse area, such as alcohol, pulp and paper, biofuel,agriculture, cosmetic, textile, and food industries, detailed overview
additional information
the recombinant isotzyme MnP3 from Cerrena unicolor strain BBP6, rMnP3-BBP6, has promising biotechnological application potential in textile industries and polycyclic aromatic hydrocarbon bioremediation
additional information
-
maganese peroxidase (MnP) has a great application potential and ample opportunities in diverse area, such as alcohol, pulp and paper, biofuel, agriculture, cosmetic, textile, and food industries, detailed overview
-
additional information
-
maganese peroxidase (MnP) has a great application potential and ample opportunities in diverse area, such as alcohol, pulp and paper, biofuel, agriculture, cosmetic, textile, and food industries, detailed overview
-
additional information
-
maganese peroxidase (MnP) has a great application potential and ample opportunities in diverse area, such as alcohol, pulp and paper, biofuel, agriculture, cosmetic, textile, and food industries, detailed overview
-
additional information
-
maganese peroxidase (MnP) has a great application potential and ample opportunities in diverse area, such as alcohol, pulp and paper, biofuel, agriculture, cosmetic, textile, and food industries, detailed overview
-
additional information
-
maganese peroxidase (MnP) has a great application potential and ample opportunities in diverse area, such as alcohol, pulp and paper, biofuel, agriculture, cosmetic, textile, and food industries, detailed overview
-
additional information
-
the recombinant isotzyme MnP3 from Cerrena unicolor strain BBP6, rMnP3-BBP6, has promising biotechnological application potential in textile industries and polycyclic aromatic hydrocarbon bioremediation
-
additional information
-
maganese peroxidase (MnP) has a great application potential and ample opportunities in diverse area, such as alcohol, pulp and paper, biofuel, agriculture, cosmetic, textile, and food industries, detailed overview
-
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brenda
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4268-4277
1997
Phanerodontia chrysosporium, Phanerodontia chrysosporium OGC101
brenda
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Engineering a disulfide bond in recombinant manganese peroxidase results in increased thermostability
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2000
Phanerodontia chrysosporium
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2000
Phanerodontia chrysosporium, Phanerodontia chrysosporium OGC101
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69
3957-3964
2003
Stropharia coronilla
brenda
Kamitsuji, H.; Honda, Y.; Watanabe, T.; Kuwahara, M.
Production and induction of manganese peroxidase isozymes in a white-rot fungus Pleurotus ostreatus
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65
287-294
2004
Pleurotus ostreatus
brenda
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Direct oxidation of polymeric substrates by multifunctional manganese peroxidase isoenzyme from Pleurotus ostreatus without redox mediators
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386
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2005
Pleurotus ostreatus
brenda
Sundaramoorthy, M.; Youngs, H.L.; Gold, M.H.; Poulos, T.L.
High-resolution crystal structure of manganese peroxidase: substrate and inhibitor complexes
Biochemistry
44
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2005
Phanerodontia chrysosporium (Q02567)
brenda
Lisov, A.V.; Leontievsky, A.A.; Golovleva, L.A.
Hybrid Mn-peroxidase from the ligninolytic fungus Panus tigrinus 8/18. Isolation, substrate specificity, and catalytic cycle
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2003
Lentinus tigrinus, Lentinus tigrinus 8/18
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NADH oxidation by manganese peroxidase with or without alpha-hydroxy acid
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2002
Pleurotus ostreatus
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Expression of a Phanerochaete chrysosporium manganese peroxidase gene in the yeast Pichia pastoris
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19
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2003
Phanerodontia chrysosporium
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35
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2004
Trichophyton rubrum, Trichophyton rubrum LSK-27
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Thermally stable and hydrogen peroxide tolerant manganese peroxidase (MnP) from Lenzites betulinus
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249-252
2002
Lenzites betulinus
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Decolorization of sulfonphthalein dyes by manganese peroxidase activity of the white-rot fungus Phanerochaete chrysosporium
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48
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2003
Phanerodontia chrysosporium
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Separation of manganese peroxidase isoenzymes on strong anion-exchange monolithic column using pH-salt gradient
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343-347
2004
Phanerodontia chrysosporium, Phanerodontia chrysosporium MZKI B-223
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Purification and partial characterization of manganese peroxidase from immobilized Phanerochaete chrysosporium
Proc. Biochem.
39
2061-2068
2004
Phanerodontia chrysosporium
-
brenda
de la Rubia, T.; Linares, A.; Perez, J.; Munoz-Dorado, J.; Romera, J.; Martinez, J.
Characterization of manganese-dependent peroxidase isoenzymes from the ligninolytic fungus Phanerochaete flavido-alba
Res. Microbiol.
153
547-554
2002
Phanerochaete flavidoalba
brenda
Jiang, F.; Kongsaeree, P.; Schilke, K.; Lajoie, C.; Kelly, C.
Effects of pH and temperature on recombinant manganese peroxidase production and stability
Appl. Biochem. Biotechnol.
146
15-27
2008
Phanerodontia chrysosporium
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Jiang, F.; Kongsaeree, P.; Charron, R.; Lajoie, C.; Xu, H.; Scott, G.; Kelly, C.
Production and separation of manganese peroxidase from heme amended yeast cultures
Biotechnol. Bioeng.
99
540-549
2008
Phanerodontia chrysosporium
brenda
Kwon, H.; Chung, E.; Oh, J.; Lee, C.; Ahn, I.
Optimized production of lignolytic manganese peroxidase in immobilized cultures of Phanerochaete chrysosporium
Biotechnol. Bioprocess Eng.
13
108-114
2008
Phanerodontia chrysosporium
-
brenda
Hwang, S.; Lee, C.H.; Ahn, I.S.; Park, K.
Manganese peroxidase-catalyzed oxidative degradation of vanillylacetone
Chemosphere
72
572-577
2008
Phanerodontia chrysosporium, Phanerodontia chrysosporium BKM-F-1767
brenda
Cheng, X.; Jia, R.; Li, P.; Tu, S.; Zhu, Q.; Tang, W.; Li, X.
Purification of a new manganese peroxidase of the white-rot fungus Schizophyllum sp. F17, and decolorization of azo dyes by the enzyme
Enzyme Microb. Technol.
41
258-264
2007
Schizophyllum sp., Schizophyllum sp. F17
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brenda
Songulashvili, G.; Elisashvili, V.; Wasser, S.P.; Nevo, E.; Hadar, Y.
Basidiomycetes laccase and manganese peroxidase activity in submerged fermentation of food industry wastes
Enzyme Microb. Technol.
41
57-61
2007
Trametes maxima, Trametes versicolor, Fomes fomentarius, Ganoderma lucidum, Phlebia radiata, Coriolopsis trogii, Ganoderma adspersum, Phellinus robustus, Trametes zonata, Omphalotus olearius, Phellinus robustus 250, Omphalotus olearius 174, Ganoderma adspersum 845, Phlebia radiata 511, Ganoderma lucidum 447, Trametes maxima 681, Coriolopsis trogii 146, Trametes zonata 540
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brenda
Feijoo, G.; Moreira, M.T.; Alvarez, P.; Lu-Chau, T.A.; Lema, J.M.
Evaluation of the enzyme manganese peroxidase in an industrial sequence for the lignin oxidation and bleaching of eucalyptus kraft pulp
J. Appl. Polym. Sci.
109
1319-1327
2008
Bjerkandera sp., Bjerkandera sp. BOS55
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Yeo, S.; Park, N.; Song, H.; Choi, H.T.
Generation of a transformant showing higher manganese peroxidase (Mnp) activity by overexpression of Mnp gene in Trametes versicolor
J. Microbiol.
45
213-218
2007
Trametes versicolor (Q6KB19), Trametes versicolor
brenda
Hilden, K.S.; Bortfeldt, R.; Hofrichter, M.; Hatakka, A.; Lundell, T.K.
Molecular characterization of the basidiomycete isolate Nematoloma frowardii b19 and its manganese peroxidase places the fungus in the corticioid genus Phlebia
Microbiology
154
2371-2379
2008
Hypholoma frowardii (B2BF37), Hypholoma frowardii (B2BF38), Hypholoma frowardii, Hypholoma frowardii b19 (B2BF37)
brenda
Catal, T.; Liu, H.; Bermek, H.
Selenium induces manganese-dependent peroxidase production by the white-rot fungus Bjerkandera adusta (Willdenow) P. Karsten
Biol. Trace Elem. Res.
123
211-217
2008
Bjerkandera adusta
brenda
Silva, E.; Martins, S.; Milagres, A.
Extraction of manganese peroxidase produced by Lentinula edodes
Biores. Technol.
99
2471-2475
2008
Lentinula edodes
brenda
Sato, S.; Ohashi, Y.; Kojima, M.; Watanabe, T.; Honda, Y.; Watanabe, T.
Degradation of sulfide linkages between isoprenes by lipid peroxidation catalyzed by manganese peroxidase
Chemosphere
77
798-804
2009
Gelatoporia subvermispora
brenda
Erdem, E.; Ucar, M.; Kaymaz, Y.; Pazarlioglu, N.
New and different lignocellulosic materials from Turkey for laccase and manganese peroxidase production by Trametes versicolor
Eng. Life Sci.
9
60-65
2009
Trametes versicolor
-
brenda
Susla, M.; Novotny, C.; Erbanova, P.; Svobodova, K.
Implication of Dichomitus squalens manganese-dependent peroxidase in dye decolorization and cooperation of the enzyme with laccase
Folia Microbiol. (Praha)
53
479-485
2008
Dichomitus squalens
brenda
Alvarez, J.M.; Canessa, P.; Mancilla, R.A.; Polanco, R.; Santibanez, P.A.; Vicuna, R.
Expression of genes encoding laccase and manganese-dependent peroxidase in the fungus Ceriporiopsis subvermispora is mediated by an ACE1-like copper-fist transcription factor
Fungal Genet. Biol.
46
104-111
2009
Gelatoporia subvermispora, Gelatoporia subvermispora FP-105752
brenda
Kenkebashvili, N.; Elisashvili, V.; Hadar, Y.
Effect of nutrient medium composition on laccase and manganese peroxidase activity in medicinal mushrooms
Int. J. Med. Mushr.
11
191-198
2009
Basidiomycota, Trametes ochracea, Trichaptum biforme, Trichaptum biforme 117, Trametes ochracea 1215
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brenda
Petruccioli, M.; Frasconi, M.; Quaratino, D.; Covino, S.; Favero, G.; Mazzei, F.; Federici, F.; DAnnibale, A.
Kinetic and redox properties of MnP II, a major manganese peroxidase isoenzyme from Panus tigrinus CBS 577.79
J. Biol. Inorg. Chem.
14
1153-1163
2009
Lentinus tigrinus, Lentinus tigrinus CBS 577.79, Lentinus tigrinus 577.79
brenda
Zhang, X.; Wang, Y.; Wang, L.; Chen, G.; Liu, W.; Gao, P.
Site-directed mutagenesis of manganese peroxidase from Phanerochaete chrysosporium in an in vitro expression system
J. Biotechnol.
139
176-178
2009
Phanerodontia chrysosporium (Q02567), Phanerodontia chrysosporium
brenda
Elisashvili, V.; Kachlishvili, E.
Physiological regulation of laccase and manganese peroxidase production by white-rot Basidiomycetes
J. Biotechnol.
144
37-42
2009
Basidiomycota, Bjerkandera adusta, Cerrena unicolor, Fomes fomentarius, Trametes maxima, Trametes ochracea, Trametes pubescens, Trametes versicolor, Trichaptum biforme
brenda
Sakamoto, Y.; Nakade, K.; Nagai, M.; Uchimiya, H.; Sato, T.
Cloning of Lentinula edodes lemnp2, a manganese peroxidase that is secreted abundantly in sawdust medium
Mycoscience
50
116-122
2009
Lentinula edodes (B5U990), Lentinula edodes SR-1 (B5U990)
brenda
Erden, E.; Cigdem Ucar, M.; Gezer, T.; Pazarlioglu, N.
Screening for ligninolytic enzymes from autochthonous fungi and applications for decolorization of Remazole Marine Blue
Braz. J. Microbiol.
40
346-353
2009
Abortiporus biennis, Abortiporus biennis ECN 100601, Agaricus sp., Agrocybe sp. 1, Agrocybe sp. 2, Clitocybe sp., Coprinopsis atramentaria, Cortinarius sp. 1, Cortinarius sp. 2, Cortinarius sp. 2 ECN 100602, Cyclocybe aegerita, Ganoderma carnosum, Ganoderma carnosum ECN 100603, Inocybe lacera, Inocybe longicystis, Lactarius deliciosus, Lactarius deliciosus ECN 100604, Lepiota naucina, Lepiota sp. 1, Lepiota sp. 2, Lepista nuda, Lepista nuda ECN 100605, Leptonia lazunila, Lyophyllum subglobisporium, Lyophyllum subglobisporium ECN 100606, Parasola plicatilis, Pleurotus ostreatus, Pleurotus ostreatus ECN 100607, Ramaria stricta, Ramaria stricta ECN 100608, Rhizopogon luteolus, Russula rosacea, Russula sp., Trametes hirsuta, Trametes versicolor, Trametes versicolor ECN 100609, Volvariella sp.
brenda
Ruiz-Duenas, F.J.; Morales, M.; Garcia, E.; Miki, Y.; Martinez, M.J.; Martinez, A.T.
Substrate oxidation sites in versatile peroxidase and other basidiomycete peroxidases
J. Exp. Bot.
60
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2009
Phanerodontia chrysosporium (Q02567)
brenda
Hu, M.; Zhang, W.; Wu, Y.; Gao, P.; Lu, X.
Characteristics and function of a low-molecular-weight compound with reductive activity from Phanerochaete chrysosporium in lignin biodegradation
Biores. Technol.
100
2077-2081
2009
Phanerodontia chrysosporium
brenda
Lupo, S.; Perez, A.; Martinez, S.; Simeto, S.; Rivas, F.; Bettucci, L.
In vitro characterization of Inocutis jamaicensis and experimental inoculation of Eucalyptus globulus standing trees
Forest Pathol.
39
293-303
2009
Inocutis jamaicensis, Inocutis jamaicensis MVHC11379
brenda
Vassilev, N.; Requena, A.; Nieto, L.; Nikolaeva, I.; Vassileva, M.
Production of manganese peroxidase by Phanerochaete chrisosporium grown on medium containing agro-wastes/rock phosphate and biocontrol properties of the final product
Ind. Crops Prod.
30
28-32
2009
Phanerodontia chrysosporium
brenda
Wang, J.; Ogata, M.; Hirai, H.; Kawagishi, H.
Detoxification of aflatoxin B1 by manganese peroxidase from the white-rot fungus Phanerochaete sordida YK-624
FEMS Microbiol. Lett.
314
164-169
2011
Phanerochaete sordida, Phanerochaete sordida YK-624
brenda
Yadav, P.; Singh, V.K.; Yadav, M.; Singh, S.K.; Yadava, S.; Yadav, K.D.
Purification and characterization of Mn-peroxidase from Musa paradisiaca (banana) stem juice
Indian J. Biochem. Biophys.
49
42-48
2012
Musa x paradisiaca
brenda
Asgher, M.; Irshad, M.; Iqbal, H.
Purification and characterization of novel manganese peroxidase from Schizophyllum commune IBL-06
Int. J. Agric. Biol.
15
749-754
2013
Schizophyllum commune, Schizophyllum commune IBL-06
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brenda
Fernandez-Fueyo, E.; Ruiz-Duenas, F.J.; Martinez, A.T.
Engineering a fungal peroxidase that degrades lignin at very acidic pH
Biotechnol. Biofuels
7
114
2014
Gelatoporia subvermispora (M2REM6), Gelatoporia subvermispora B (M2REM6)
brenda
Ninomiya, R.; Zhu, B.; Kojima, T.; Iwasaki, Y.; Nakano, H.
Role of disulfide bond isomerase DsbC, calcium ions, and hemin in cell-free protein synthesis of active manganese peroxidase isolated from Phanerochaete chrysosporium
J. Biosci. Bioeng.
117
652-657
2014
Phanerodontia chrysosporium
brenda
Wen, X.; Jia, Y.; Li, J.
Enzymatic degradation of tetracycline and oxytetracycline by crude manganese peroxidase prepared from Phanerochaete chrysosporium
J. Hazard. Mater.
177
924-928
2010
Phanerodontia chrysosporium, Phanerodontia chrysosporium BKM-F-1767
brenda
Thamvithayakorn, P.; Phosri, C.; Pisutpaisal, N.; Krajangsang, S.; Whalley, A.J.S.; Suwannasai, N.
Utilization of oil palm decanter cake for valuable laccase and manganese peroxidase enzyme production from a novel white-rot fungus, Pseudolagarobasidium sp. PP17-33
3 Biotech
9
417
2019
Pseudolagarobasidium sp. PP17-33
brenda
Duan, Z.; Shen, R.; Liu, B.; Yao, M.; Jia, R.
Comprehensive investigation of a dye-decolorizing peroxidase and a manganese peroxidase from Irpex lacteus F17, a lignin-degrading basidiomycete
AMB Express
8
119
2018
Irpex lacteus (A0A2P1C6N7), Irpex lacteus, Irpex lacteus F17 (A0A2P1C6N7)
brenda
Zhang, H.; Zhang, X.; Geng, A.
Expression of a novel manganese peroxidase from Cerrena unicolor BBP6 in Pichia pastoris and its application in dye decolorization and PAH degradation
Biochem. Eng. J.
153
107402
2020
Cerrena unicolor (A0A7D5FUQ6), Cerrena unicolor BBP6 (A0A7D5FUQ6)
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Bronikowski, A.; Koschorreck, K.; Urlacher, V.B.
Redesign of a new manganese peroxidase highly expressed in Pichia pastoris towards a lignin-degrading versatile peroxidase
ChemBioChem
19
2481-2489
2018
Moniliophthora roreri (V2XS39), Moniliophthora roreri, Moniliophthora roreri MCA 2997 (V2XS39)
brenda
Al-Dhabi, N.A.; Esmail, G.A.; Valan Arasu, M.
Effective degradation of tetracycline by manganese peroxidase producing Bacillus velezensis strain Al-Dhabi 140 from Saudi Arabia using fibrous-bed reactor
Chemosphere
268
128726
2021
Bacillus velezensis, Bacillus velezensis Al-Dhabi 140
brenda
Li, L.; Liu, B.; Yang, J.; Zhang, Q.; He, C.; Jia, R.
Catalytic properties of a short manganese peroxidase from Irpex lacteus F17 and the role of Glu166 in the Mn2+-independent activity
Int. J. Biol. Macromol.
136
859-869
2019
Irpex lacteus (S4W784), Irpex lacteus, Irpex lacteus F17 (S4W784), Irpex lacteus CCTCC AF2014020 (S4W784)
brenda
Ding, Y.; Cui, K.; Guo, Z.; Cui, M.; Chen, Y.
Manganese peroxidase mediated oxidation of sulfamethoxazole integrating the computational analysis to reveal the reaction kinetics, mechanistic insights, and oxidation pathway
J. Hazard. Mater.
415
125719
2021
Phanerodontia chrysosporium, Phanerodontia chrysosporium CCTCC AF96007, Phanerodontia chrysosporium BKMF-1767
brenda
Kamei, I.; Tomitaka, N.; Motoda, T.; Yamasaki, Y.
Isozyme selective homologous expression of recombinant manganese peroxidase of salt-tolerant white-rot fungus Phlebia sp. MG-60, and its salt-tolerance and thermostability
J. Microbiol. Biotechnol.
32
248-255
2021
Phlebia sp. MG-60 (A0A068PC52), Phlebia sp. MG-60 (A0A068PCH3), Phlebia sp. MG-60 (B1B554)
brenda
Zhang, H.; Zhang, J.; Zhang, X.; Geng, A.
Purification and characterization of a novel manganese peroxidase from white-rot fungus Cerrena unicolor BBP6 and its application in dye decolorization and denim bleaching
Process Biochem.
66
222-229
2018
Cerrena unicolor (A0A7D5FUQ6), Cerrena unicolor BBP6 (A0A7D5FUQ6)
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Lin, M.I.; Nagata, T.; Katahira, M.
High yield production of fungal manganese peroxidases by E. coli through soluble expression, and examination of the activities
Protein Expr. Purif.
145
45-52
2018
Gelatoporia subvermispora (A0A2I7M8U2), Gelatoporia subvermispora (A0A2I7M8W6), Gelatoporia subvermispora (O42736), Gelatoporia subvermispora B (A0A2I7M8U2), Gelatoporia subvermispora B (A0A2I7M8W6), Gelatoporia subvermispora B (O42736)
brenda
Gaur, N.; Narasimhulu, K.; Pydisetty, Y.
Biochemical and kinetic characterization of laccase and manganese peroxidase from novel Klebsiella pneumoniae strains and their application in bioethanol production
RSC Adv.
8
15044-15055
2018
Klebsiella pneumoniae
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brenda
Chowdhary, P.; Shukla, G.; Raj, G.; Ferreira, L.; Bharagava, R.
Microbial manganese peroxidase a ligninolytic enzyme and its ample opportunities in research
SN Appl. Sci.
1
45
2019
Acinetobacter baumannii, Alcaligenes faecalis, Bacillus cereus, Bacillus subtilis, Gelatoporia subvermispora, Ganoderma lucidum, Ganoderma lucidum (A0A1I9KRQ0), Irpex lacteus, Irpex lacteus (A0A1S6KK55), Irpex lacteus (S4W784), Schizophyllum commune, Trametes villosa, Trametes sp. 48424, Cerrena unicolor (A0A7D5FUQ6), Agrocybe praecox (G4WG41), Phanerodontia chrysosporium (Q02567), Phlebia radiata (Q70LM3), Irpex lacteus CD2 (A0A1S6KK55), Irpex lacteus F17 (S4W784), Irpex lacteus CCBAS238, Schizophyllum commune IBL-06, Ganoderma lucidum IBL-05, Cerrena unicolor BBP6 (A0A7D5FUQ6)
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brenda
Kumar, V.; Chandra, R.
Characterisation of manganese peroxidase and laccase producing bacteria capable for degradation of sucrose glutamic acid-Maillard reaction products at different nutritional and environmental conditions
World J. Microbiol. Biotechnol.
34
32
2018
Klebsiella aerogenes, Enterobacter cloacae, Salmonella enterica, Klebsiella pneumoniae
brenda