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2 L-ascorbate + H2O2 + 2 H+
2 monodehydroascorbate + 2 H2O
2 L-ascorbate + H2O2 + 2 H+
L-ascorbate + L-dehydroascorbate + 2 H2O
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2 + H+
? + H2O
-
-
-
-
?
2,2'-azino-di-(3-ethyl-benzothiazoline-(6)-sulfonic acid) + H2O2
? + H2O
-
3% relative activity to L-ascorbate
-
?
2,2'-azino-di-[3-ethylbenzothiazoline-(6)-sulfonic acid] + H2O2
?
2,2'-azinobis-(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2
?
-
cytosolic ascorbate peroxidase shows 3% activity compared to L-ascorbate, in the presence of 0.1 mM H2O2 and 3.6% activity compared to L-ascorbate in the presence of 0.5 mM H2O2
-
-
?
cysteine + H2O2
? + H2O
-
enzyme partially purified from whole body homogenate, 40% of the activity with L-ascorbate
-
?
Cytochrome c + H2O
?
-
-
-
-
?
cytochrome c + H2O2
?
-
able to use both ascorbate and cytochrome c as reducing electron donors
-
-
?
cytochrome c + H2O2
? + H2O
D-araboascorbic acid + H2O2
dehydroascorbate + H2O
-
56% activity relative to L-ascorbate
-
?
D-iso-ascorbate + H2O2
dehydroascorbate + H2O
Chlamydomonas sp.
native enzyme: the activity with D-isoascorbate corresponds to 131% of that found with ascorbate, recombinant enzyme: the activity with D-isoascorbate corresponds to 129% of that found with ascorbate
-
?
D-isoascorbate + H2O2
?
-
60.3% activity compared to L-ascorbate
-
-
?
dihydrorhodamine 123 + H2O2
?
ethyl phenyl sulfide + H2O2
? + H2O
-
-
-
-
?
ferrocyanide + H2O2
ferricyanide + H2O
-
the Cys32Ser mutation has little effect on the kinetics of ferrocyanide turnover, but the DTNB modification decreases activity by approximately 90% at 300 mM ferrocyanide
-
?
glutathione + H2O2
? + H2O
GSSG + H2O2
?
about 20% of the activity with L-ascorbate
-
-
?
iodide + H2O2
?
-
2.3% activity relative to L-ascorbate
-
?
isopropyl phenyl sulfide + H2O2
? + H2O
-
-
-
?
L-ascorbate + cumene hydroperoxide
?
-
8.0% activity compared to H2O2
-
-
?
L-ascorbate + H2O2
? + H2O
-
-
-
-
?
L-ascorbate + H2O2
dehydroascorbate + 2 H2O
L-ascorbate + H2O2
dehydroascorbate + H2O
L-ascorbate + tert-butyl hydroperoxide
?
-
17.4% activity compared to H2O2
-
-
?
L-ascorbic acid + cumene hydroperoxide
dehydroascorbate + 1,1-dimethylbenzylalcohol + H2O
L-ascorbic acid + tert-butylhydroperoxide
dehydroascorbate + tert-butylalcohol
methyl naphthalene sulfide + H2O2
? + H2O
-
-
-
?
methyl phenyl sulfide + H2O2
? + H2O
-
-
-
?
n-propyl phenyl sulfide + H2O2
? + H2O
-
-
-
?
NADH + H+ + H2O2
NAD+ + H2O
-
10% of the activity with ascorbate, APX 1, 1% of the activity with ascorbate, APX 2
-
-
?
NADPH + H+ + H2O2
NADP+ + H2O
-
27% of the activity with ascorbate, APX 1, 21% of the activity with ascorbate, APX 2
-
-
?
p-chlorophenyl methyl sulfide + H2O2
? + H2O
-
-
-
?
p-cresol + cumene-hydroperoxide
4a,9b-dihydro-8,9b-dimethyl-3(4H)-dibenzofuranone + 2,2'-dihydroxy-5,5'-dimethylbiphenyl + 1,1-dimethylbenzylalcohol + bis-(1-methyl-1-phenylethyl)peroxide
-
-
the formation of bis-(1-methyl-1-phenylethyl)peroxide derives from the reaction of 1,1-dimethylbenzylalcohol with either p-cresol or 2,2'-dihydroxy-5,5'-dimethylbiphenyl
?
p-cresol + H2O2
4a,9b-dihydro-8,9b-dimethyl-3(4H)-dibenzofuranone + 2,2'-dihydroxy-5,5'-dimethylbiphenyl + H2O
-
-
these products, which are derived from reactions of the p-methylphenoxy radical, itself form as a direct result of single-electron oxidation of p-cresol by the enzyme, can be accommodated from the known chemistry of the radical products, the product ratio 4alpha,9beta-dihydro-8,9beta-dimethyl-3(4H)-dibenzofuranone: 2,2'-dihydroxy-5,5'-dimethylbiphenyl is found to depend on enzyme concentration
?
p-nitrophenyl methyl sulfide + H2O2
? + H2O
-
-
-
?
pyrocatechol + H2O2
1,2-benzoquinone + H2O
-
low activity compared to L-ascorbate
-
?
pyrogallol + H2O2
3-hydroxybenzo-1,2-quinone + H2O
pyrogallol + H2O2
? + H2O
-
32% of the activity with ascorbate
-
-
?
reductic acid + H2O2
?
-
i.e. 2,3-dihydroxy-2-cyclopenten-1-one, 7.1% activity relative to L-ascorbate
-
?
additional information
?
-
2 L-ascorbate + H2O2 + 2 H+
2 monodehydroascorbate + 2 H2O
-
-
-
?
2 L-ascorbate + H2O2 + 2 H+
2 monodehydroascorbate + 2 H2O
-
-
-
-
?
2 L-ascorbate + H2O2 + 2 H+
2 monodehydroascorbate + 2 H2O
-
-
-
?
2 L-ascorbate + H2O2 + 2 H+
L-ascorbate + L-dehydroascorbate + 2 H2O
-
-
-
-
?
2 L-ascorbate + H2O2 + 2 H+
L-ascorbate + L-dehydroascorbate + 2 H2O
-
-
-
?
2 L-ascorbate + H2O2 + 2 H+
L-ascorbate + L-dehydroascorbate + 2 H2O
-
-
-
?
2 L-ascorbate + H2O2 + 2 H+
L-ascorbate + L-dehydroascorbate + 2 H2O
-
-
-
?
2 L-ascorbate + H2O2 + 2 H+
L-ascorbate + L-dehydroascorbate + 2 H2O
-
-
-
?
2 L-ascorbate + H2O2 + 2 H+
L-ascorbate + L-dehydroascorbate + 2 H2O
-
-
-
?
2 L-ascorbate + H2O2 + 2 H+
L-ascorbate + L-dehydroascorbate + 2 H2O
Blastochritidia sp. P57
-
-
-
-
?
2 L-ascorbate + H2O2 + 2 H+
L-ascorbate + L-dehydroascorbate + 2 H2O
-
-
-
?
2 L-ascorbate + H2O2 + 2 H+
L-ascorbate + L-dehydroascorbate + 2 H2O
-
-
-
?
2 L-ascorbate + H2O2 + 2 H+
L-ascorbate + L-dehydroascorbate + 2 H2O
-
-
-
-
?
2 L-ascorbate + H2O2 + 2 H+
L-ascorbate + L-dehydroascorbate + 2 H2O
-
-
-
-
?
2 L-ascorbate + H2O2 + 2 H+
L-ascorbate + L-dehydroascorbate + 2 H2O
-
-
-
-
?
2 L-ascorbate + H2O2 + 2 H+
L-ascorbate + L-dehydroascorbate + 2 H2O
-
-
-
?
2 L-ascorbate + H2O2 + 2 H+
L-ascorbate + L-dehydroascorbate + 2 H2O
-
-
-
-
?
2 L-ascorbate + H2O2 + 2 H+
L-ascorbate + L-dehydroascorbate + 2 H2O
-
-
-
?
2 L-ascorbate + H2O2 + 2 H+
L-ascorbate + L-dehydroascorbate + 2 H2O
-
-
-
-
?
2 L-ascorbate + H2O2 + 2 H+
L-ascorbate + L-dehydroascorbate + 2 H2O
-
-
-
-
?
2 L-ascorbate + H2O2 + 2 H+
L-ascorbate + L-dehydroascorbate + 2 H2O
-
-
-
?
2 L-ascorbate + H2O2 + 2 H+
L-ascorbate + L-dehydroascorbate + 2 H2O
-
-
-
-
?
2 L-ascorbate + H2O2 + 2 H+
L-ascorbate + L-dehydroascorbate + 2 H2O
-
the reaction is initiated by the addition of H2O2 and oxidation of ascorbate is monitored by measuring the decrease in absorbance at 290 nm
-
-
?
2 L-ascorbate + H2O2 + 2 H+
L-ascorbate + L-dehydroascorbate + 2 H2O
-
-
-
-
?
2 L-ascorbate + H2O2 + 2 H+
L-ascorbate + L-dehydroascorbate + 2 H2O
-
-
-
-
?
2 L-ascorbate + H2O2 + 2 H+
L-ascorbate + L-dehydroascorbate + 2 H2O
-
-
-
?
2 L-ascorbate + H2O2 + 2 H+
L-ascorbate + L-dehydroascorbate + 2 H2O
-
-
-
?
2 L-ascorbate + H2O2 + 2 H+
L-ascorbate + L-dehydroascorbate + 2 H2O
-
-
-
?
2 L-ascorbate + H2O2 + 2 H+
L-ascorbate + L-dehydroascorbate + 2 H2O
-
-
-
?
2 L-ascorbate + H2O2 + 2 H+
L-ascorbate + L-dehydroascorbate + 2 H2O
-
-
-
?
2 L-ascorbate + H2O2 + 2 H+
L-ascorbate + L-dehydroascorbate + 2 H2O
-
-
-
-
?
2 L-ascorbate + H2O2 + 2 H+
L-ascorbate + L-dehydroascorbate + 2 H2O
-
-
-
?
2 L-ascorbate + H2O2 + 2 H+
L-ascorbate + L-dehydroascorbate + 2 H2O
-
-
-
?
2 L-ascorbate + H2O2 + 2 H+
L-ascorbate + L-dehydroascorbate + 2 H2O
-
-
-
-
?
2 L-ascorbate + H2O2 + 2 H+
L-ascorbate + L-dehydroascorbate + 2 H2O
-
-
-
-
?
2,2'-azino-di-[3-ethylbenzothiazoline-(6)-sulfonic acid] + H2O2
?
-
-
-
-
?
2,2'-azino-di-[3-ethylbenzothiazoline-(6)-sulfonic acid] + H2O2
?
-
-
-
-
?
2,2'-azino-di-[3-ethylbenzothiazoline-(6)-sulfonic acid] + H2O2
?
-
-
-
-
?
2,2'-azino-di-[3-ethylbenzothiazoline-(6)-sulfonic acid] + H2O2
?
-
-
-
-
?
2,2'-azino-di-[3-ethylbenzothiazoline-(6)-sulfonic acid] + H2O2
?
-
-
-
-
?
2,2'-azino-di-[3-ethylbenzothiazoline-(6)-sulfonic acid] + H2O2
?
-
-
-
-
?
2,2'-azino-di-[3-ethylbenzothiazoline-(6)-sulfonic acid] + H2O2
?
-
-
-
-
?
2,2'-azino-di-[3-ethylbenzothiazoline-(6)-sulfonic acid] + H2O2
?
-
-
-
-
?
2,2'-azino-di-[3-ethylbenzothiazoline-(6)-sulfonic acid] + H2O2
?
-
-
-
-
?
2,2'-azino-di-[3-ethylbenzothiazoline-(6)-sulfonic acid] + H2O2
?
-
-
-
-
?
cytochrome c + H2O2
? + H2O
-
no activity
-
-
?
cytochrome c + H2O2
? + H2O
Chlamydomonas sp.
no activity
-
-
?
cytochrome c + H2O2
? + H2O
-
no activity
-
-
?
cytochrome c + H2O2
? + H2O
-
no activity
-
-
?
cytochrome c + H2O2
? + H2O
-
enzyme partially purified from whole body homogenate, 44% of the activity with L-ascorbate
-
?
cytochrome c + H2O2
? + H2O
-
no activity
-
-
?
cytochrome c + H2O2
? + H2O
-
-
-
?
dihydrorhodamine 123 + H2O2
?
-
assay, peroxidase substrate
-
-
?
dihydrorhodamine 123 + H2O2
?
-
assay, peroxidase substrate
-
-
?
glutathione + H2O2
? + H2O
-
no activity
-
-
?
glutathione + H2O2
? + H2O
Chlamydomonas sp.
no activity
-
-
?
glutathione + H2O2
? + H2O
-
no activity
-
-
?
glutathione + H2O2
? + H2O
-
no activity
-
-
?
glutathione + H2O2
? + H2O
-
no activity
-
-
?
glutathione + H2O2
? + H2O
-
enzyme partially purified from whole body homogenate: 22% of the activity with L-ascorbate, enzyme partially purified from regurgitant: 0% relative activity to L-ascorbate, when assayed at the same concentration
-
?
glutathione + H2O2
? + H2O
-
30% of the activity with ascorbate, APX 1, 13% of the activity with ascorbate, APX 2
-
-
?
guaiacol + H2O2
?
-
no reaction
-
-
?
guaiacol + H2O2
?
Chlamydomonas sp.
native enzyme: the activity corresponds to 7.2% of that found with L-ascorbate, recombinant enzyme: the activity corresponds to 8% of that found with L-ascorbate
-
?
guaiacol + H2O2
?
-
no activity
-
-
?
guaiacol + H2O2
?
-
8% activity relative to L-ascorbate
-
?
guaiacol + H2O2
?
-
30.5% activity relative to L-ascorbate
-
?
guaiacol + H2O2
?
-
the reaction rate is approximately equal to the rate with L-ascorbate
-
?
guaiacol + H2O2
?
-
recombinant enzyme 1: 6% activity relative to L-ascorbate, recombinant enzyme 2: 11% relative activity to L-ascorbate
-
?
guaiacol + H2O2
?
about 30% of the activity with L-ascorbate
-
-
?
guaiacol + H2O2
?
-
no activity
-
-
?
guaiacol + H2O2
?
-
-
-
-
?
guaiacol + H2O2
?
-
cytosolic ascorbate peroxidase shows 12% activity compared to L-ascorbate, in the presence of 0.1 mM H2O2 and 24.7% activity compared to L-ascorbate in the presence of 0.5 mM H2O2
-
-
?
guaiacol + H2O2
?
-
-
-
?
guaiacol + H2O2
?
-
-
-
?
guaiacol + H2O2
?
-
the DTNB-modified enzyme exhibits full activity
-
?
guaiacol + H2O2
?
-
form C enzyme, only onesixteenth the rate observed with L-ascorbate
-
?
guaiacol + H2O2
?
-
no activity
-
-
?
guaiacol + H2O2
?
-
the activity is lower than with L-ascorbate
-
?
guaiacol + H2O2
?
-
low activity compared to L-ascorbate
-
?
guaiacol + H2O2
?
-
poor electron donor
-
?
guaiacol + H2O2
? + H2O
-
45% of the activity with ascorbate, APX 1, 15% of the activity with ascorbate, APX 2
-
-
?
guaiacol + H2O2
? + H2O
-
-
-
-
?
guaiacol + H2O2
? + H2O
-
20% of the activity with ascorbate
-
-
?
L-ascorbate + H2O2
dehydroascorbate + 2 H2O
-
-
-
?
L-ascorbate + H2O2
dehydroascorbate + 2 H2O
-
the enzyme works for protection of cell membrane, by reducing the peroxide compounds generated endogenously from unsaturated fatty acids
-
?
L-ascorbate + H2O2
dehydroascorbate + 2 H2O
-
the enzyme appears to be the sole agent destroying H2O2
-
?
L-ascorbate + H2O2
dehydroascorbate + 2 H2O
-
physiological role of the enzyme: removal of H2O2, prevention of H2O2 accumulation
-
?
L-ascorbate + H2O2
dehydroascorbate + 2 H2O
-
physiological role of the enzyme: removal of H2O2, prevention of H2O2 accumulation
-
?
L-ascorbate + H2O2
dehydroascorbate + 2 H2O
-
the enzyme is responsible for most H2O2 removal outside of peroxisomes in root nodules
-
?
L-ascorbate + H2O2
dehydroascorbate + 2 H2O
-
physiological role of the enzyme: removal of H2O2, prevention of H2O2 accumulation
-
?
L-ascorbate + H2O2
dehydroascorbate + 2 H2O
-
the enzyme may be important in removing H2O2 and lipid peroxides in insects
-
?
L-ascorbate + H2O2
dehydroascorbate + 2 H2O
-
-
-
?
L-ascorbate + H2O2
dehydroascorbate + 2 H2O
-
physiological role of the enzyme: removal of H2O2, prevention of H2O2 accumulation
-
?
L-ascorbate + H2O2
dehydroascorbate + 2 H2O
-
-
-
-
?
L-ascorbate + H2O2
dehydroascorbate + 2 H2O
-
role of the mitochondrial enzyme in the scanvenging of toxic oxygen species inside potato tuber mitochondria
-
?
L-ascorbate + H2O2
dehydroascorbate + H2O
-
-
-
?
L-ascorbate + H2O2
dehydroascorbate + H2O
-
-
-
-
?
L-ascorbate + H2O2
dehydroascorbate + H2O
-
-
-
?
L-ascorbate + H2O2
dehydroascorbate + H2O
-
-
-
?
L-ascorbate + H2O2
dehydroascorbate + H2O
-
L-ascorbate is the most effective natural electron donor
-
?
L-ascorbate + H2O2
dehydroascorbate + H2O
-
-
-
?
L-ascorbate + H2O2
dehydroascorbate + H2O
-
-
-
?
L-ascorbate + H2O2
dehydroascorbate + H2O
Chlamydomonas sp.
native and recombinant enzyme, no activation is observed, when the enzyme is incubated with H2O2 under anaerobic conditions, thus one of the reasons for the stability mechanism in the enzyme may be the insusceptibility of compound I to H2O2
-
?
L-ascorbate + H2O2
dehydroascorbate + H2O
-
-
-
?
L-ascorbate + H2O2
dehydroascorbate + H2O
-
-
-
-
?
L-ascorbate + H2O2
dehydroascorbate + H2O
-
-
-
-
?
L-ascorbate + H2O2
dehydroascorbate + H2O
-
-
-
-
?
L-ascorbate + H2O2
dehydroascorbate + H2O
-
-
-
-
?
L-ascorbate + H2O2
dehydroascorbate + H2O
-
-
-
-
?
L-ascorbate + H2O2
dehydroascorbate + H2O
-
-
-
?
L-ascorbate + H2O2
dehydroascorbate + H2O
-
tert-butyl hydroperoxide and cumene hydroperoxide also serve as electron acceptor
-
?
L-ascorbate + H2O2
dehydroascorbate + H2O
-
100% activity
-
-
?
L-ascorbate + H2O2
dehydroascorbate + H2O
-
-
-
?
L-ascorbate + H2O2
dehydroascorbate + H2O
-
-
-
?
L-ascorbate + H2O2
dehydroascorbate + H2O
-
-
-
-
?
L-ascorbate + H2O2
dehydroascorbate + H2O
-
-
-
?
L-ascorbate + H2O2
dehydroascorbate + H2O
-
-
-
?
L-ascorbate + H2O2
dehydroascorbate + H2O
-
-
-
?
L-ascorbate + H2O2
dehydroascorbate + H2O
-
-
-
?
L-ascorbate + H2O2
dehydroascorbate + H2O
-
-
-
?
L-ascorbate + H2O2
dehydroascorbate + H2O
-
-
-
?
L-ascorbate + H2O2
dehydroascorbate + H2O
-
-
-
?
L-ascorbate + H2O2
dehydroascorbate + H2O
-
-
-
?
L-ascorbate + H2O2
dehydroascorbate + H2O
-
tert-butyl hydroperoxide and cumene hydroperoxide also serve as electron acceptor
-
?
L-ascorbate + H2O2
dehydroascorbate + H2O
-
L-ascorbate is the most effective natural electron donor
-
?
L-ascorbate + H2O2
dehydroascorbate + H2O
-
-
-
-
?
L-ascorbate + H2O2
dehydroascorbate + H2O
-
-
-
?
L-ascorbate + H2O2
dehydroascorbate + H2O
-
-
-
-
?
L-ascorbate + H2O2
dehydroascorbate + H2O
-
-
-
-
?
L-ascorbate + H2O2
dehydroascorbate + H2O
-
-
-
?
L-ascorbate + H2O2
dehydroascorbate + H2O
-
-
-
?
L-ascorbate + H2O2
dehydroascorbate + H2O
-
-
-
?
L-ascorbate + H2O2
dehydroascorbate + H2O
-
-
-
?
L-ascorbate + H2O2
dehydroascorbate + H2O
-
-
-
-
?
L-ascorbate + H2O2
dehydroascorbate + H2O
-
-
-
?
L-ascorbate + H2O2
dehydroascorbate + H2O
-
-
-
-
?
L-ascorbate + H2O2
dehydroascorbate + H2O
-
-
-
-
?
L-ascorbate + H2O2
dehydroascorbate + H2O
-
-
-
?
L-ascorbate + H2O2
dehydroascorbate + H2O
-
cytosolic ascorbate peroxidase shows 100% activity in the presence of 0.1 mM and 0.5 mM H2O2
-
-
?
L-ascorbate + H2O2
dehydroascorbate + H2O
-
-
-
?
L-ascorbate + H2O2
dehydroascorbate + H2O
-
-
-
?
L-ascorbate + H2O2
dehydroascorbate + H2O
-
-
-
?
L-ascorbate + H2O2
dehydroascorbate + H2O
-
-
-
?
L-ascorbate + H2O2
dehydroascorbate + H2O
-
-
-
?
L-ascorbate + H2O2
dehydroascorbate + H2O
-
-
-
-
?
L-ascorbate + H2O2
dehydroascorbate + H2O
-
the DTNB-modified enzyme exhibits only 1.3% wild-type activity when ascorbate is used as substrate, the DTNB-modified enzyme reacts normally with peroxide to give compound I but the rates of reduction of both compounds I and II by ascorbate are dramatically slowed. The Cys32Ser mutant has one-third wild-type activity. The ascorbate interactions with the enzyme are partly mediated through electrostatic interactions
-
?
L-ascorbate + H2O2
dehydroascorbate + H2O
-
an equimolar mixture of native enzyme and H2O2 forms some transient compound I which, within 60 s is converted to compound II, addition of 5 mM ascorbate rapidly reduces compound II back to the native enzyme
-
?
L-ascorbate + H2O2
dehydroascorbate + H2O
Populus simonii x Populus pyramidalis
-
-
-
-
?
L-ascorbate + H2O2
dehydroascorbate + H2O
-
-
-
?
L-ascorbate + H2O2
dehydroascorbate + H2O
-
highly specific for L-ascorbate
-
?
L-ascorbate + H2O2
dehydroascorbate + H2O
-
-
-
-
?
L-ascorbate + H2O2
dehydroascorbate + H2O
-
-
-
-
?
L-ascorbate + H2O2
dehydroascorbate + H2O
-
-
-
-
?
L-ascorbate + H2O2
dehydroascorbate + H2O
-
-
-
?
L-ascorbate + H2O2
dehydroascorbate + H2O
-
-
-
-
?
L-ascorbate + H2O2
dehydroascorbate + H2O
-
highly specific for
-
?
L-ascorbate + H2O2
dehydroascorbate + H2O
-
-
-
?
L-ascorbate + H2O2
dehydroascorbate + H2O
-
-
-
?
L-ascorbate + H2O2
dehydroascorbate + H2O
-
-
-
-
?
L-ascorbate + H2O2
dehydroascorbate + H2O
-
-
-
?
L-ascorbate + H2O2
dehydroascorbate + H2O
-
-
?
L-ascorbate + H2O2
dehydroascorbate + H2O
-
-
-
?
L-ascorbate + H2O2
dehydroascorbate + H2O
-
-
-
?
L-ascorbate + H2O2
dehydroascorbate + H2O
-
-
-
?
L-ascorbate + H2O2
dehydroascorbate + H2O
-
-
-
?
L-ascorbic acid + cumene hydroperoxide
dehydroascorbate + 1,1-dimethylbenzylalcohol + H2O
Chlamydomonas sp.
no activity
-
-
?
L-ascorbic acid + cumene hydroperoxide
dehydroascorbate + 1,1-dimethylbenzylalcohol + H2O
-
no activity
-
-
?
L-ascorbic acid + cumene hydroperoxide
dehydroascorbate + 1,1-dimethylbenzylalcohol + H2O
-
-
-
?
L-ascorbic acid + cumene hydroperoxide
dehydroascorbate + 1,1-dimethylbenzylalcohol + H2O
-
34% of the activity with H2O2
-
?
L-ascorbic acid + tert-butylhydroperoxide
dehydroascorbate + tert-butylalcohol
Chlamydomonas sp.
no activity
-
-
?
L-ascorbic acid + tert-butylhydroperoxide
dehydroascorbate + tert-butylalcohol
-
no activity
-
-
?
L-ascorbic acid + tert-butylhydroperoxide
dehydroascorbate + tert-butylalcohol
-
-
-
?
L-ascorbic acid + tert-butylhydroperoxide
dehydroascorbate + tert-butylalcohol
-
both enzymes A and B
-
?
L-ascorbic acid + tert-butylhydroperoxide
dehydroascorbate + tert-butylalcohol
-
92% of the activity with H2O2
-
?
NADPH + H2O2
? + H2O
-
no activity
-
-
?
NADPH + H2O2
? + H2O
Chlamydomonas sp.
no activity
-
-
?
NADPH + H2O2
? + H2O
-
no activity
-
-
?
NADPH + H2O2
? + H2O
-
no activity
-
-
?
NADPH + H2O2
? + H2O
-
no activity
-
-
?
NADPH + H2O2
? + H2O
-
enzyme partially purified from whole body homogenate: 93% of the activity with L-ascorbate, enzyme partially purified from regurgitant: 36% of the activity with L-ascorbate, when assayed at the same concentration
-
?
o-dianisidine + H2O2
?
-
reaction rate approximately equal to the rate with L-ascorbate
-
?
o-dianisidine + H2O2
?
-
the oxidation rate is only 8.6% of that with L-ascorbate
-
?
pyrogallol + H2O2
3-hydroxybenzo-1,2-quinone + H2O
-
2.5-fold higher rate than that of L-ascorbate
-
?
pyrogallol + H2O2
3-hydroxybenzo-1,2-quinone + H2O
Chlamydomonas sp.
native enzyme: the activity corresponds to 121% of that found with L-ascorbate, recombinant enzyme: the activity corresponds to 130% of that found with L-ascorbate
-
?
pyrogallol + H2O2
3-hydroxybenzo-1,2-quinone + H2O
-
62.6% activity relative to L-ascorbate
-
?
pyrogallol + H2O2
3-hydroxybenzo-1,2-quinone + H2O
-
-
-
?
pyrogallol + H2O2
3-hydroxybenzo-1,2-quinone + H2O
-
73.1% activity relative to L-ascorbate
-
?
pyrogallol + H2O2
3-hydroxybenzo-1,2-quinone + H2O
-
the reaction rate is 38-fold higher than the rate with L-ascorbate
-
?
pyrogallol + H2O2
3-hydroxybenzo-1,2-quinone + H2O
-
recombinant enzyme 1: 355% activity relative to L-ascorbate, recombinant enzyme 2: 304% activity relative to L-ascorbate
-
?
pyrogallol + H2O2
3-hydroxybenzo-1,2-quinone + H2O
-
723% activity relative to L-ascorbate
-
?
pyrogallol + H2O2
3-hydroxybenzo-1,2-quinone + H2O
-
-
-
?
pyrogallol + H2O2
3-hydroxybenzo-1,2-quinone + H2O
-
the DTNB-modified enzyme exhibits full activity
-
?
pyrogallol + H2O2
3-hydroxybenzo-1,2-quinone + H2O
-
the oxidation rate is only 5.5% of that with L-ascorbate
-
?
pyrogallol + H2O2
3-hydroxybenzo-1,2-quinone + H2O
-
the activity is lower than with L-ascorbate
-
?
pyrogallol + H2O2
3-hydroxybenzo-1,2-quinone + H2O
-
low activity compared to L-ascorbate
-
?
pyrogallol + H2O2
3-hydroxybenzo-1,2-quinone + H2O
-
238% activity relative to L-ascorbate
-
-
?
pyrogallol + H2O2
?
-
little activity
-
-
?
pyrogallol + H2O2
?
-
little activity
-
-
?
pyrogallol + H2O2
?
-
90.1% activity compared to L-ascorbate
-
-
?
pyrogallol + H2O2
?
-
cytosolic ascorbate peroxidase shows 29% activity compared to L-ascorbate, in the presence of 0.1 mM H2O2 and 208% activity compared to L-ascorbate in the presence of 0.5 mM H2O2
-
-
?
additional information
?
-
AtAPX1 exhibits both peroxidase and chaperone activities
-
-
-
additional information
?
-
-
AtAPX1 exhibits both peroxidase and chaperone activities
-
-
-
additional information
?
-
enzyme interaction analysis, overview
-
-
-
additional information
?
-
enzyme interaction analysis, overview
-
-
-
additional information
?
-
enzyme interaction analysis, overview
-
-
-
additional information
?
-
enzyme interaction analysis, overview
-
-
-
additional information
?
-
enzyme interaction analysis, overview
-
-
-
additional information
?
-
enzyme interaction analysis, overview
-
-
-
additional information
?
-
enzyme interaction analysis, overview
-
-
-
additional information
?
-
APX enzymatic activity is measured by the decrease in absorbance at 290 nm due to the oxidation of ascorbate. The AtAPX1 protein shows a high chaperone activity as incubation of MDH with increasing amounts of AtAPX1 results in a concomitant decrease in the aggregation of MDH at 43°C. The aggregation of MDH is effectively suppressed at a subunit molar ratio of MDH to AtAPX1 of 1:2
-
-
-
additional information
?
-
-
APX enzymatic activity is measured by the decrease in absorbance at 290 nm due to the oxidation of ascorbate. The AtAPX1 protein shows a high chaperone activity as incubation of MDH with increasing amounts of AtAPX1 results in a concomitant decrease in the aggregation of MDH at 43°C. The aggregation of MDH is effectively suppressed at a subunit molar ratio of MDH to AtAPX1 of 1:2
-
-
-
additional information
?
-
AtAPX1 exhibits both peroxidase and chaperone activities
-
-
-
additional information
?
-
APX enzymatic activity is measured by the decrease in absorbance at 290 nm due to the oxidation of ascorbate. The AtAPX1 protein shows a high chaperone activity as incubation of MDH with increasing amounts of AtAPX1 results in a concomitant decrease in the aggregation of MDH at 43°C. The aggregation of MDH is effectively suppressed at a subunit molar ratio of MDH to AtAPX1 of 1:2
-
-
-
additional information
?
-
-
the cytosolic enzyme exhibits no activity with: glutathione, cytochrome c and NAD(P)H
-
-
?
additional information
?
-
-
enzyme interaction analysis, overview
-
-
-
additional information
?
-
enzyme interaction analysis, overview
-
-
-
additional information
?
-
enzyme interaction analysis, overview
-
-
-
additional information
?
-
enzyme interaction analysis, overview
-
-
-
additional information
?
-
Chlamydomonas sp.
native and recombinant enzyme, no activity with: glutathione, NADPH and cytochrome c
-
-
?
additional information
?
-
-
no activity with: glutathione, cytochrome c, NADH and NADPH
-
-
?
additional information
?
-
-
the activity with glutathione is less than 1.1% of that with L-ascorbic acid, no activity with: cytochrome c, NADH, NADPH, palmitic acid and triose reductone
-
-
?
additional information
?
-
-
no activity with: NADH, NADPH, cytochrome c, glutathione and palmitic acid as the natural electron donor
-
-
?
additional information
?
-
-
no activity with guaiacol and NADPH
-
-
?
additional information
?
-
-
no activity with: NAD(P)H, reduced glutathione or urate
-
-
?
additional information
?
-
GhAPX1 is involved in hydrogen peroxide homeostasis during cotton fibre development
-
-
?
additional information
?
-
-
GhAPX1 is involved in hydrogen peroxide homeostasis during cotton fibre development
-
-
?
additional information
?
-
-
no activity with guaiacol
-
-
?
additional information
?
-
interaction analysis of enzyme MaAPX1 with enzyme MaMsrB2, overview. The repair of oxidized MaAPX1 is conducted by incubating oxidized proteins (0.002 mM each) and 10 mM DTT at 37°C for 3 h
-
-
-
additional information
?
-
-
interaction analysis of enzyme MaAPX1 with enzyme MaMsrB2, overview. The repair of oxidized MaAPX1 is conducted by incubating oxidized proteins (0.002 mM each) and 10 mM DTT at 37°C for 3 h
-
-
-
additional information
?
-
-
the enzyme transforms approximately 97% methyl phenyl sulfide to its sulfoxide. The product is a racemic mixture
-
-
-
additional information
?
-
APXs in rice plant are able to interact with dehydroascorbate reductase 2 (EC 1.8.5.1). Enzyme interaction analysis, overview
-
-
-
additional information
?
-
APXs in rice plant are able to interact with dehydroascorbate reductase 2 (EC 1.8.5.1). Enzyme interaction analysis, overview
-
-
-
additional information
?
-
APXs in rice plant are able to interact with dehydroascorbate reductase 2 (EC 1.8.5.1). Enzyme interaction analysis, overview
-
-
-
additional information
?
-
APXs in rice plant are able to interact with dehydroascorbate reductase 2 (EC 1.8.5.1). Enzyme interaction analysis, overview
-
-
-
additional information
?
-
APXs in rice plant are able to interact with dehydroascorbate reductase 2 (EC 1.8.5.1). Enzyme interaction analysis, overview
-
-
-
additional information
?
-
APXs in rice plant are able to interact with dehydroascorbate reductase 2 (EC 1.8.5.1). Enzyme interaction analysis, overview
-
-
-
additional information
?
-
APXs in rice plant are able to interact with dehydroascorbate reductase 2 (EC 1.8.5.1). Enzyme interaction analysis, overview
-
-
-
additional information
?
-
APXs in rice plant are able to interact with dehydroascorbate reductase 2 (EC 1.8.5.1). Enzyme interaction analysis, overview
-
-
-
additional information
?
-
determination of H2O2 by recording the absorbance at 390 nm
-
-
-
additional information
?
-
determination of H2O2 by recording the absorbance at 390 nm
-
-
-
additional information
?
-
determination of H2O2 by recording the absorbance at 390 nm
-
-
-
additional information
?
-
determination of H2O2 by recording the absorbance at 390 nm
-
-
-
additional information
?
-
determination of H2O2 by recording the absorbance at 390 nm
-
-
-
additional information
?
-
determination of H2O2 by recording the absorbance at 390 nm
-
-
-
additional information
?
-
determination of H2O2 by recording the absorbance at 390 nm
-
-
-
additional information
?
-
determination of H2O2 by recording the absorbance at 390 nm
-
-
-
additional information
?
-
-
cytosolic and chloroplastic ascorbate peroxidase shows no activity with tert-butyl hydroperoxide and cumene hydroperoxide, pyrocatechol, hydroxyurea, GSH, cytochrome c, NADH, and NADPH. Chlorplastic ascorbate peroxidase displays no activity with pyrogallol, guaiacol, pyrocatechol, and 2,2'-azinobis-(3-ethylbenzothiazoline-6-sulfonic acid)
-
-
?
additional information
?
-
-
guaiacol and pyrogallol are substrates, but the enzyme is inactivated by the oxidized guaiacol and pyrogallol products
-
-
?
additional information
?
-
enzyme interaction analysis, overview
-
-
-
additional information
?
-
enzyme interaction analysis, overview
-
-
-
additional information
?
-
enzyme interaction analysis, overview
-
-
-
additional information
?
-
enzyme interaction analysis, overview
-
-
-
additional information
?
-
enzyme interaction analysis, overview
-
-
-
additional information
?
-
-
-
-
-
?
additional information
?
-
-
experimental and modelled enantiomeric ratios R: S for oxidation of thioethers by recombinant enzyme and mutant Trp-41-Ala
-
-
?
additional information
?
-
there are two main sites for substrate oxidation. The first, close to the gamma-heme edge, is used by ascorbate peroxidase and is presumed to be the main physiological binding site. The second site is close to the delta-heme edge. Role of Ala134 in controlling peroxidase reactivity at the delta-heme edge, overview. Assaying with L-ascorbate, guaiacol and 2,2'-azinobis-3-ethylbenzothiazoline-6-sulphonic acid
-
-
-
additional information
?
-
-
enzyme interaction analysis, overview
-
-
-
additional information
?
-
enzyme interaction analysis, overview
-
-
-
additional information
?
-
enzyme interaction analysis, overview
-
-
-
additional information
?
-
enzyme interaction analysis, overview
-
-
-
additional information
?
-
enzyme interaction analysis, overview
-
-
-
additional information
?
-
enzyme interaction analysis, overview
-
-
-
additional information
?
-
enzyme interaction analysis, overview
-
-
-
additional information
?
-
enzyme interaction analysis, overview
-
-
-
additional information
?
-
enzyme interaction analysis, overview
-
-
-
additional information
?
-
enzyme interaction analysis, overview
-
-
-
additional information
?
-
-
no activity with: cytochrome c, reduced glutathione, NADH, NADPH, 6-palmityl-ascorbate, ascorbate-2-sulfate, guaiacol, 3,3'-diaminobenzidine, pyrocatechol or D-iso-ascorbate
-
-
?
additional information
?
-
-
can cooperate with monodehydroascorbate reductase in glyoxysomal membrane to oxidize NADH, regenerate ascorbate, detoxify H2O2
-
-
?
additional information
?
-
-
essential for photosynthesis
-
-
?
additional information
?
-
reaction includes formation of a compound I-like product, characteristic of the generation of a tryptophanyl radical-cation at residue W233. In addition, formation of a C222-derived radical is observed. electron transfer between Trp233 and Cys222 is possible and likely to participate in the catalytic cycle
-
-
?
additional information
?
-
-
no activity with NADH
-
-
?