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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
?
A7KIX5
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
J7EIR8
-
-
-
?
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
U5RZT9
-
-
-
?
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
?
A7KIX5
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
?
-
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
A4ZYP9
-
-
-
?
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
Q43758
-
-
-
?
L-ascorbate + H2O2
dehydroascorbate + H2O
-
-
-
?
L-ascorbate + H2O2
dehydroascorbate + H2O
-
-
-
-
?
L-ascorbate + H2O2
dehydroascorbate + H2O
A7KIX5
-
-
-
?
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
-
-
-
?
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
-
-
-
-
?
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

?
-
-
the cytosolic enzyme exhibits no activity with: glutathione, cytochrome c and NAD(P)H
-
-
-
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
?
-
A7KIX5
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
?
-
-
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
?
-
-
-
-
-
-
additional information
?
-
-
experimental and modelled enantiomeric ratios R: S for oxidation of thioethers by recombinant enzyme and mutant Trp-41-Ala
-
-
-
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
-
-
-
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2,2,6,6-tetramethylpiperidinyl-1-oxide
-
formation of 2,2,6,6-tetramethylpiperidinyl-1-oxy-adducts and subsequent oxidation of the cysteine residue located near the propionate group of heme leads to loss of enzyme activity
2,2,6,6-tetramethylpiperidinyl-1-oxyl radical
-
formation of 2,2,6,6-tetramethylpiperidinyl-1-oxy-adducts and subsequent oxidation of the cysteine residue located near the propionate group of heme leads to loss of enzyme activity
2,6-dichloroisonicotinic acid
-
54% inhibition at 0.1 mM, 95% inhibition at 1 mM, the inhibition is not time-dependent
2,6-dihydroxybenzoic acid
-
biologically active, 72% inhibition at 0.2 mM
3,3'-dithiobis(6-nitrobenzoic acid)
-
5 mM, 80% residual activity, APX 1, 24% residual activity, APX 2
3,5-dichlorosalicylic acid
-
biologically active, 59% inhibition at 0.2 mM
3-Hydroxybenzoic acid
-
biologically inactive, 28% inhibition at 0.2 mM
4-aminosalicylic acid
-
biologically inactive, 9% inhibition at 0.2 mM
4-chlorosalicylic acid
-
biologically active, 58% inhibition at 0.2 mM
5,5'-dithiobis(2-nitrobenzoic acid)
5-chlorosalicylic acid
-
biologically active, 73% inhibition at 0.2 mM
beta-mercaptoethanol
-
29% inhibition at 3 mM
Br-
-
marked inhibition at 1 mM
diethylenetriamine pentaacetic acid
-
9% inhibition at 5 mM
Hg2+
-
complete inhibition at 1 mM
imidazole
J7EIR8
enzyme shows a decrease in its activity with increasing imidazole concentration, approximately 50% activity is lost in the presence of 0.8 M imidazole
L-cysteine
-
28% inhibition at 3 mM
Mersalyl
-
58% inhibition at 0.005 mM, 100% inhibition at 0.05 mM
Mn2+
-
marked inhibition at 1 mM
N-ethylmaleimide
-
33% inhibition at 0.05 mM, 28% inhibition at 0.5 mM
Na2HAsO4
-
inhibition in the range of 0.01-0.5 mM
p-chloromercuriphenyl sulfonic acid
-
100% inhibition at 0.05 mM, recombinant enzyme 1 and 2
p-hydroxymercuribenzoate
-
43% inhibition at 0.005 mM, 100% inhibition at 0.05 mM
Sodium azide
-
1 mM, 72% residual activity, APX 1, 55% residual activity, APX 2
sodium nitroprusside
-
partial
2-mercaptoethanol

-
enzyme form C: 50% inhibition at 5 mM, 6 min, 100% inhibition after 18 min
2-mercaptoethanol
-
not inhibitory at 0.5 mM, 31% inhibition at 5 mM
5,5'-dithiobis(2-nitrobenzoic acid)

-
96% inhibition at 0.5 mM
5,5'-dithiobis(2-nitrobenzoic acid)
-
40% inhibition at 0.1 mM
Al3+

-
-
Al3+
-
inhibition in the range of 0.01-0.5 mM
azide

-
-
azide
-
46% inhibition at 0.5 mM
C2H2

-
potent inhibitor
C2H2
-
recombinant enzyme 1: 94% inhibition at 0.1 ml per l, recombinant enzyme 2: 2% inhibition at 0.1 ml per l
cysteine

-
50% inhibition at 5 mM
cysteine
-
100% inhibition at 5 mM
dithioerythritol

-
37% inhibition at 3 mM
dithioerythritol
-
67% inhibition at 0.05 mM
dithiothreitol

-
40% inhibition at 3 mM
dithiothreitol
-
enzyme form C: 100% inhibition at 0.1 mM for 5 min, 57% of the inhibition can be recovered by filtration on Sephadex G-25 and a further 14% is recovered after the addition of homocystine at 2 mM
dithiothreitol
-
54% inhibition at 0.05 mM
EDTA

-
slight inhibition, but when the enzyme is incubated with EDTA 1 mM at 37°C for 3 min in the absence of sucrose and ferrous sulfate there is nearly complete inhibition
EDTA
-
97% inhibition at 3 mM
H2O2

wild-type enzyme has a half-time of inactivation of less than 10 sec. Triple mutant C26S/W35F/C126A retains 50% of the initial activity after H2O2 treatment for 3 min
H2O2
-
when inactivated by H2O2, heme is irreversibly cross-linked to the APX apoprotein. tsAPXW35F is inactivated in 3 min by H2O2. It is possible that tsAPXW35F is inactivated by adistinct mechanism because the heme can no longer be cross-linked to the enzyme
hydroxylamine

A4ZYP9
-
hydroxylamine
-
recombinant enzyme 1: 74% inhibition at 1 mM and 100% inhibition at 10 mM, recombinant enzyme 2: 86% inhibition at 1 mM and 100% inhibition at 10 mM
Hydroxyurea

-
26% inhibition at 1 mM
iodoacetamide

-
19% inhibition at 3 mM
iodoacetamide
-
30% inhibition at 1 mM, 65% inhibition at 5 mM
iodoacetate

-
not inhibitory
iodoacetate
-
potent inhibitor
KCN

-
complete inhibition at 0.05 mM
KCN
Chlamydomonas sp.
complete inhibition at 0.1 mM
KCN
-
strong inhibition at 1 mM
KCN
-
96.4% inhibition at 1 mM
KCN
-
recombinant enzyme 1: 69% inhibition at 0.1 mM and 100% inhibition at 0.5 mM, recombinant enzyme 2: 81% inhibition at 0.1 mM and 100% inhibition at 0.5 mM
KCN
-
10% inhibition at 5 mM
KCN
-
1 mM, 69% residual activity, APX 1, 20% residual activity, APX 2
KCN
-
enzyme form C: 74% inhibition at 0.1 mM
KCN
-
95% inhibition at 0.1 mM
KCN
-
100% inhibition at 0.5 mM
KCN
-
87% inhibition at 1 mM
NaN3

-
complete inhibition at 1 mM
NaN3
Chlamydomonas sp.
complete inhibition at 4 mM
NaN3
-
strong inhibition at 5 mM
NaN3
-
91.5% inhibition at 1 mM
NaN3
-
enzyme form C: 27% inhibition at 5 mM
NaN3
-
17% inhibition at 1 mM, 87% inhibition at 10 mM
NaN3
-
80% inhibition at 1 mM
NaN3
-
13% inhibition at 5 mM
Ni2+

-
-
Ni2+
-
below 0.01 mM, activation, inhibition above
p-Aminophenol

-
not inhibitory
p-Aminophenol
-
time-dependent inhibition
p-chloromercuribenzoate

Chlamydomonas sp.
84% inhibition at 0.2 mM for 5 min
p-chloromercuribenzoate
-
82% inhibition at 0.2 mM for 5 min
p-chloromercuribenzoate
-
27% inhibition at 3 mM
p-chloromercuribenzoate
-
87% inhibition at 0.005 mM, inactivation is partially reversible, 2-mercaptoethanol protects
p-chloromercuribenzoate
-
95% inhibition at 0.05 mM
reduced glutathione

-
25% inhibition at 3 mM
reduced glutathione
-
enzyme form C: 75% inhibition at 0.25 mM for 10 min
reduced glutathione
-
33% inhibition at 5 mM
salicylic acid

-
reducing substrate, not inhibitory
salicylic acid
-
biologically active, reversible inhibition, 59% inhibition at 0.1 mM, 83% inhibition at 0.2 mM, 95% inhibition at 1 mM, the inhibition is not time-dependent
salicylic acid
-
reducing substrate, not inhibitory
salicylic acid
-
98% inhibition at 0.5 mM
Zn2+

-
-
Zn2+
-
leaves of plants grown with both low and high Zn show accumulation of lipid peroxides, ascorbate and dehydroascorbate, associated with a decrease in the activity of the enzyme
additional information

-
not inhibitory up to 100 mM: cyanide, azide, aminotriazole
-
additional information
-
not inhibitory: alpha,alphaā-dipyridyl, EDTA
-
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0.01
-
crude extract of root nodules, the activity is rapidly lost after extraction
0.092
-
crude extract of root nodules
0.096
-
crude extract of root nodules, cv Alaska
0.11
-
crude extract of root nodules
0.161
-
crude extract of root nodules, cv Austrian winter
0.213
-
crude extract of root nodules
0.241
-
crude extract of root nodules
0.258
-
crude extract of root nodules
0.26
-
effect of abscisic acid and EGTA on APX activity, 1 day following chilling stress
0.27
-
effect of abscisic acid and EGTA on APX activity, 7 days, under normal temperature
0.28
-
effect of abscisic acid and EGTA on APX activity, 4 days following chilling stress; effect of abscisic acid and LaCl3 on APX activity, 4 days following chilling stress
0.284
-
crude extract of root nodules
0.3
-
effect of EGTA on APX activity, 4 days following chilling stress; in water, 4 days following chilling stress
0.31
-
effect of abscisic acid and EGTA on APX activity, 4 days, under normal temperature; effect of abscisic acid on APX activity, 7 days, under normal temperature; effect of LaCl3 on APX activity, 7 days, under normal temperature
0.32
-
effect of abscisic acid and LaCl3 on APX activity, 1 day following chilling stress; effect of EGTA on APX activity, 1 day following chilling stress; effect of LaCl3 on APX activity, 4 days following chilling stress; in water, 1 day following chilling stress
0.33
-
effect of abscisic acid and LaCl3 on APX activity, 4 days, under normal temperature; effect of abscisic acid and LaCl3 on APX activity, 7 days, under normal temperature; effect of EGTA on APX activity, 4 days, under normal temperature; effect of EGTA on APX activity, 7 days, under normal temperature; in water, 7 days, under normal temperature
0.35
-
in water, 4 days, under normal temperature
0.36
-
effect of abscisic acid on APX activity, 4 days following chilling stress; effect of LaCl3 on APX activity, 1 day following chilling stress
0.366
-
crude extract of root nodules
0.37
-
effect of LaCl3 on APX activity, 4 days, under normal temperature
0.4
-
effect of abscisic acid on APX activity, 1 day following chilling stress
0.45
-
effect of abscisic acid on APX activity, 4 days, under normal temperature
1.3
Chlamydomonas sp.
recombinant enzyme, soluble fraction, addition of 3% NaCl
1.6
-
crude extract, in 50 mM potassium phosphate (pH 7.0), at 22°C
2.8
-
purified enzyme, electron donor: glutathione, electron acceptor: H2O2
3 - 4
-
affinity purified preparation
4.32
-
crude extract of root nodules, activity is only detected when soluble polyvinylpolypyrrolidone is included in the buffer and O2 is excluded by through degassing of buffers and performing all extraction steps under a vigorous stream of N2 gas
5.8
-
purified enzyme, electron donor: iodide, electron acceptor: H2O2
7.1
-
substrate: cumene hydroperoxide
9.4
-
recombinant enzyme 1, after DEAE-column chromatography
19.2
-
substrate: tert-butyl hydroperoxide
20.3
-
purified enzyme, electron donor: guaiacol, electron acceptor: H2O2
31.7
-
purified recombinant enzyme
37
-
stress factor drought
46.7
-
partially purified enzyme
53
-
stress factors drought and heat
63.6
-
recombinant enzyme 2, after chromatofocusing
100
-
cytosolic enzyme, in the presence and absence of salicylic acid
117
-
purified recombinant enzyme
132.2
-
purified enzyme, electron donor: L-ascorbic acid, electron acceptor: cumene hydroperoxide
142.1
-
purified enzyme, electron donor: D-araboascorbic acid, electron acceptor: H2O2
172.8
-
purified enzyme, electron donor: L-ascorbic acid, electron acceptor: tert-butyl hydroperoxide
185.5
-
purified enzyme, electron donor: pyrogallol, electron acceptor: H2O2
254
-
purified enzyme, electron donor: L-ascorbic acid, electron acceptor: H2O2
456
-
after 285fold purification, in 50 mM potassium phosphate (pH 7.0), at 22°C
580
Chlamydomonas sp.
purified recombinant enzyme
636
Chlamydomonas sp.
purified native enzyme
1500
-
chloroplastic enzyme, in the presence and absence of salicylic acid
additional information
-
effects of media amendments
18

-
stress factor heat
18
-
purified enzyme, electron donor: reductic acid, electron acceptor: H2O2
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