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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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2 L-ascorbate + H2O2 + 2 H+
L-ascorbate + L-dehydroascorbate + 2 H2O
L-ascorbate + H2O2
dehydroascorbate + 2 H2O
L-ascorbate + H2O2
dehydroascorbate + H2O
additional information
?
-
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
-
-
-
-
?
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
-
-
-
-
?
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 + 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
-
-
-
-
?
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
?
-
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
?
-
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
?
-
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
?
-
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
?
-
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
?
-
-
can cooperate with monodehydroascorbate reductase in glyoxysomal membrane to oxidize NADH, regenerate ascorbate, detoxify H2O2
-
-
?
additional information
?
-
-
essential for photosynthesis
-
-
?
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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
2-nitrobenzoic acid
-
1.48% activity remaining at 1 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
Cd2+
-
inhibits the enzyme at 1-10 mM
Co2+
-
inhibits the enzyme at 1-10 mM
Cu2+
-
inhibits the enzyme at 1 mM, complete inhibition at 5 mM
diethylenetriamine pentaacetic acid
-
9% inhibition at 5 mM
Fe3+
-
inhibits the enzyme at 1-10 mM
imidazole
enzyme shows a decrease in its activity with increasing imidazole concentration, approximately 50% activity is lost in the presence of 0.8 M imidazole
K+
-
inhibits the enzyme at 1-10 mM
Mersalyl
-
58% inhibition at 0.005 mM, 100% inhibition at 0.05 mM
N-ethylmaleimide
-
33% inhibition at 0.05 mM, 28% inhibition at 0.5 mM
Na+
-
inhibits the enzyme at 1-10 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
Pb2+
-
inhibits the enzyme at 1-5 mM, almost complete inhibition at 10 mM
phenylhydrazine
a suicide substrate
Sn2+
-
inhibits the enzyme at 1 mM, complete inhibition at 5 mM
sodium nitroprusside
-
partial
2-mercaptoethanol
-
70.3% activity remaining at 1 mM
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+
-
inhibits the enzyme at 1-5 mM, almost complete inhibition at 10 mM
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
Ca2+
-
inhibits the enzyme at 1-10 mM
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
-
85.1% activity remaining at 10 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
Hg2+
-
inhibits the enzyme strongly at 1-10 mM
Hg2+
-
complete inhibition at 1 mM
hydroxylamine
-
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
-
92.5% activity remaining 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
-
13.3% activity remaining 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
L-cysteine
-
51.8% activity remaining at 1 mM
L-cysteine
-
28% inhibition at 3 mM
Li+
-
inhibits the enzyme at 1-10 mM
Mg2+
-
inhibits the enzyme at 1-10 mM
Mn2+
-
inhibits the enzyme at 1-10 mM
Mn2+
-
marked 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+
-
inhibits the enzyme at 1-10 mM
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
Sodium azide
-
25.9% activity remaining at 1 mM
Sodium azide
-
1 mM, 72% residual activity, APX 1, 55% residual activity, APX 2
Zn2+
-
inhibits the enzyme at 1-10 mM
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
tyrosine nitration has a negative impact. No effects are observed on the chaperone function and the oligomeric status of AtAPX1
-
additional information
-
tyrosine nitration has a negative impact. No effects are observed on the chaperone function and the oligomeric status of AtAPX1
-
additional information
-
not inhibitory up to 100 mM: cyanide, azide, aminotriazole
-
additional information
-
not inhibitory: alpha,alpha-dipyridyl, EDTA
-
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Anemia, Hypochromic
Characterization of the response of in vitro cultured Myrtus communis L. plants to high concentrations of NaCl.
Anemia, Hypochromic
Divalent nutrient cations: Friend and foe during zinc stress in rice.
Bacterial Infections
Modulation of tobacco bacterial disease resistance using cytosolic ascorbate peroxidase and Cu,Zn?superoxide dismutase
Bacterial Infections
Up-regulation of antioxidants in tobacco by low concentrations of H?O? suppresses necrotic disease symptoms.
Carcinoma, Hepatocellular
Identification of APEX2 as an oncogene in liver cancer.
Cysts
Analysis of ascorbate peroxidase genes expressed in resistant and susceptible wheat lines infected by the cereal cyst nematode, Heterodera avenae.
Dehydration
Abscisic acid mediated differential growth responses of root and shoot of Vigna radiata (L.) Wilczek seedlings under water stress.
Dehydration
Antioxidant Response of Three Tillandsia Species Transplanted to Urban, Agricultural, and Industrial Areas.
Dehydration
Antioxidative protection in the inducible CAM plant Sedum album L. following the imposition of severe water stress and recovery.
Dehydration
Ascorbic acid mitigation of water stress-inhibition of root growth in association with oxidative defense in tall fescue (Festuca arundinacea Schreb.).
Dehydration
Cytological and physiological changes in orthodox maize embryos during cryopreservation.
Dehydration
Cytological and physiological changes in recalcitrant Chinese fan palm (Livistona chinensis) embryos during cryopreservation.
Dehydration
Differential proteomic responses to water stress induced by PEG in two creeping bentgrass cultivars differing in stress tolerance.
Dehydration
Effect of short-term water deficit stress on antioxidative systems in cucumber seedling roots.
Dehydration
Effect of water stress on antioxidant systems and oxidative parameters in fruits of tomato (Solanum lycopersicon L, cv. Micro-tom).
Dehydration
Effects of droplet-vitrification cryopreservation based on physiological and antioxidant enzyme activities of Brassidium shooting star orchid.
Dehydration
Effects of water stress on antioxidant enzymes of leaves and nodules of transgenic alfalfa overexpressing superoxide dismutases.
Dehydration
Effects of water-saving superabsorbent polymer on antioxidant enzyme activities and lipid peroxidation in oat (Avena sativa L.) under drought stress.
Dehydration
Implications of terminal oxidase function in regulation of salicylic acid on soybean seedling photosynthetic performance under water stress.
Dehydration
Influence of water stress on antioxidative enzymes and yield of banana cultivars and hybrids.
Dehydration
Involvement of cytosolic ascorbate peroxidase and Cu/Zn-superoxide dismutase for improved tolerance against drought stress.
Dehydration
Nitric oxide reduces hydrogen peroxide accumulation involved in water stress-induced subcellular anti-oxidant defense in maize plants.
Dehydration
Nitrogen Metabolism in Adaptation of Photosynthesis to Water Stress in Rice Grown under Different Nitrogen Levels.
Dehydration
Pretreatment with NaCl Promotes the Seed Germination of White Clover by Affecting Endogenous Phytohormones, Metabolic Regulation, and Dehydrin-Encoded Genes Expression under Water Stress.
Dehydration
Response of Chinese wampee axes and maize embryos to dehydration at different rates.
Dehydration
Role of abscissic acid in water stress-induced antioxidant defense in leaves of maize seedlings.
Dehydration
Roles of dehydrin genes in wheat tolerance to drought stress.
Dehydration
Transformation of plum plants with a cytosolic ascorbate peroxidase transgene leads to enhanced water stress tolerance.
Dehydration
Water stress-induced abscisic acid accumulation triggers the increased generation of reactive oxygen species and up-regulates the activities of antioxidant enzymes in maize leaves.
Dehydration
[Effects of exogenous betaine on physiological responses of peach tree under water stress]
Dermatitis, Phototoxic
Mg protoporphyrin monomethylester cyclase deficiency and effects on tetrapyrrole metabolism in different light conditions.
Hepatitis
Identification of APEX2 as an oncogene in liver cancer.
Hypersensitivity
Ascorbic acid in plants: biosynthesis and function.
Infections
A meta-analysis of affinity purification-mass spectrometry experimental systems used to identify eukaryotic and chlamydial proteins at the Chlamydia trachomatis inclusion membrane.
Infections
Antioxidant defense response induced by Trichoderma viride against Aspergillus niger Van Tieghem causing collar rot in groundnut (Arachis hypogaea L.).
Infections
Biochemical characterization of compatible plant-viral interaction: A case study with a Begomovirus-Kenaf host-pathosystem.
Infections
Coordinated expression of defense-related genes by TMV infection or salicylic acid treatment in tobacco.
Infections
Dengue Virus Hijacks a Noncanonical Oxidoreductase Function of a Cellular Oligosaccharyltransferase Complex.
Infections
Early response of wheat antioxidant system with special reference to Fusarium head blight stress.
Infections
Effect of alginic acid decomposing bacterium on the growth of Laminaria japonica (Phaeophyceae).
Infections
Evidences for growth-promoting and fungicidal effects of low doses of tricyclazole in barley.
Infections
Fructans Prime ROS Dynamics and Botrytis cinerea Resistance in Arabidopsis.
Infections
Glycolytic profile shift and antioxidant triggering in symbiont-free and H2O2-resistant Strigomonas culicis.
Infections
Heterologous expression of wheat TaRUB1 gene enhances disease resistance in Arabidopsis thaliana.
Infections
Organ-specific differences in endogenous phytohormone and antioxidative responses in potato upon PSTVd infection.
Infections
Ozonated water reduces susceptibility in tomato plants to Meloidogyne incognita by the modulation of the antioxidant system.
Infections
Proximity-dependent proteomics of the Chlamydia trachomatis inclusion membrane reveals functional interactions with endoplasmic reticulum exit sites.
Infections
Response of antioxidative enzymes to long-term Tomato spotted wilt virus infection and virus elimination by meristem-tip culture in two Impatiens species
Infections
Spermine and Spermidine Priming against Botrytis cinerea Modulates ROS Dynamics and Metabolism in Arabidopsis.
Infections
Temporal modulation of oxidant and antioxidative responses in Brassica carinata during ?-aminobutyric acid-induced resistance against Alternaria brassicae
Infections
The effect of Botrytis cinerea infection on the antioxidant profile of mitochondria from tomato leaves.
Infections
Up-regulation of the ascorbate-dependent antioxidative system in barley leaves during powdery mildew infection.
Iron Deficiencies
Glutathione and ascorbic acid protect Arabidopsis plants against detrimental effects of iron deficiency.
Iron Deficiencies
Understanding the Role of the Antioxidant System and the Tetrapyrrole Cycle in Iron Deficiency Chlorosis.
Iron Overload
Iron triggers a rapid induction of ascorbate peroxidase gene expression in Brassica napus.
Iron Overload
Reactive oxygen intermediates and glutathione regulate the expression of cytosolic ascorbate peroxidase during iron-mediated oxidative stress in bean.
l-ascorbate peroxidase deficiency
Apex2 is required for efficient somatic hypermutation but not for class switch recombination of immunoglobulin genes.
Liver Neoplasms
Identification of APEX2 as an oncogene in liver cancer.
Lymphoma
Apex2 is required for efficient somatic hypermutation but not for class switch recombination of immunoglobulin genes.
Magnesium Deficiency
Magnesium Deficiency and High Light Intensity Enhance Activities of Superoxide Dismutase, Ascorbate Peroxidase, and Glutathione Reductase in Bean Leaves.
Mesothelioma
Evaluation of gene expression levels in the diagnosis of lung adenocarcinoma and malignant pleural mesothelioma.
Mesothelioma, Malignant
Evaluation of gene expression levels in the diagnosis of lung adenocarcinoma and malignant pleural mesothelioma.
Neoplasms
An inverted CAV1 (caveolin 1) topology defines novel autophagy-dependent exosome secretion from prostate cancer cells.
Neoplasms
Identification of APEX2 as an oncogene in liver cancer.
Neoplasms
Protein changes in the albedo of citrus fruits on postharvesting storage.
Phytoplasma Disease
Biochemical and epigenetic changes in phytoplasma-recovered periwinkle after indole-3-butyric acid treatment.
Phytoplasma Disease
Tc-cAPX, a cytosolic ascorbate peroxidase of Theobroma cacao L. engaged in the interaction with Moniliophthora perniciosa, the causing agent of witches' broom disease.
Prostatic Neoplasms
An inverted CAV1 (caveolin 1) topology defines novel autophagy-dependent exosome secretion from prostate cancer cells.
Pulmonary Disease, Chronic Obstructive
Identification of APEX2 as an oncogene in liver cancer.
Severe Acute Respiratory Syndrome
Neutron crystallography for the elucidation of enzyme catalysis.
Starvation
Divalent nutrient cations: Friend and foe during zinc stress in rice.
Starvation
Glutathione-Mediated Regulation of ATP Sulfurylase Activity, SO42- Uptake, and Oxidative Stress Response in Intact Canola Roots.
Starvation
Sulfur Deprivation Results in Oxidative Perturbation in Chlorella sorokiniana (211/8k).
Sunburn
Photoprotection mechanism in the 'Fuji' apple peel at different levels of photooxidative sunburn.
Sunburn
Photoprotection mechanism in the Fuji apple peel at different levels of photooxidative sunburn
Virus Diseases
Evidence of oxidative stress following the viral infection of two lepidopteran insect cell lines.
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-
brenda
high expression level
brenda
during endormancy breaking, Apx activity decreases from deepest period to mid-breaking period, but then increases rapidly during ate-breaking period
brenda
-
-
brenda
-
brenda
-
-
brenda
-
brenda
-
brenda
-
55.6% relative activity to salivary gland
brenda
-
-
brenda
-
presence of two major non-plastid isozymes
brenda
high expression level
brenda
-
31.1% relative activity to salivary gland
brenda
-
-
brenda
-
20% relative activity to salivary gland
brenda
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
highest activity
brenda
-
-
brenda
-
-
brenda
-
-
brenda
GhAPX1 is highly expressed in wild-type 5-day postanthesis fibres with much lower transcript levels in the fuzzless-lintless mutant ovules. GhAPX1 expression is upregulated in response to an increase in cellular H2O2 and ethylene
brenda
-
cotton bolls
brenda
-
brenda
high expression level
brenda
green mature banana fruit approximately 110 days after anthesis, harvested from an orchard in Guangzhou, Guangdong province, China. MaMsrB2 and MaAPX1 are isolated from a banana transcriptome database. Their transcript levels in the peel during fruit ripening and senescence are investigated by quantitative real-time PCR expression analysis
brenda
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
brenda
APX6 is nearly 4fold higher in late senescing leaves of 6.5-week-old plants compared with young green leaves of 4-week-old plants
brenda
-
activity decreases during germination, strongly increases during callus induction and proliferation, and decreases during shoot and root induction
brenda
salt stressed leaves
brenda
-
-
brenda
-
-
brenda
-
-
brenda
the gene expression profile of CsAPX1 encoding ascorbate peroxidase (APX) is regulated by light/dark conditions. AsA accumulation and APX activity are suppressed by light/dark conditions
brenda
-
brenda
-
-
brenda
-
presence of two major non-plastid isozymes
brenda
-
-
brenda
highest expression level
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
blades and sheaths
brenda
-
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low expression level at blade sheath, high expression level at blade ear
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high expression level. Isoform Apx1 expression level is higher compared to isoform Apx2
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isoform Apx1 expression level is higher compared to isoform Apx2
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Populus simonii x Populus pyramidalis
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expression levels are higher in leaves than in roots or stems
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total APX activity, on a fresh weight basis, is stimulated only at 2 mM methyl viologen at 24 h, but dropps at higher doses
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young leaves contain low amounts of enzyme, in mature green leaves, small amounts of the enzyme are distributed in vascular systems, in particular in companion cells
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nodules
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nodules
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activity decreases during germination, strongly increases during callus induction and proliferation, and decreases during shoot and root induction
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nodules
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presence of two major non-plastid isozymes
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nodules
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nodules
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of seedlings. NaCl-enhanced expression of OsAPx8 in rice roots is mediated through an accumulation of abscisic acid. Na+ but not Cl- is required for enhancing OsAPx8 expression. H2O2 is not involved in the regulation of NaCl-induced OsAPx8 expression in rice roots
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of seedlings. No significant increase due to NaCl can be detected in the expression of OsAPx1
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of seedlings. No significant increase due to NaCl can be detected in the expression of OsAPx2
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of seedlings. No significant increase due to NaCl can be detected in the expression of OsAPx3
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of seedlings. No significant increase due to NaCl can be detected in the expression of OsAPx4
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of seedlings. No significant increase due to NaCl can be detected in the expression of OsAPx5
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of seedlings. No significant increase due to NaCl can be detected in the expression of OsAPx6
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of seedlings. The expression of OsAPx7 is not affected by 150 mM and 200 mM NaCl, but is 40% decreased by 300 mM NaCl
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low expression level
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nodules
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expression levels are higher in leaves than in roots or stems
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nodules
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nodules
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nodules
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nodules
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germinating
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cAPX 2 is involved in flooding stress responses in young soybean seedlings
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root of seedling, increase in enzyme activity after treatment with NaCl or H2O2, inhibition of enzyme accumulation by diphenyleneiodinium chloride or imidazole, but not by dimethylthiourea
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root. NaCl-enhanced expression of OsAPx8 in rice roots is mediated through an accumulation of abscisic acid. Na+ but not Cl- is required for enhancing OsAPx8 expression. H2O2 is not involved in the regulation of NaCl-induced OsAPx8 expression in rice roots
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root. No significant increase due to NaCl can be detected in the expression of OsAPx1
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root. No significant increase due to NaCl can be detected in the expression of OsAPx2
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root. No significant increase due to NaCl can be detected in the expression of OsAPx3
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root. No significant increase due to NaCl can be detected in the expression of OsAPx4
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root. No significant increase due to NaCl can be detected in the expression of OsAPx5
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root. No significant increase due to NaCl can be detected in the expression of OsAPx6
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root. The expression of OsAPx7 is not affected by 150 mM and 200 mM NaCl, but is 40% decreased by 300 mM NaCl
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activity decreases during germination, strongly increases during callus induction and proliferation, and decreases during shoot and root induction
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lowest expression level
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high expression level
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expression levels are higher in leaves than in roots or stems
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additional information
the constitutive expression of APX6 is restricted to old and dying cells and absent in younger tissues
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additional information
ascorbate peroxidase is not detected in dry mature seed
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additional information
ascorbate peroxidase is not detected in dry mature seed
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additional information
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ascorbate peroxidase is not detected in dry mature seed
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additional information
expression in all tissues, level of expression varies considerably
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additional information
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transcriptomic analysis, the organisms possesses kinetoplastid-specific hAPX-CCP. Gene expression shows the highest number of transcripts at 14°C and its decrease with elevated temperature
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additional information
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APX activity is highest in the leaf blades and tends to be higher in older than in younger plant parts
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additional information
eight APX isozymes are expressed differently in root, leaf, panicle, anther, pistil and seed
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additional information
eight APX isozymes are expressed differently in root, leaf, panicle, anther, pistil and seed
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additional information
eight APX isozymes are expressed differently in root, leaf, panicle, anther, pistil and seed
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additional information
eight APX isozymes are expressed differently in root, leaf, panicle, anther, pistil and seed
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additional information
eight APX isozymes are expressed differently in root, leaf, panicle, anther, pistil and seed
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additional information
eight APX isozymes are expressed differently in root, leaf, panicle, anther, pistil and seed
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additional information
eight APX isozymes are expressed differently in root, leaf, panicle, anther, pistil and seed
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additional information
eight APX isozymes are expressed differently in root, leaf, panicle, anther, pistil and seed
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additional information
eight APX isozymes are expressed differently in root, leaf, panicle, anther, pistil and seed. High expression level of isozyme OsAPX1
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additional information
eight APX isozymes are expressed differently in root, leaf, panicle, anther, pistil and seed. High expression level of isozyme OsAPX1
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additional information
eight APX isozymes are expressed differently in root, leaf, panicle, anther, pistil and seed. High expression level of isozyme OsAPX1
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additional information
eight APX isozymes are expressed differently in root, leaf, panicle, anther, pistil and seed. High expression level of isozyme OsAPX1
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additional information
eight APX isozymes are expressed differently in root, leaf, panicle, anther, pistil and seed. High expression level of isozyme OsAPX1
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additional information
eight APX isozymes are expressed differently in root, leaf, panicle, anther, pistil and seed. High expression level of isozyme OsAPX1
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additional information
eight APX isozymes are expressed differently in root, leaf, panicle, anther, pistil and seed. High expression level of isozyme OsAPX1
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additional information
eight APX isozymes are expressed differently in root, leaf, panicle, anther, pistil and seed. High expression level of isozyme OsAPX1
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additional information
eight APX isozymes are expressed differently in root, leaf, panicle, anther, pistil and seed. High expression level of isozyme OsAPX2
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additional information
eight APX isozymes are expressed differently in root, leaf, panicle, anther, pistil and seed. High expression level of isozyme OsAPX2
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additional information
eight APX isozymes are expressed differently in root, leaf, panicle, anther, pistil and seed. High expression level of isozyme OsAPX2
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additional information
eight APX isozymes are expressed differently in root, leaf, panicle, anther, pistil and seed. High expression level of isozyme OsAPX2
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additional information
eight APX isozymes are expressed differently in root, leaf, panicle, anther, pistil and seed. High expression level of isozyme OsAPX2
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additional information
eight APX isozymes are expressed differently in root, leaf, panicle, anther, pistil and seed. High expression level of isozyme OsAPX2
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additional information
eight APX isozymes are expressed differently in root, leaf, panicle, anther, pistil and seed. High expression level of isozyme OsAPX2
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additional information
eight APX isozymes are expressed differently in root, leaf, panicle, anther, pistil and seed. High expression level of isozyme OsAPX2
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additional information
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RcAPX is found in all tested tissues with highest amounts in young petioles. Enzyme RcAPX shows differential expression in different tissues at various developmental stages. RcAPX expression is significantly suppressed by galls, Galla chinensis, resulting from the galling aphid Schlechtendalia chinensis parasitizing the vein or compound leaves of Rhus chinensis
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evolution
APX belongs to the class I heme-peroxidases, isozyme AtAPX1 belongs to group I. APXs in the selected plant species show high evolutionary conservation and are able to divide into seven groups, group I to VII. Members in the groups contain abundant phosphorylation sites. Group I and VII have only protein kinase C site. Additionally, promoters of the APXs contain abundant stress-related cis-elements. APX is comprised of different isozymes, which are encoded by a multi-gene family and found in many compartments of cell
evolution
APX belongs to the class I heme-peroxidases, isozyme AtAPX2 belongs to group I. APXs in the selected plant species show high evolutionary conservation and are able to divide into seven groups, group I to VII. Members in the groups contain abundant phosphorylation sites. Group I and VII have only protein kinase C site. Additionally, promoters of the APXs contain abundant stress-related cis-elements. APX is comprised of different isozymes, which are encoded by a multi-gene family and found in many compartments of cell
evolution
APX belongs to the class I heme-peroxidases, isozyme AtAPX3 belongs to group II. APXs in the selected plant species show high evolutionary conservation and are able to divide into seven groups, group I to VII. Members in the groups contain abundant phosphorylation sites. Group I and VII have only protein kinase C site. Additionally, promoters of the APXs contain abundant stress-related cis-elements. APX is comprised of different isozymes, which are encoded by a multi-gene family and found in many compartments of cell
evolution
APX belongs to the class I heme-peroxidases, isozyme AtAPX5 belongs to group II. APXs in the selected plant species show high evolutionary conservation and are able to divide into seven groups, group I to VII. Members in the groups contain abundant phosphorylation sites. Group I and VII have only protein kinase C site. Additionally, promoters of the APXs contain abundant stress-related cis-elements. APX is comprised of different isozymes, which are encoded by a multi-gene family and found in many compartments of cell
evolution
APX belongs to the class I heme-peroxidases, isozyme AtAPX6 belongs to group V. APXs in the selected plant species show high evolutionary conservation and are able to divide into seven groups, group I to VII. Members in the groups contain abundant phosphorylation sites. Group I and VII have only protein kinase C site. Additionally, promoters of the APXs contain abundant stress-related cis-elements. APX is comprised of different isozymes, which are encoded by a multi-gene family and found in many compartments of cell
evolution
APX belongs to the class I heme-peroxidases, isozyme AtSAPX belongs to group IV. APXs in the selected plant species show high evolutionary conservation and are able to divide into seven groups, group I to VII. Members in the groups contain abundant phosphorylation sites. Group I and VII have only protein kinase C site. Additionally, promoters of the APXs contain abundant stress-related cis-elements. APX is comprised of different isozymes, which are encoded by a multi-gene family and found in many compartments of cell
evolution
APX belongs to the class I heme-peroxidases, isozyme AtTAPX belongs to group IV. APXs in the selected plant species show high evolutionary conservation and are able to divide into seven groups, group I to VII. Members in the groups contain abundant phosphorylation sites. Group I and VII have only protein kinase C site. Additionally, promoters of the APXs contain abundant stress-related cis-elements. APX is comprised of different isozymes, which are encoded by a multi-gene family and found in many compartments of cell
evolution
APX belongs to the class I heme-peroxidases, isozyme CreAPX1 belongs to group IV. APXs in the selected plant species show high evolutionary conservation and are able to divide into seven groups, group I to VII. Members in the groups contain abundant phosphorylation sites. Group I and VII have only protein kinase C site. Additionally, promoters of the APXs contain abundant stress-related cis-elements. APX is comprised of different isozymes, which are encoded by a multi-gene family and found in many compartments of cell
evolution
APX belongs to the class I heme-peroxidases, isozyme CreAPX2 belongs to group V. APXs in the selected plant species show high evolutionary conservation and are able to divide into seven groups, group I to VII. Members in the groups contain abundant phosphorylation sites. Group I and VII have only protein kinase C site. Additionally, promoters of the APXs contain abundant stress-related cis-elements. APX is comprised of different isozymes, which are encoded by a multi-gene family and found in many compartments of cell
evolution
APX belongs to the class I heme-peroxidases, isozyme CreAPX4 belongs to group VI. APXs in the selected plant species show high evolutionary conservation and are able to divide into seven groups, group I to VII. Members in the groups contain abundant phosphorylation sites. Group I and VII have only protein kinase C site. Additionally, promoters of the APXs contain abundant stress-related cis-elements. APX is comprised of different isozymes, which are encoded by a multi-gene family and found in many compartments of cell
evolution
APX belongs to the class I heme-peroxidases, isozyme CreAPXheme belongs to group III. APXs in the selected plant species show high evolutionary conservation and are able to divide into seven groups, group I to VII. Members in the groups contain abundant phosphorylation sites. Group I and VII have only protein kinase C site. Additionally, promoters of the APXs contain abundant stress-related cis-elements. APX is comprised of different isozymes, which are encoded by a multi-gene family and found in many compartments of cell
evolution
APX belongs to the class I heme-peroxidases, isozyme OsAPX1 belongs to group I. APXs in the selected plant species show high evolutionary conservation and are able to divide into seven groups, group I to VII. Members in the groups contain abundant phosphorylation sites. Group I and VII have only protein kinase C site. Additionally, promoters of the APXs contain abundant stress-related cis-elements. APX is comprised of different isozymes, which are encoded by a multi-gene family and found in many compartments of cell
evolution
APX belongs to the class I heme-peroxidases, isozyme OsAPX2 belongs to group I. APXs in the selected plant species show high evolutionary conservation and are able to divide into seven groups, group I to VII. Members in the groups contain abundant phosphorylation sites. Group I and VII have only protein kinase C site. Additionally, promoters of the APXs contain abundant stress-related cis-elements. APX is comprised of different isozymes, which are encoded by a multi-gene family and found in many compartments of cell
evolution
APX belongs to the class I heme-peroxidases, isozyme OsAPX3 belongs to group II. APXs in the selected plant species show high evolutionary conservation and are able to divide into seven groups, group I to VII. Members in the groups contain abundant phosphorylation sites. Group I and VII have only protein kinase C site. Additionally, promoters of the APXs contain abundant stress-related cis-elements. APX is comprised of different isozymes, which are encoded by a multi-gene family and found in many compartments of cell
evolution
APX belongs to the class I heme-peroxidases, isozyme OsAPX4 belongs to group II. APXs in the selected plant species show high evolutionary conservation and are able to divide into seven groups, group I to VII. Members in the groups contain abundant phosphorylation sites. Group I and VII have only protein kinase C site. Additionally, promoters of the APXs contain abundant stress-related cis-elements. APX is comprised of different isozymes, which are encoded by a multi-gene family and found in many compartments of cell
evolution
APX belongs to the class I heme-peroxidases, isozyme OsAPX5 belongs to group IV. APXs in the selected plant species show high evolutionary conservation and are able to divide into seven groups, group I to VII. Members in the groups contain abundant phosphorylation sites. Group I and VII have only protein kinase C site. Additionally, promoters of the APXs contain abundant stress-related cis-elements. APX is comprised of different isozymes, which are encoded by a multi-gene family and found in many compartments of cell
evolution
APX belongs to the class I heme-peroxidases, isozyme OsAPX6 belongs to group IV. APXs in the selected plant species show high evolutionary conservation and are able to divide into seven groups, group I to VII. Members in the groups contain abundant phosphorylation sites. Group I and VII have only protein kinase C site. Additionally, promoters of the APXs contain abundant stress-related cis-elements. APX is comprised of different isozymes, which are encoded by a multi-gene family and found in many compartments of cell
evolution
APX belongs to the class I heme-peroxidases, isozyme OsAPX7 belongs to group IV. APXs in the selected plant species show high evolutionary conservation and are able to divide into seven groups, group I to VII. Members in the groups contain abundant phosphorylation sites. Group I and VII have only protein kinase C site. Additionally, promoters of the APXs contain abundant stress-related cis-elements. APX is comprised of different isozymes, which are encoded by a multi-gene family and found in many compartments of cell
evolution
APX belongs to the class I heme-peroxidases, isozyme OsAPX8 belongs to group IV. APXs in the selected plant species show high evolutionary conservation and are able to divide into seven groups, group I to VII. Members in the groups contain abundant phosphorylation sites. Group I and VII have only protein kinase C site. Additionally, promoters of the APXs contain abundant stress-related cis-elements. APX is comprised of different isozymes, which are encoded by a multi-gene family and found in many compartments of cell
evolution
APX belongs to the class I heme-peroxidases, isozyme PpAPX-S belongs to group IV. APXs in the selected plant species show high evolutionary conservation and are able to divide into seven groups, group I to VII. Members in the groups contain abundant phosphorylation sites. Group I and VII have only protein kinase C site. Additionally, promoters of the APXs contain abundant stress-related cis-elements. APX is comprised of different isozymes, which are encoded by a multi-gene family and found in many compartments of cell
evolution
APX belongs to the class I heme-peroxidases, isozyme PpAPX2.1 belongs to group I. APXs in the selected plant species show high evolutionary conservation and are able to divide into seven groups, group I to VII. Members in the groups contain abundant phosphorylation sites. Group I and VII have only protein kinase C site. Additionally, promoters of the APXs contain abundant stress-related cis-elements. APX is comprised of different isozymes, which are encoded by a multi-gene family and found in many compartments of cell
evolution
APX belongs to the class I heme-peroxidases, isozyme PpAPX2.2 belongs to group I. APXs in the selected plant species show high evolutionary conservation and are able to divide into seven groups, group I to VII. Members in the groups contain abundant phosphorylation sites. Group I and VII have only protein kinase C site. Additionally, promoters of the APXs contain abundant stress-related cis-elements. APX is comprised of different isozymes, which are encoded by a multi-gene family and found in many compartments of cell
evolution
APX belongs to the class I heme-peroxidases, isozyme PpAPX3 belongs to group II. APXs in the selected plant species show high evolutionary conservation and are able to divide into seven groups, group I to VII. Members in the groups contain abundant phosphorylation sites. Group I and VII have only protein kinase C site. Additionally, promoters of the APXs contain abundant stress-related cis-elements. APX is comprised of different isozymes, which are encoded by a multi-gene family and found in many compartments of cell
evolution
APX belongs to the class I heme-peroxidases, isozyme PpAPX6-related belongs to group V. APXs in the selected plant species show high evolutionary conservation and are able to divide into seven groups, group I to VII. Members in the groups contain abundant phosphorylation sites. Group I and VII have only protein kinase C site. Additionally, promoters of the APXs contain abundant stress-related cis-elements. APX is comprised of different isozymes, which are encoded by a multi-gene family and found in many compartments of cell
evolution
APX belongs to the class I heme-peroxidases, isozyme PtAPX-S.1 belongs to group IV. APXs in the selected plant species show high evolutionary conservation and are able to divide into seven groups, group I to VII. Members in the groups contain abundant phosphorylation sites. Group I and VII have only protein kinase C site. Additionally, promoters of the APXs contain abundant stress-related cis-elements. APX is comprised of different isozymes, which are encoded by a multi-gene family and found in many compartments of cell
evolution
APX belongs to the class I heme-peroxidases, isozyme PtAPX-S.2 belongs to group IV. APXs in the selected plant species show high evolutionary conservation and are able to divide into seven groups, group I to VII. Members in the groups contain abundant phosphorylation sites. Group I and VII have only protein kinase C site. Additionally, promoters of the APXs contain abundant stress-related cis-elements. APX is comprised of different isozymes, which are encoded by a multi-gene family and found in many compartments of cell
evolution
APX belongs to the class I heme-peroxidases, isozyme PtAPX-TL29 belongs to group VII. APXs in the selected plant species show high evolutionary conservation and are able to divide into seven groups, group I to VII. Members in the groups contain abundant phosphorylation sites. Group I and VII have only protein kinase C site. Additionally, promoters of the APXs contain abundant stress-related cis-elements. APX is comprised of different isozymes, which are encoded by a multi-gene family and found in many compartments of cell
evolution
APX belongs to the class I heme-peroxidases, isozyme PtAPX.3 belongs to group I. APXs in the selected plant species show high evolutionary conservation and are able to divide into seven groups, group I to VII. Members in the groups contain abundant phosphorylation sites. Group I and VII have only protein kinase C site. Additionally, promoters of the APXs contain abundant stress-related cis-elements. APX is comprised of different isozymes, which are encoded by a multi-gene family and found in many compartments of cell
evolution
APX belongs to the class I heme-peroxidases, isozyme PtAPX1.1 belongs to group I. APXs in the selected plant species show high evolutionary conservation and are able to divide into seven groups, group I to VII. Members in the groups contain abundant phosphorylation sites. Group I and VII have only protein kinase C site. Additionally, promoters of the APXs contain abundant stress-related cis-elements. APX is comprised of different isozymes, which are encoded by a multi-gene family and found in many compartments of cell
evolution
APX belongs to the class I heme-peroxidases, isozyme PtAPX1.2 belongs to group I. APXs in the selected plant species show high evolutionary conservation and are able to divide into seven groups, group I to VII. Members in the groups contain abundant phosphorylation sites. Group I and VII have only protein kinase C site. Additionally, promoters of the APXs contain abundant stress-related cis-elements. APX is comprised of different isozymes, which are encoded by a multi-gene family and found in many compartments of cell
evolution
APX belongs to the class I heme-peroxidases, isozyme PtAPX2 belongs to group I. APXs in the selected plant species show high evolutionary conservation and are able to divide into seven groups, group I to VII. Members in the groups contain abundant phosphorylation sites. Group I and VII have only protein kinase C site. Additionally, promoters of the APXs contain abundant stress-related cis-elements. APX is comprised of different isozymes, which are encoded by a multi-gene family and found in many compartments of cell
evolution
APX belongs to the class I heme-peroxidases, isozyme PtAPX3 belongs to group II. APXs in the selected plant species show high evolutionary conservation and are able to divide into seven groups, group I to VII. Members in the groups contain abundant phosphorylation sites. Group I and VII have only protein kinase C site. Additionally, promoters of the APXs contain abundant stress-related cis-elements. APX is comprised of different isozymes, which are encoded by a multi-gene family and found in many compartments of cell
evolution
APX belongs to the class I heme-peroxidases, isozyme PtAPX5 belongs to group II. APXs in the selected plant species show high evolutionary conservation and are able to divide into seven groups, group I to VII. Members in the groups contain abundant phosphorylation sites. Group I and VII have only protein kinase C site. Additionally, promoters of the APXs contain abundant stress-related cis-elements. APX is comprised of different isozymes, which are encoded by a multi-gene family and found in many compartments of cell
evolution
APX belongs to the class I heme-peroxidases, isozyme PtAPX5-like belongs to group II. APXs in the selected plant species show high evolutionary conservation and are able to divide into seven groups, group I to VII. Members in the groups contain abundant phosphorylation sites. Group I and VII have only protein kinase C site. Additionally, promoters of the APXs contain abundant stress-related cis-elements. APX is comprised of different isozymes, which are encoded by a multi-gene family and found in many compartments of cell
evolution
APX belongs to the class I heme-peroxidases, isozyme PtAPX6 related belongs to group V. APXs in the selected plant species show high evolutionary conservation and are able to divide into seven groups, group I to VII. Members in the groups contain abundant phosphorylation sites. Group I and VII have only protein kinase C site. Additionally, promoters of the APXs contain abundant stress-related cis-elements. APX is comprised of different isozymes, which are encoded by a multi-gene family and found in many compartments of cell
evolution
ascorbate peroxidase (APX) is a class I heme peroxidase. Heme peroxidases catalyse the H2O2-dependent oxidation of a wide variety of substrates. The family of heme peroxidases share a common mechanism of oxidation which involves the formation of high-valent Compound I and Compound II intermediates. Ascorbate peroxidase and manganese peroxidase bind some substrates at the gamma-heme edge, others at the delta-heme edge
evolution
Euglena gracilis contains a photosynthesis-specific APX shared with other phototrophic euglenophytes, along with a putative plastidial APX acquired from and limited to Chloroplastida. Moreover, both diplonemids and euglenids encode a novel clade of peroxidases with a yet unknown function, while most kinetoplastids share a unique hAPX-CCP enzyme exhibiting both the APX and cytochrome c peroxidases (CCP) activities
evolution
gene MaAPX1 has a high homology (83.9%) with Arabidopsis thaliana gene APX1
evolution
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sequence comparison, phylogenetic analysis and tree
evolution
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the complex phylogenetic pattern, diversity, and distribution of catalase and APX in euglenozoans testify to their importance for these protists. The distribution of APX and catalase (CAT) in diplonemids is best explained by a scenario, in which the predecessor of these marine protists lacked both enzymes, which were reacquired by horizontal gene transfer from either prokaryotic or eukaryotic sources. Moreover, both diplonemids and euglenids encode a novel clade of peroxidases with a yet unknown function, while most kinetoplastids share a unique hAPX-CCP enzyme exhibiting both the APX and cytochrome c peroxidases (CCP) activities
evolution
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the complex phylogenetic pattern, diversity, and distribution of catalase and APX in euglenozoans testify to their importance for these protists. The distribution of APX and catalase (CAT) in diplonemids is best explained by a scenario, in which the predecessor of these marine protists lacked both enzymes, which were reacquired by horizontal gene transfer from either prokaryotic or eukaryotic sources. Moreover, both diplonemids and euglenids encode a novel clade of peroxidases with a yet unknown function, while most kinetoplastids share a unique hAPX-CCP enzyme exhibiting both the APX and cytochrome c peroxidases (CCP) activities
evolution
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the complex phylogenetic pattern, diversity, and distribution of catalase and APX in euglenozoans testify to their importance for these protists. The distribution of APX and catalase (CAT) in diplonemids is best explained by a scenario, in which the predecessor of these marine protists lacked both enzymes, which were reacquired by horizontal gene transfer from either prokaryotic or eukaryotic sources. Moreover, both diplonemids and euglenids encode a novel clade of peroxidases with a yet unknown function, while most kinetoplastids share a unique hAPX-CCP enzyme exhibiting both the APX and cytochrome c peroxidases (CCP) activities
malfunction
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CrAPX4 knockdown amiRNA lines show low APX activity and CrAPX4 transcript level without a change in CrAPX1 and CrAPX2 transcript levels, and monodehydroascorbate reductase (MDAR), dehydroascorbate reductase (DHAR), and glutathione reductase (GR) activities and transcript levels. Upon exposure to high-light (HL), CrAPX4 knockdown amiRNA lines show a modification in the expression of genes encoding the enzymes in the ascorbate-glutathione cycle, including an increase in transcript level of CrVTC2, a key enzyme for ascorbate (AsA) biosynthesis but a decrease in MDAR and DHAR transcription and activity after 1 h, followed by increases in reactive oxygen species production and lipid peroxidation after 6 h, and exhibit cell death after 9 h. Besides, AsA content and AsA/DHA (dehydroascorbate) ratio decrease in CrAPX4 knockdown amiRNA lines after prolonged HL treatment
malfunction
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downregulation of cytosolic ascorbate peroxidases inhibits the development of sink organs in cotton. Downregulated expression of cAPXs inhibits the development of cotton bolls, fibers, and seeds and reduces the storage capacity of the sink organs. The photosynthetic rate is suppressed in the knockout mutant plants, and the reactive oxygen species level is increased in guard cells. Overexpression of GhAPX1 has little effect on the photosynthetic characteristics of the plants. The decrease of cAPX expression in leaves increases ROS level in stomatal guard cells, leading to the decrease of stomatal aperture, which might decrease the supply of carbon dioxide and water used for photosynthesis. The downregulation of cytosolic ascorbate peroxidases (APXs) decreases the water content and increases the water loss rate in cotton leaf. There is a close relationship between the stomatal opening and the inhibition of plant growth caused by the deficiency of antioxidant enzyme in cells
malfunction
ectopic recombinant overexpression of MaAPX1 delays the detached leaf senescence induced by darkness in Arabidopsis thaliana
malfunction
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light-induced chloroplast development is enhanced in PtotAPX-overexpressing transgenic Populus tomentosa callus with lower levels of hydrogen peroxide, but is suppressed in PtotAPX antisense transgenic callus with higher levels of hydrogen peroxide
malfunction
reduced APX activity, increased H2O2 level, and altered redox state of the ascorbate pool in mature pre-senescing green leaves of the apx6 mutants correlated with the early onset of senescence. Mutants of squamosa promoter binding protein-like7 (SPL7), the master regulator of copper homeostasis and miR398 expression, have a higher APX6 level compared to the wild-type, which further increases under copper deficiency. APX6-deficient mutants prematurely induce senescence programs triggered by the transition to flowering, extended darkness, and ethylene. Mutants of SPL7 show increased levels of APX6 in as yet flowering or senescing plants. The earlier onset of senescence in the mutants is accompanied by higher levels of H2O2 compared with the wild-type and reduced ability to adjust the leaves' redox state
malfunction
stromal and thylakoid membrane-bound ascorbate peroxidases (sAPX and tAPX, respectively) knockout mutants do not exhibit a visible phenotype under high-light (HL) stress. PGR5-dependent mechanisms compensate for chloroplast APXs, and vice versa
metabolism
cytosolic ascorbate peroxidase is S-nitrosylated at the onset of programmed cell death, induced by both heat shock or hydrogen peroxide. S-nitrosylation of Apx is responsible for the rapid decrease in its activity, and the decrease in activity is a precocious event in the programmed cell death signaling pathway, occurring when no cellular death hallmarks are evident
metabolism
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chloroplasts with elaborate thylakoids can develop from proplastids in the cells of calli derived from leaf tissues of Populus tomentosa upon exposure to light. Chloroplast development is confirmed at the molecular and cellular levels and transcriptome analysis reveals that genes related to photoreceptors and photosynthesis are significantly upregulated during chloroplast development in a time-dependent manner. In light-induced chloroplast development, a key process is the removal of hydrogen peroxide, in which thylakoid-localized PtotAPX plays a major role
metabolism
enzyme ascorbate peroxidase 1 (CsAPX1) is involved in ascorbic acid (AsA) metabolism
metabolism
methionine sulfoxide reductase B regulates the activity of ascorbate peroxidase of banana fruit, proposed model of the involvement of MaMsrB2-mediated redox modification of methionine in MaAPX1 in regulating ripening and senescence, overview
metabolism
Simulated acid rain (SAR)stress (pH 3.5/2.5) destroys the redox state in rice cells and induces H2O2 excessive accumulation, and inhibits growth of rice. Exogenous Ca2+ alleviates SAR-induced inhibition on activities of APX and GR by regulating the concentration, activation, and transcription of their isozymes, and then maintains the redox level of cells and protects cells from oxidative damage, being beneficial to the growth of rice, effect of Ca2+ on contents of AsA and DHA in leaves and roots of rice under the simulated acid rain stress, overview
physiological function
-
APX is physiologically important to the metabolism of H2O2
physiological function
knockout mutant plants lacking Apx1 show high sensitivity to wounding and methyl jasmonate treatment. In the leaves of wild-type plants, H2O2 accumulates only in the vicinity of the wound, while in the leaves of the knockout mutant plants it accumulates extensively from damaged to undamaged regions. During methyl jasmonate treatment, the levels of H2O2 are much higher in the leaves of Apx1 knockout plants. Oxidative damage in the chloroplasts and nucleus is also enhanced in the leaves of apx1 knockout plants
physiological function
constitutive overexpression of APx in an amphotericin B-resistant strain prevents cells from the deleterious effect of oxidative stress, i.e., mitochondrial dysfunction and cellular death induced by amphotericin B
physiological function
-
heterologous overexpression of Apx6 increases the survival rate and reduces leaf water loss rate in Arabidopsis thaliana under drought treatment. Compared to the wild type plants, high salinity treatment reduces the concentrations of malondialdehyde, H2O2 and proline but elevates the activities of Apx, glutathione peroxidase, catalase and superoxide dismutases in the Apx6-overexpressing plants. Germination rate, cotyledon greening, and root length are improved in the transgenic under salt and water deficit conditions
physiological function
isoform Apx1-overexpressing Arabidopsis thaliana lines show increased germination rate and root length compared with wild-type under 200 mM NaCl stress treatment. Transgeneic lines display higher chlorophyll content, relative water content, total Apx activity, proline content, and lower H2O2 accumulation
physiological function
loss of Apx2 function affects the growth and development of rice seedlings, resulting in semi-dwarf seedlings, yellow-green leaves, leaf lesion mimic and seed sterility. Apx2 mutants have lower Apx activity and are sensitive to abiotic stresses. Overexpression of Apx2 increases activity and enhances stress tolerance. H2O2 and malondialdehyde levels are high in Apx2 mutants but low in overexpressing transgenic lines relative to wild-type plants after stress treatments
physiological function
overexpressing strains are significantly more infective to macrophages and cardiomyocytes, as well as in the mouse model of Chagas disease than wild-type
physiological function
transgenic tobacco plants overexpressing Apx show no significant difference in morphology under normal conditions. The transgenic plants are more resistant to drought, salt and oxidative stress conditions and show decreased H2O2 levels, increased ascorbate consumption, an increase in the NADP to NADPH ratio, and higher Apx activity
physiological function
under 150-mM NaCl stress, compared with wild-type, the overexpression of Apx in Arabidopsis increases the germination rate, the number of leaves and the rosette area. The transgenic plants have longer roots, higher total chlorophyll content, higher total Apx activity, and lower H2O2 content
physiological function
-
ascorbate peroxidase (APS) is an important antoxidant enzyme responsible for the conversion of H2O2 to H2O and O2. Role of APX in the tolerance of the boreal cushion moss Dicranum scoparium to abiotic stress
physiological function
-
ascorbate peroxidase (APX) is the key enzyme in hydrogen peroxide degradation, and may have a critical function in plant-aphid interactions. The enzyme has an essential function in the scavenging of H2O2 produced in normal metabolic conditions or under environmental stress due to drought
physiological function
ascorbate peroxidase 1 regulates ascorbic acid metabolism in fresh-cut leaves of tea plant during postharvest storage under light/dark conditions. CsAPX1 is involved in regulating AsA metabolism through effecting on the changes of AsA accumulation and APX activity in the leaves
physiological function
-
chloroplast development is a complex process that is critical to the growth and development of plants, overview. Chloroplast thylakoid ascorbate peroxidase PtotAPX plays a key role in chloroplast development from proplastids upon exposure to light in Populus tomentosa and in thylakoid development by decreasing hydrogen peroxide
physiological function
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cytosolic ascorbate peroxidases (APXs) are hydrogen peroxide (H2O2) scavenging enzymes in plants. H2O2 is a signaling molecule involved in regulating photosynthesis in plants. Cytosolic ascorbate peroxidase members provide an important guarantee to maintain photosynthetic rate
physiological function
enzyme APX6 is a modulator of ROS/redox homeostasis and signaling in aging leaves that plays an important role in developmental- and stress-induced senescence programs. Senescence marks the last step in the development of annual plants, culminating in the death of tissues, and finally, the entire organism
physiological function
-
Euglenozoa recruit APXs as detoxifying enzymes for specific molecular tasks, such as photosynthesis in euglenids and membrane-bound peroxidase activity in kinetoplastids and some diplonemids
physiological function
-
Euglenozoa recruit APXs as detoxifying enzymes for specific molecular tasks, such as photosynthesis in euglenids and membrane-bound peroxidase activity in kinetoplastids and some diplonemids. The diplonemid Rhynchopus humris shows very low APX activity despite the fact that the species apparently lacks the corresponding gene. The kinetic parameters of catalase (CAT) suggest yet another explanation for the lack of measurable activity in Rhynchopus humris. The low affinity of CAT to H2O2 implies that it is responsible for the removal of excessive ROS when their concentration is high, while high-affinity APX modulates low concentration of ROS, necessary for cell signaling
physiological function
Blastochritidia sp. P57
-
Euglenozoa recruit APXs as detoxifying enzymes for specific molecular tasks, such as photosynthesis in euglenids and membrane-bound peroxidase activity in kinetoplastids and some diplonemids. The kinetoplastid Blastochritidia sp. P57 shows very low APX activity despite the fact that the species apparently lacks the corresponding gene. The kinetic parameters of catalase (CAT) suggest yet another explanation for the lack of measurable activity in Blastocrithidia sp. P57. The low affinity of CAT to H2O2 implies that it is responsible for the removal of excessive ROS when their concentration is high, while high-affinity APX modulates low concentration of ROS, necessary for cell signaling
physiological function
-
Euglenozoa recruit APXs as detoxifying enzymes for specific molecular tasks, such as photosynthesis in euglenids and membrane-bound peroxidase activity in kinetoplastids and some diplonemids. The respiration rate does not correlate with APX activity
physiological function
Euglenozoa recruit APXs as detoxifying enzymes for specific molecular tasks, such as photosynthesis in euglenids and membrane-bound peroxidase activity in kinetoplastids and some diplonemids. The respiration rate does not correlate with APX activity
physiological function
-
Euglenozoa recruit APXs as detoxifying enzymes for specific molecular tasks, such as photosynthesis in euglenids and membrane-bound peroxidase activity in kinetoplastids and some diplonemids. The respiration rate does not correlate with APX activity
physiological function
exogenous calcium enhances rice tolerance to acid rain stress by regulating isozymes composition and transcriptional expression of ascorbate peroxidase and glutathione reductase
physiological function
hydrogen peroxide (H2O2) is one important component of ROS and able to modulate plant growth and development at low level and damage plant cells at high concentrations. Ascorbate peroxidase (APX) shows high affinity towards H2O2 and plays vital roles in H2O2-scavenging
physiological function
hydrogen peroxide (H2O2) is one important component of ROS and able to modulate plant growth and development at low level and damage plant cells at high concentrations. Ascorbate peroxidase (APX) shows high affinity towards H2O2 and plays vital roles in H2O2-scavenging
physiological function
hydrogen peroxide (H2O2) is one important component of ROS and able to modulate plant growth and development at low level and damage plant cells at high concentrations. Ascorbate peroxidase (APX) shows high affinity towards H2O2 and plays vital roles in H2O2-scavenging
physiological function
hydrogen peroxide (H2O2) is one important component of ROS and able to modulate plant growth and development at low level and damage plant cells at high concentrations. Ascorbate peroxidase (APX) shows high affinity towards H2O2 and plays vital roles in H2O2-scavenging
physiological function
hydrogen peroxide (H2O2) is one important component of ROS and able to modulate plant growth and development at low level and damage plant cells at high concentrations. Ascorbate peroxidase (APX) shows high affinity towards H2O2 and plays vital roles in H2O2-scavenging
physiological function
-
isozyme CrAPX4 induction together with its association with the modulation of MDAR and DHAR expression for AsA regeneration is critical for Chlamydomonas to cope with photooxidative stress. APX is a central enzyme for ROS scavenging in plants can be induced under abiotic and biotic stresses
physiological function
MaAPX1 interacts with methionine sulfoxide reductase B2 (MsrB2) in bananas. Enzyme MaAPX1 might be a target of MaMsrB2 by Co-IP and mass spectrum techniques in banana fruit. The redox state of methionine in MaAPX1 is critical to its activity, and MaMsrB2 can regulate the redox state and activity of MaAPX1. Among the antioxidant enzymes, APX plays a crucial role in scavenging H2O2 by catalyzing the conversion of H2O2 to H2O and O2, using ascorbic acid as the electron donor. APX has a higher affinity than does catalase for H2O2 and contributes maximally to H2O2 detoxification in chloroplasts, cytosol, mitochondria, and peroxisomes, as well as in the apoplastic space. APX is involved in the physiological and developmental response, such as seed germination, leaf senescence, and programmed cell death. APX also participates in environmental stresses in plants, including drought, salt, chilling, photo-oxidative stress, and high temperature. MaAPX 1 might be involved in ripening and senescence in relation to oxidative stress
physiological function
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recombinant overexpression of celery enzyme AgAPX1 in Arabidopsis thaliana positively regulates drought tolerance by regulating the stomata aperture, physiological changes in Arabidopsis leaves exposed to drought stress, phenotype, overview. The AgAPX1 gene seems to be involved in the response of celery to drought stress. The response of the AgAPX1 gene to adversity may be attributed to the conservation of APX sequences among different species
physiological function
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role of Musa paradisiaca ascorbate peroxidase in the transformation of methyl phenyl sulfide to its sulfoxide
physiological function
stromal and thylakoid membrane-bound ascorbate peroxidases (sAPX and tAPX, respectively) are major H2O2-scavenging enzymes in chloroplasts. PGR5-dependent mechanisms compensate for chloroplast APXs, and vice versa under high-light stress
physiological function
the ascorbate peroxidase (APX) derived from Cyanidioschyzon merolae, a primitive red alga living in high temperature and acidic environments (42°C, pH 2.5), has greater anti-oxidative capacity than similar peroxidases occurring in other plants. Cyanidioschyzon merolae-derived APX (cAPX) expressed in mammalian cells increases cellular antioxidative capacity. Heat and H2O2 stimulation results in ROS production. cAPX-expressing cells are more tolerant to oxidative stress induced by heat, H2O2, and acid stimulations than control cells lacking cAPX
physiological function
the ascorbate-glutathione cycle is a pivotal antioxidant system involved in the regulation of H2O2 levels. Ascorbate peroxidase, being an important enzymatic antioxidant of this cycle, catalyzes the reduction of H2O2 to water using ascorbate as a specific electron donor. Cytosolic APX1 from Arabidopsis thaliana (AtAPX1) is crucial for tuning the regulation of H2O2, playing a key role in providing acclimation to a combination of heat and drought stress. Enzyme AtAPX1 plays a dual role behaving both as a regular peroxidase and a chaperone molecule, as the latter with the ability to inhibit the thermal aggregation of malate dehydrogenase (MDH), a heat-sensitive substrate. The dual activity of AtAPX1 is strongly related to its structural status. Abiotic stresses, such as heat and salt, regulate this dual function and structural status of AtAPX1 through the association and dissociation of APX proteins, respectively. The main dimeric form of the AtAPX1 protein shows the highest peroxidase activity, whereas the HMW form exhibits the highest chaperone activity. S-nitrosylation and S-sulfhydration positively regulate the peroxidase activity, whereas tyrosine nitration has a negative impact. No effects are observed on the chaperone function and the oligomeric status of AtAPX1
physiological function
-
the ascorbate-glutathione cycle is a pivotal antioxidant system involved in the regulation of H2O2 levels. Ascorbate peroxidase, being an important enzymatic antioxidant of this cycle, catalyzes the reduction of H2O2 to water using ascorbate as a specific electron donor. Cytosolic APX1 from Arabidopsis thaliana (AtAPX1) is crucial for tuning the regulation of H2O2, playing a key role in providing acclimation to a combination of heat and drought stress. Enzyme AtAPX1 plays a dual role behaving both as a regular peroxidase and a chaperone molecule, as the latter with the ability to inhibit the thermal aggregation of malate dehydrogenase (MDH), a heat-sensitive substrate. The dual activity of AtAPX1 is strongly related to its structural status. Abiotic stresses, such as heat and salt, regulate this dual function and structural status of AtAPX1 through the association and dissociation of APX proteins, respectively. The main dimeric form of the AtAPX1 protein shows the highest peroxidase activity, whereas the HMW form exhibits the highest chaperone activity. S-nitrosylation and S-sulfhydration positively regulate the peroxidase activity, whereas tyrosine nitration has a negative impact. No effects are observed on the chaperone function and the oligomeric status of AtAPX1
-
additional information
abiotic stress modulates structural changes in AtAPX1 protein and function in vivo. The recombinant AtAPX1 protein shows oligomeric forms besides the major dimeric form, and these different forms appear to play varying roles depending on the structural status of the protein. The protein exhibits a transition from dimeric units to HMW complexes under heat stress, whereas the HMW complexes are dissociated under salt stress
additional information
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abiotic stress modulates structural changes in AtAPX1 protein and function in vivo. The recombinant AtAPX1 protein shows oligomeric forms besides the major dimeric form, and these different forms appear to play varying roles depending on the structural status of the protein. The protein exhibits a transition from dimeric units to HMW complexes under heat stress, whereas the HMW complexes are dissociated under salt stress
additional information
bioinformatics methods and public databases are used to evaluate the physicochemical properties, conserved motifs, potential modifications and cis-elements in all the APXs, and protein-protein network and expression profiles of rice APX isozymes, and three-dimensional modeling using the enzyme structure (PDB ID 1apx), overview
additional information
bioinformatics methods and public databases are used to evaluate the physicochemical properties, conserved motifs, potential modifications and cis-elements in all the APXs, and protein-protein network and expression profiles of rice APX isozymes, and three-dimensional modeling using the enzyme structure (PDB ID 1apx), overview
additional information
bioinformatics methods and public databases are used to evaluate the physicochemical properties, conserved motifs, potential modifications and cis-elements in all the APXs, and protein-protein network and expression profiles of rice APX isozymes, and three-dimensional modeling using the enzyme structure (PDB ID 1apx), overview
additional information
bioinformatics methods and public databases are used to evaluate the physicochemical properties, conserved motifs, potential modifications and cis-elements in all the APXs, and protein-protein network and expression profiles of rice APX isozymes, and three-dimensional modeling using the enzyme structure (PDB ID 1apx), overview
additional information
bioinformatics methods and public databases are used to evaluate the physicochemical properties, conserved motifs, potential modifications and cis-elements in all the APXs, and protein-protein network and expression profiles of rice APX isozymes, and three-dimensional modeling using the enzyme structure (PDB ID 1apx), overview
additional information
bioinformatics methods and public databases are used to evaluate the physicochemical properties, conserved motifs, potential modifications and cis-elements in all the APXs, and protein-protein network and expression profiles of rice APX isozymes, and three-dimensional modeling using the enzyme structure (PDB ID 1apx), overview
additional information
bioinformatics methods and public databases are used to evaluate the physicochemical properties, conserved motifs, potential modifications and cis-elements in all the APXs, and protein-protein network and expression profiles of rice APX isozymes, and three-dimensional modeling using the enzyme structure (PDB ID 1apx), overview
additional information
bioinformatics methods and public databases are used to evaluate the physicochemical properties, conserved motifs, potential modifications and cis-elements in all the APXs, and protein-protein network and expression profiles of rice APX isozymes, and three-dimensional modeling using the enzyme structure (PDB ID 1apx), overview
additional information
bioinformatics methods and public databases are used to evaluate the physicochemical properties, conserved motifs, potential modifications and cis-elements in all the APXs, and protein-protein network and expression profiles of rice APX isozymes, and three-dimensional modeling using the enzyme structure (PDB ID 1iyn), overview
additional information
bioinformatics methods and public databases are used to evaluate the physicochemical properties, conserved motifs, potential modifications and cis-elements in all the APXs, and protein-protein network and expression profiles of rice APX isozymes, and three-dimensional modeling using the enzyme structure (PDB ID 1iyn), overview
additional information
bioinformatics methods and public databases are used to evaluate the physicochemical properties, conserved motifs, potential modifications and cis-elements in all the APXs, and protein-protein network and expression profiles of rice APX isozymes, and three-dimensional modeling using the enzyme structure (PDB ID 1iyn), overview
additional information
bioinformatics methods and public databases are used to evaluate the physicochemical properties, conserved motifs, potential modifications and cis-elements in all the APXs, and protein-protein network and expression profiles of rice APX isozymes, and three-dimensional modeling using the enzyme structure (PDB ID 1iyn), overview
additional information
bioinformatics methods and public databases are used to evaluate the physicochemical properties, conserved motifs, potential modifications and cis-elements in all the APXs, and protein-protein network and expression profiles of rice APX isozymes, and three-dimensional modeling using the enzyme structure (PDB ID 1iyn), overview
additional information
bioinformatics methods and public databases are used to evaluate the physicochemical properties, conserved motifs, potential modifications and cis-elements in all the APXs, and protein-protein network and expression profiles of rice APX isozymes, and three-dimensional modeling using the enzyme structure (PDB ID 1iyn), overview
additional information
bioinformatics methods and public databases are used to evaluate the physicochemical properties, conserved motifs, potential modifications and cis-elements in all the APXs, and protein-protein network and expression profiles of rice APX isozymes, and three-dimensional modeling using the enzyme structure (PDB ID 1iyn), overview
additional information
bioinformatics methods and public databases are used to evaluate the physicochemical properties, conserved motifs, potential modifications and cis-elements in all the APXs, and protein-protein network and expression profiles of rice APX isozymes, and three-dimensional modeling using the enzyme structure (PDB ID 1iyn), overview
additional information
bioinformatics methods and public databases are used to evaluate the physicochemical properties, conserved motifs, potential modifications and cis-elements in all the APXs, and protein-protein network and expression profiles of rice APX isozymes, and three-dimensional modeling using the enzyme structure (PDB ID 5jqr), overview
additional information
bioinformatics methods and public databases are used to evaluate the physicochemical properties, conserved motifs, potential modifications and cis-elements in all the APXs, and protein-protein network and expression profiles of rice APX isozymes, and three-dimensional modeling using the enzyme structure (PDB ID 5jqr), overview
additional information
bioinformatics methods and public databases are used to evaluate the physicochemical properties, conserved motifs, potential modifications and cis-elements in all the APXs, and protein-protein network and expression profiles of rice APX isozymes, and three-dimensional modeling using the enzyme structure (PDB ID 5jqr), overview
additional information
bioinformatics methods and public databases are used to evaluate the physicochemical properties, conserved motifs, potential modifications and cis-elements in all the APXs, and protein-protein network and expression profiles of rice APX isozymes, and three-dimensional modeling using the enzyme structure (PDB ID 5jqr), overview
additional information
bioinformatics methods and public databases are used to evaluate the physicochemical properties, conserved motifs, potential modifications and cis-elements in all the APXs, and protein-protein network and expression profiles of rice APX isozymes, and three-dimensional modeling using the enzyme structure (PDB ID 5jqr), overview
additional information
bioinformatics methods and public databases are used to evaluate the physicochemical properties, conserved motifs, potential modifications and cis-elements in all the APXs, and protein-protein network and expression profiles of rice APX isozymes, and three-dimensional modeling using the enzyme structure (PDB ID 5jqr), overview
additional information
bioinformatics methods and public databases are used to evaluate the physicochemical properties, conserved motifs, potential modifications and cis-elements in all the APXs, and protein-protein network and expression profiles of rice APX isozymes, and three-dimensional modeling using the enzyme structure (PDB ID 5jqr), overview
additional information
bioinformatics methods and public databases are used to evaluate the physicochemical properties, conserved motifs, potential modifications and cis-elements in all the APXs, and protein-protein network and expression profiles of rice APX isozymes, and three-dimensional modeling using the enzyme structure (PDB ID 5jqr), overview
additional information
-
bioinformatics methods and public databases are used to evaluate the physicochemical properties, conserved motifs, potential modifications and cis-elements in all the APXs, and protein-protein network and expression profiles of rice APX isozymes, modeling, overview
additional information
bioinformatics methods and public databases are used to evaluate the physicochemical properties, conserved motifs, potential modifications and cis-elements in all the APXs, and protein-protein network and expression profiles of rice APX isozymes, modeling, overview
additional information
bioinformatics methods and public databases are used to evaluate the physicochemical properties, conserved motifs, potential modifications and cis-elements in all the APXs, and protein-protein network and expression profiles of rice APX isozymes, modeling, overview
additional information
bioinformatics methods and public databases are used to evaluate the physicochemical properties, conserved motifs, potential modifications and cis-elements in all the APXs, and protein-protein network and expression profiles of rice APX isozymes, modeling, overview
additional information
-
bioinformatics methods and public databases are used to evaluate the physicochemical properties, conserved motifs, potential modifications and cis-elements in all the APXs, and protein-protein network and expression profiles of rice APX isozymes, modeling, overview
additional information
bioinformatics methods and public databases are used to evaluate the physicochemical properties, conserved motifs, potential modifications and cis-elements in all the APXs, and protein-protein network and expression profiles of rice APX isozymes, modeling, overview
additional information
bioinformatics methods and public databases are used to evaluate the physicochemical properties, conserved motifs, potential modifications and cis-elements in all the APXs, and protein-protein network and expression profiles of rice APX isozymes, modeling, overview
additional information
bioinformatics methods and public databases are used to evaluate the physicochemical properties, conserved motifs, potential modifications and cis-elements in all the APXs, and protein-protein network and expression profiles of rice APX isozymes, modeling, overview
additional information
bioinformatics methods and public databases are used to evaluate the physicochemical properties, conserved motifs, potential modifications and cis-elements in all the APXs, and protein-protein network and expression profiles of rice APX isozymes, modeling, overview
additional information
bioinformatics methods and public databases are used to evaluate the physicochemical properties, conserved motifs, potential modifications and cis-elements in all the APXs, and protein-protein network and expression profiles of rice APX isozymes, modeling, overview
additional information
bioinformatics methods and public databases are used to evaluate the physicochemical properties, conserved motifs, potential modifications and cis-elements in all the APXs, and protein-protein network and expression profiles of rice APX isozymes, modeling, overview
additional information
bioinformatics methods and public databases are used to evaluate the physicochemical properties, conserved motifs, potential modifications and cis-elements in all the APXs, and protein-protein network and expression profiles of rice APX isozymes, modeling, overview
additional information
bioinformatics methods and public databases are used to evaluate the physicochemical properties, conserved motifs, potential modifications and cis-elements in all the APXs, and protein-protein network and expression profiles of rice APX isozymes, modeling, overview
additional information
bioinformatics methods and public databases are used to evaluate the physicochemical properties, conserved motifs, potential modifications and cis-elements in all the APXs, and protein-protein network and expression profiles of rice APX isozymes, modeling, overview
additional information
bioinformatics methods and public databases are used to evaluate the physicochemical properties, conserved motifs, potential modifications and cis-elements in all the APXs, and protein-protein network and expression profiles of rice APX isozymes, modeling, overview
additional information
bioinformatics methods and public databases are used to evaluate the physicochemical properties, conserved motifs, potential modifications and cis-elements in all the APXs, and protein-protein network and expression profiles of rice APX isozymes, modeling, overview
additional information
bioinformatics methods and public databases are used to evaluate the physicochemical properties, conserved motifs, potential modifications and cis-elements in all the APXs, and protein-protein network and expression profiles of rice APX isozymes, modeling, overview
additional information
bioinformatics methods and public databases are used to evaluate the physicochemical properties, conserved motifs, potential modifications and cis-elements in all the APXs, and protein-protein network and expression profiles of rice APX isozymes, modeling, overview
additional information
bioinformatics methods and public databases are used to evaluate the physicochemical properties, conserved motifs, potential modifications and cis-elements in all the APXs, and protein-protein network and expression profiles of rice APX isozymes, modeling, overview
additional information
bioinformatics methods and public databases are used to evaluate the physicochemical properties, conserved motifs, potential modifications and cis-elements in all the APXs, and protein-protein network and expression profiles of rice APX isozymes, modeling, overview
additional information
bioinformatics methods and public databases are used to evaluate the physicochemical properties, conserved motifs, potential modifications and cis-elements in all the APXs, and protein-protein network and expression profiles of rice APX isozymes, modeling, overview
additional information
bioinformatics methods and public databases are used to evaluate the physicochemical properties, conserved motifs, potential modifications and cis-elements in all the APXs, and protein-protein network and expression profiles of rice APX isozymes, modeling, overview
additional information
bioinformatics methods and public databases are used to evaluate the physicochemical properties, conserved motifs, potential modifications and cis-elements in all the APXs, and protein-protein network and expression profiles of rice APX isozymes, modeling, overview
additional information
bioinformatics methods and public databases are used to evaluate the physicochemical properties, conserved motifs, potential modifications and cis-elements in all the APXs, and protein-protein network and expression profiles of rice APX isozymes, modeling, overview
additional information
bioinformatics methods and public databases are used to evaluate the physicochemical properties, conserved motifs, potential modifications and cis-elements in all the APXs, and protein-protein network and expression profiles of rice APX isozymes, modeling, overview
additional information
bioinformatics methods and public databases are used to evaluate the physicochemical properties, conserved motifs, potential modifications and cis-elements in all the APXs, and protein-protein network and expression profiles of rice APX isozymes, modeling, overview
additional information
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possible substrate binding sites include His42, His162 and Asp20, substrate docking study
additional information
the coding sequence of APX6 is a potential target of miR398, which is a key regulator of copper redistribution
additional information
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the enzyme contains a H2O2 binding domain, the critical residues that coordinate binding of H2O2 by APX are R158,W161, and H162(numbering according to the chloroplastic ascorbate peroxidase from tobacco plants)
additional information
the enzyme contains a H2O2 binding domain, the critical residues that coordinate binding of H2O2 by APX are R158,W161, and H162(numbering according to the chloroplastic ascorbate peroxidase from tobacco plants)
additional information
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the enzyme contains a H2O2 binding domain, the critical residues that coordinate binding of H2O2 by APX are R158,W161, and H162(numbering according to the chloroplastic ascorbate peroxidase from tobacco plants)
additional information
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the enzyme contains a H2O2 binding domain, the critical residues that coordinate binding of H2O2 by APX are R158,W161, and H162(numbering according to the chloroplastic ascorbate peroxidase from tobacco plants). Enzyme domain structure, overview
additional information
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abiotic stress modulates structural changes in AtAPX1 protein and function in vivo. The recombinant AtAPX1 protein shows oligomeric forms besides the major dimeric form, and these different forms appear to play varying roles depending on the structural status of the protein. The protein exhibits a transition from dimeric units to HMW complexes under heat stress, whereas the HMW complexes are dissociated under salt stress
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C25S
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kcat/Km for L-ascorbate is 5.4fold lower than wild-type value. kcat/KM for H2O2 is 2.1fold lower than wild-type value. In contrast to wild-type enzyme, the mutant enzyme retains more than 90% of the initial activity after incubation for 10 min with the radical scavenger 2,2,6,6-tetramethylpiperidinyl-1-oxy and H2O2
C25S/C121S
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kcat/Km for L-ascorbate is 4.5fold lower than wild-type value. kcat/KM for H2O2 is 2.1fold lower than wild-type value. In contrast to wild-type enzyme, the mutant enzyme retains more than 90% of the initial activity after incubation for 10 min with the radical scavenger 2,2,6,6-tetramethylpiperidinyl-1-oxy and H2O2
W41A
the mutant is a six-coordinate heme peroxidase which has bis-histidine coordination, like a cytochrome, but that is catalytically active because the distal histidine reversibly dissociates to form a five-coordinate heme in response to binding of hydrogen peroxide
W208F
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the optical spectrum of the W208F mutant closely resembles that of wild type LmAPX at pH 7.5 in the absence of ascorbate. W208F mutant causes a spectral red shift from high spin to low spin, indicating that the mutant can react with H2O2. Cytochrome c binding affinity to the enzyme does not alter after mutation. The mutant is 1000times less active than the wild type in cytochrome c oxidation
W208Y
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mutant shows low spin hem. The mutant does not react with H2O2
M36Q
site-directed mutagenesis, mimicking sulfoxidation by mutating Met36 to Gln also decreases its activity in vitro and in vivo, whereas substitution of Met36 with Val36 to mimic the blocking of sulfoxidation has little effect on APX activity. Mimicking sulfoxidation of Met36 hinders the formation of compound I, the first intermediate between APX and H2O2
C126A
kcat/KM for L-ascorbate is 1.4fold higher than wild-type enzyme. kcat/Km for H2O2 is 1.7fold lower than wild-type enzyme
C26S/C126A
kcat/KM for L-ascorbate is 1.3fold lower than wild-type enzyme. kcat/Km for H2O2 is 2.5fold lower than wild-type enzyme
C26S/W35F/C126A
kcat/KM for L-ascorbate is 1.6fold than wild-type enzyme. kcat/Km for H2O2 is 3.4fold lower than wild-type enzyme. Mutant shows increased tolerance to H2O2 (retains 50% of the initial activity after H2O2 treatment for 3 min) compared to wild-type enzyme (half-time of inactivation is less than 10 sec)
R172S
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negligible ascorbate peroxidase activity, but shows near wild type activity toward other aromatic substrates
A143P
site-directed mutagenesis of the delta-site of substrate oxidation, the electronic absorption spectra and dissociation constants for binding of cyanide and azide to the isolated heme are not significantly different for the mutant compared to wild-type, also the rate constants in the peroxidase reaction mechanism are not significantly affected by the replacement of A134 by proline. The insertion of a proline does not substantially alter the product distribution in APX
C32S
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the mutation leads to approximately 70% drop in ascorbate peroxidase activity with no effect on guaiacol peroxidase activity, these results indicate that uncharged aromatic substrates and the anionic ascorbate molecule interact with different sites on the enzyme
H42A
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inactive, partial recovery of activity by addition of exogenous imidazoles
H42E
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decrease in kcat- and Km-value
S160M
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expression of apo-protein in Escherichia coli, reconstitution with exogenous heme, gives kinetic properties similar to wild-type enzyme
W41A
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the mutation enables the efficient conversion of recombinant enzyme into a stereoselective oxidizing agent for sulfides
D207A
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site-directed mutagenesis, the mutant retains 18.5% activity of the wild-type activity
H162L
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site-directed mutagenesis, the mutant retains 24.2% activity of the wild-type activity
H42L
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site-directed mutagenesis, the mutant retains 23.5% activity of the wild-type activity
CCP2APX
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residues 30-42, LREDDEYDNYIGY, of wild-type CCP are replaced with residues 27-32, IAEKKC, of APX in order to introduce the ascorbate-binding loop, a N184R point mutation is added
CCP2APX/F191
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in order to enable CCP2APX to form a porphyrin pi-cation radical during catalysis, Trp191 is converted to Phe
W233F
complete loss of cytochrome c-dependent activity
K14D/W41F/E112K/A134P
APEX2, i.e. engineered mutant of APX. APEX2 fused to a protein of interest covalently tags nearby proteins with biotin-phenol when H2O2 is added. High osmolarity and disruption of cell wall integrity permits live-cell biotin labeling in Schizosaccharomyces pombe and Saccharomyces cerevisiae, respectively. APEX2 permits targeted and proximity-dependent labeling of proteins
K14D/W41F/E112K/A134P
i.e. APEX2, engineered mutant of APX used for biotinylation of neighboring endogenous proteins. APEX labeling functions effectively in multiple Drosophila melanogaster tissues for different subcellular compartments and maps the mitochondrial matrix proteome of Drosophila muscle in different physiological conditions
C26S
kcat/KM for L-ascorbate is 1.8fold lower than wild-type enzyme. kcat/Km for H2O2 is 3.1fold lower than wild-type enzyme
C26S
kcat/Km for L-ascorbate is 1.8fold lower than wild-type value. kcat/KM for H2O2 is 3.1fold lower than wild-type value. In contrast to wild-type enzyme, the mutant enzyme retains 60% of the initial activity after incubation for 10 min with the radical scavenger 2,2,6,6-tetramethylpiperidinyl-1-oxy and H2O2
W35F
kcat/KM for L-ascorbate is 2.6fold higher than wild-type enzyme. kcat/Km for H2O2 is 2.3fold lower than wild-type enzyme
W35F
mutation does not cause a significant change in the structure of tsAPX. Mutation increases H2O2 tolerance. 2.3fold decrease in KM-value for L-ascorbate. 4.3fold increase in Km-value for H2O2
additional information
expression with hyperacidic fusion partners such as C-end tail of human alpha-synuclein, C-end tails of Arabidopsis tubulins, TUA2 and TUB3, Escherichia coli msyB and C-end tail of Escherichia coli yjgD efficiently improves the thermostability and prevents thermal inactivation of APX1 with an elevated heat tolerance of at least 2°C
additional information
expression analysis of cytosolic APX isozymes in recombinant Nicotiana benthamiana shows that only APX6 displays a gradual increase in expression along the leaf blade with about a 4 and a 30fold higher level in the mid and tip sections, respectively, compared with the base. The changes in the level of APX6 correlate with the changes in the expression of the senescence marker gene SAG12. The age-dependent activation of the APX6 promoter is proven by APX6pro::GUS expression in leaves at different ages of the plants, phenotypes, detailed overview
additional information
generation of stromal and thylakoid membrane-bound ascorbate peroxidases (sAPX and tAPX, respectively) knockout mutants, exhibiting no visible phenotype under high-light (HL) stress. The Arabidopsis thaliana sapx/tapx double mutant is crossed with a proton gradient regulation 5 (pgr5) single mutant, wherein both DELTApH-dependent mechanisms are impaired. The sapx/tapx/pgr5 triple mutant exhibits extreme sensitivity to HL compared with its parental lines. This phenotype is consistent with cellular redox perturbations and enhanced expression of many oxidative stress-responsive genes. These findings demonstrate that the PGR5-dependent mechanisms compensate for chloroplast APXs, and vice versa. The failure of induction of non-photochemical quenching in pgr5 (because of the limitation in DELTApH formation) is partially recovered in sapx/tapx/pgr5 mutants. This recovery is dependent on the NADH dehydrogenase-like complex-dependent pathway for cyclic electron flow around photosystem I
additional information
generation of stromal and thylakoid membrane-bound ascorbate peroxidases (sAPX and tAPX, respectively) knockout mutants, exhibiting no visible phenotype under high-light (HL) stress. The Arabidopsis thaliana sapx/tapx double mutant is crossed with a proton gradient regulation 5 (pgr5) single mutant, wherein both DELTApH-dependent mechanisms are impaired. The sapx/tapx/pgr5 triple mutant exhibits extreme sensitivity to HL compared with its parental lines. This phenotype is consistent with cellular redox perturbations and enhanced expression of many oxidative stress-responsive genes. These findings demonstrate that the PGR5-dependent mechanisms compensate for chloroplast APXs, and vice versa. The failure of induction of non-photochemical quenching in pgr5 (because of the limitation in DELTApH formation) is partially recovered in sapx/tapx/pgr5 mutants. This recovery is dependent on the NADH dehydrogenase-like complex-dependent pathway for cyclic electron flow around photosystem I
additional information
overexpression CsAPX1 in Arabidopsis thaliana indicates that the decrease of AsA content and APX activity in transgenic lines is less significant than that of the wild-type during postharvest storage under light/dark conditions
additional information
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overexpression CsAPX1 in Arabidopsis thaliana indicates that the decrease of AsA content and APX activity in transgenic lines is less significant than that of the wild-type during postharvest storage under light/dark conditions
additional information
expression of Cyanidioschyzon merolae-derived APX (cAPX) in mammalian cells increases cellular antioxidative capacity. Heat and H2O2 stimulation results in ROS production. cAPX-expressing cells are more tolerant to oxidative stress induced by heat, H2O2, and acid stimulations than control cells lacking cAPX
additional information
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expression of Cyanidioschyzon merolae-derived APX (cAPX) in mammalian cells increases cellular antioxidative capacity. Heat and H2O2 stimulation results in ROS production. cAPX-expressing cells are more tolerant to oxidative stress induced by heat, H2O2, and acid stimulations than control cells lacking cAPX
additional information
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generation of transgenic cotton with changes of endogenous ROS by overexpressing or suppressing the expression of cytosolic ascorbate peroxidases (APXs). Downregulation of cytosolic ascorbate peroxidases inhibits the development of sink organs in Gossipium hirsutum. Plant growth and plant size, including plant heights and leaf sizes (lengths and widths), are seriously reduced in the cAPX-suppressed cottons compared to wild-type plants, phenotypes, detailed overview. Downregulated expression of cAPXs inhibits the development of cotton bolls, fibers, and seeds and reduces the storage capacity of the sink organs. The photosynthetic rate is suppressed in the mutant plants. Overexpression of GhAPX1 has little effect on the photosynthetic characteristics of the plants, except that the transpiration rate (Trmmol) and leaf surface temperature (CTleaf) are lower than in the control plant. The downregulation of cytosolic ascorbate peroxidases (APXs) decreases the water content and increases the water loss rate in cotton leaf
additional information
expression with hyperacidic fusion partners such as C-end tail of human alpha-synuclein, C-end tails of Arabidopsis tubulins, TUA2 and TUB3, Escherichia coli msyB and C-end tail of Escherichia coli yjgD efficiently improves the thermostability and prevents thermal inactivation of APX1 with an elevated heat tolerance of at least 2°C
additional information
-
expression with hyperacidic fusion partners such as C-end tail of human alpha-synuclein, C-end tails of Arabidopsis tubulins, TUA2 and TUB3, Escherichia coli msyB and C-end tail of Escherichia coli yjgD efficiently improves the thermostability and prevents thermal inactivation of APX1 with an elevated heat tolerance of at least 2°C
additional information
attempts to decrease heme accessibility through introduction of a Phe residue at position134 are unsuccessful because the A134F variant is isolated as the apoform from Escherichia coli and reconstitution protocols with exogenous heme do not generate catalytically active enzyme
additional information
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overexpression or suppression of PtoAPX in Populus tomentosa callus. Light-induced chloroplast development is enhanced in PtotAPX-overexpressing transgenic Populus tomentosa callus with lower levels of hydrogen peroxide, but is suppressed in PtotAPX antisense transgenic callus with higher levels of hydrogen peroxide. The suppression of light-induced chloroplast development in PtotAPX antisense transgenic callus is relieved by the exogenous reactive oxygen species scavenging agent N,N'-dimethylthiourea (DMTU)
additional information
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mutant lacking activity of isozyme TaAPX-6B, reduction of total enzymic activity by 40%, mutants show significantly reduced photosynthetic activity and biomass accumulation when grown at high-light intensity photosystem II electron transfer, but no oxidative damage
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APX is comprised of different isoenzymes, which are encoded by a multi-gene family APX1 DNA and amino acid sequence analysis, sequence comparisons and phylogenetic analysis and tree, conserved cis-regulatory elements in the promoters of the APX isozyme, transcriptional profiles of the rice isozymes, overview
APX is comprised of different isoenzymes, which are encoded by a multi-gene family, APX2 DNA and amino acid sequence analysis, sequence comparisons and phylogenetic analysis and tree, conserved cis-regulatory elements in the promoters of the APX isozyme, transcriptional profiles of the rice isozymes, overview
APX is comprised of different isoenzymes, which are encoded by a multi-gene family, APX3 DNA and amino acid sequence analysis, sequence comparisons and phylogenetic analysis and tree, conserved cis-regulatory elements in the promoters of the APX isozyme, transcriptional profiles of the rice isozymes, overview
APX is comprised of different isoenzymes, which are encoded by a multi-gene family, APX4 DNA and amino acid sequence analysis, sequence comparisons and phylogenetic analysis and tree, conserved cis-regulatory elements in the promoters of the APX isozyme, transcriptional profiles of the rice isozymes, overview
APX is comprised of different isoenzymes, which are encoded by a multi-gene family, APX5 DNA and amino acid sequence analysis, sequence comparisons and phylogenetic analysis and tree, conserved cis-regulatory elements in the promoters of the APX isozyme, transcriptional profiles of the rice isozymes, overview
APX is comprised of different isoenzymes, which are encoded by a multi-gene family, APX6 DNA and amino acid sequence analysis, sequence comparisons and phylogenetic analysis and tree, conserved cis-regulatory elements in the promoters of the APX isozyme, transcriptional profiles of the rice isozymes, overview
APX is comprised of different isoenzymes, which are encoded by a multi-gene family, APX7 DNA and amino acid sequence analysis, sequence comparisons and phylogenetic analysis and tree, conserved cis-regulatory elements in the promoters of the APX isozyme, transcriptional profiles of the rice isozymes, overview
APX is comprised of different isoenzymes, which are encoded by a multi-gene family, APX8 DNA and amino acid sequence analysis, sequence comparisons and phylogenetic analysis and tree, conserved cis-regulatory elements in the promoters of the APX isozyme, transcriptional profiles of the rice isozymes, overview
cotransformation of a soybean cDNA library and the Bax gene into yeast cells, screening for expressed genes that prevent Bax-induced apoptosis, the soybean ascorbate peroxidase inhibits the generation of reactive oxygen species by Bax, which in turn suppresses Bax-induced cell death in yeast
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DNA and amino acid sequence analysis, sequence comparisons and phylogenetic analysis and tree, conserved cis-regulatory elements in the promoters of the APX isozyme, overview
enzyme expression analysis, phylogenetic analysis and tree
enzyme expression analysis, phylogenetic analysis and tree, in Blastocrithidia sp. P57 very low APX activity is detected, despite the fact that the species apparently lacks the corresponding gene
Blastochritidia sp. P57
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enzyme expression analysis, phylogenetic analysis and tree, in Rhynchopus humris very low APX activity is detected, despite the fact that the species apparently lacks the corresponding gene
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enzyme PtotAPX expression analysis in callus cultures, recombinant expression of GFP-tagged enzyme in tobacco plants, localization to the chloroplasts
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expressed in Escherichia coli strain BL21 Star
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expression as a fusion product with the Escherichia coli maltose-binding protein
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expression in Escherichia coli
expression in Escherichia coli of two soybean ascorbate peroxidase cDNAs
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expression in Escherichia coli, most of the enzyme produced is present in the apo-form, without heme
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expression in Escherichia coli, the presence of 3% NaCl as well as beta-D-thiogalactopyranoside is needed for the expression
Chlamydomonas sp.
expression in Escherichia coli. Expression of holo enzyme depends on the simultaneous production of protein and heme by the bacteria
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expression in Saccharomyces cerevisiae
expression of an epitope-tagged form of the enzyme in Trypanosoma cruzi
full length AtstAPX is cloned into the pPZP221 binary vector, introduced into Arabidopsis thaliana by the floral dip method using Agrobacterium tumefaciens strain GV3101, for the generation of antibodies into the vector pQE80L for expression in Escherichia coli cells
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full length CmstAPX is cloned into the pPZP221 binary vector, introduced into Arabidopsis thaliana by the floral dip method using Agrobacterium tumefaciens strain GV3101, for the generation of antibodies into the vector pQE80L for expression in Escherichia coli cells
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gee APX, DNA and amino acid sequence analysis, sequence comparisons and phylogenetic analysis and tree, conserved cis-regulatory elements in the promoters of the APX isozyme, overview
gene AgAPX1, DNA and amino acid sequence determination and analysis, phylogenetic tree, recombinant expression in Escherichia coli strain BL21(DE3), recombinant GFP-tagged enzyme expression in onion epidermal cells for analysis of subcellular localization of AgAPX1. Overexpression of AgAPX1 in Arabidopsis thaliana positively regulates drought tolerance by regulating the stomata aperture. Net photosynthetic rate considerably decreases in the wild-type compared to transgenic lines under drought stress
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gene APX, DNA and amino acid sequence analysis, sequence comparisons and phylogenetic analysis and tree, conserved cis-regulatory elements in the promoters of the APX isozyme, overview
gene APX, DNA and amino acid sequence determination and analysis. The 1938 bp RcAPX gene encompasses 6 introns and 7 exons. The open reading frame of RcAPX is 750 bp long and encodes a 249-amino acid peptide, sequence comparisons and phylogenetic analysis and tree, quantitative real-time PCR enzyme expression analysis. Recombinant expression in Escherichia coli
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gene APX, stable ectopic expression of His-V5-tagged or c-Myc-/GFP-tagged cAPX protein from a CMV-V5-His plasmid in mouse fibroblast-like cell line C3H10T1/2. Confirmation of cell transfection with this plasmid is performed by western blotting using anti-Myc antibody and by fluorescence microscopy. Method, overview
gene APX1, DNA and amino acid sequence analysis, sequence comparisons and phylogenetic analysis and tree, conserved cis-regulatory elements in the promoters of the APX isozyme, overview
gene APX1, overexpression CsAPX1 in Arabidopsis thaliana
gene APX1, quantitative realtime-PCR isozyme expression analysis
gene APX2, quantitative realtime-PCR isozyme expression analysis
gene APX3, quantitative realtime-PCR isozyme expression analysis
gene APX4, quantitative realtime-PCR isozyme expression analysis
gene APX5, quantitative realtime-PCR isozyme expression analysis
gene APX6, quantitative realtime-PCR isozyme expression analysis
gene APX6, quantitative RT-PCR enzyme expression analysis, transient expression assays in Nicotiana benthamiana leaves, constitutive expression of APX6 is restricted to old and dying cells and absent in younger tissues, thus age-dependent post-transcriptional regulation of APX6. The coding sequence of APX6 is a potential target of miR398, which is a key regulator of copper redistribution
gene APX7, quantitative realtime-PCR isozyme expression analysis
gene APX8, quantitative realtime-PCR isozyme expression analysis
gene AtAPX1, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3)
gene DsAPX, DNA and amino acid sequence determination and analysis, sequence comparisons, quantitative RT-PCR enzyme expression analysis
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gene MaAPX1, phenotype and genotyping, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, quantitative RT-PCR expression analysis of MaMsrB2 and MaAPX1 genes. Recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3), coexpression of gene MsrB2 as His-tagged enzyme. Ectopic recombinant overexpression of MaAPX1 in Arabidopsis thaliana leading to delay of the detached leaf senescence induced by dark in Arabidopsis
GhAPX1 is expressed in Escherichia coli
into the pBI121 binary vector for a Agrobacterium tumefaciens-mediated tobacco leaf disc transformation, a CaMV 35S promoter and a rd29A promoter driven construct is used
into the vector pET-28a+ for the expression in Escherichia coli BL21DE3 cells, the 5'-flanking region of the PgAPX1 gene is cloned into the Topo-TA vector
into the vector pGEM-T Easy for sequencing
into the vector pXG B2863 for transfection of Leishmania major cells
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into the vector pXG-B2863 for transfection of Leishmania major cells
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overexpression in Arabidopsis. Transgenic lines over-expressing OsAPXb show higher salt tolerance than OsAPXa transgenic lines. Overproduction of OsAPXb enhances and maintains APX activity to a much higher degree than OsAPXa in transgenic Arabidopsis during treatment with different concentrations of NaCl, enhances the active oxygen scavenging system, and protects plants from salt stress by equilibrating H2O2 metabolism
overexpression in Arabidopsis. Transgenic lines over-expressing OsAPXb showed higher salt tolerance than OsAPXa transgenic lines. Overproduction of OsAPXb enhances and maintains APX activity to a much higher degree than OsAPXa in transgenic Arabidopsis during treatment with different concentrations of NaCl, enhances the active oxygen scavenging system, and protects plants from salt stress by equilibrating H2O2 metabolism
overexpression in Escherichia coli
the entire and truncated versions of APX (1-140, 1-250, 140-439, 250-439 and 140-250) are cloned into pGADT7 to fuse to the GAL4 activation domain and expressed in yeast
the vector pT-7 is used, cytochrome c peroxidase, CCP, is converted into an ascorbate peroxidase, APX, by engineering the ascorbate-binding loop and critical arginine into CCP to give the CCP2APX mutant
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transgenic Arabidopsis thaliana constitutively overexpressing HvAPX1 under control of the CaMv 35S promoter
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DNA and amino acid sequence analysis, sequence comparisons and phylogenetic analysis and tree, conserved cis-regulatory elements in the promoters of the APX isozyme, overview
DNA and amino acid sequence analysis, sequence comparisons and phylogenetic analysis and tree, conserved cis-regulatory elements in the promoters of the APX isozyme, overview
DNA and amino acid sequence analysis, sequence comparisons and phylogenetic analysis and tree, conserved cis-regulatory elements in the promoters of the APX isozyme, overview
enzyme expression analysis, phylogenetic analysis and tree
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enzyme expression analysis, phylogenetic analysis and tree
enzyme expression analysis, phylogenetic analysis and tree
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enzyme expression analysis, phylogenetic analysis and tree
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expression in Escherichia coli
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expression in Escherichia coli
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expression in Escherichia coli
expression in Escherichia coli
gene APX, DNA and amino acid sequence analysis, sequence comparisons and phylogenetic analysis and tree, conserved cis-regulatory elements in the promoters of the APX isozyme, overview
gene APX, DNA and amino acid sequence analysis, sequence comparisons and phylogenetic analysis and tree, conserved cis-regulatory elements in the promoters of the APX isozyme, overview
gene APX, DNA and amino acid sequence analysis, sequence comparisons and phylogenetic analysis and tree, conserved cis-regulatory elements in the promoters of the APX isozyme, overview
into the vector pGEM-T Easy for sequencing
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into the vector pGEM-T Easy for sequencing
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