Information on EC 1.11.1.11 - L-ascorbate peroxidase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.11.1.11
-
RECOMMENDED NAME
GeneOntology No.
L-ascorbate peroxidase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2 L-ascorbate + H2O2 + 2 H+ = 2 monodehydroascorbate + 2 H2O
show the reaction diagram
2 L-ascorbate + H2O2 + 2 H+ = L-ascorbate + L-dehydroascorbate + 2 H2O
show the reaction diagram
overall reaction
-
-
-
2 monodehydroascorbate = L-ascorbate + L-dehydroascorbate
show the reaction diagram
spontaneous
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
peroxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Ascorbate and aldarate metabolism
-
-
Glutathione metabolism
-
-
L-ascorbate degradation II (bacterial, aerobic)
-
-
L-ascorbate degradation III
-
-
L-ascorbate degradation V
-
-
ascorbate metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
L-ascorbate:hydrogen-peroxide oxidoreductase
A heme protein. Oxidizes ascorbate and low molecular weight aromatic substrates. The monodehydroascorbate radical produced is either directly reduced back to ascorbate by EC 1.6.5.4 [monodehydroascorbate reductase (NADH)] or undergoes non-enzymic disproportionation to ascorbate and dehydroascorbate.
CAS REGISTRY NUMBER
COMMENTARY hide
72906-87-7
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
Uniprot
Manually annotated by BRENDA team
cultivated beet varieties, Huzar and Janosik, and their wild salt-tolerant relative Beta vulgaris ssp. maritima
-
-
Manually annotated by BRENDA team
cytoplasmic male sterility line
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
tea
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
Chlamydomonas sp.
W80 strain
Uniprot
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
L. corm
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
larvae
-
-
Manually annotated by BRENDA team
strain 5ASKH
-
-
Manually annotated by BRENDA team
low activity
-
-
Manually annotated by BRENDA team
alfalfa
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Populus simonii x Populus pyramidalis
variant Opera 8277
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Solanum pennellii acc. Atico
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
spinach
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 L-ascorbate + H2O2 + 2 H+
2 monodehydroascorbate + 2 H2O
show the reaction diagram
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2 + H+
? + H2O
show the reaction diagram
-
-
-
-
?
2,2'-azino-di-(3-ethyl-benzothiazoline-(6)-sulfonic acid) + H2O2
? + H2O
show the reaction diagram
-
3% relative activity to L-ascorbate
-
?
2,2'-azino-di-[3-ethylbenzothiazoline-(6)-sulfonic acid] + H2O2
?
show the reaction diagram
2,2'-azinobis-(3-ethylbenzothiazoline-6-sulfonic acid) + H2O2
?
show the reaction diagram
-
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
show the reaction diagram
-
enzyme partially purified from whole body homogenate, 40% of the activity with L-ascorbate
-
?
Cytochrome c + H2O
?
show the reaction diagram
-
-
-
-
?
cytochrome c + H2O2
?
show the reaction diagram
-
able to use both ascorbate and cytochrome c as reducing electron donors
-
-
?
cytochrome c + H2O2
? + H2O
show the reaction diagram
D-araboascorbic acid + H2O2
dehydroascorbate + H2O
show the reaction diagram
-
56% activity relative to L-ascorbate
-
?
D-iso-ascorbate + H2O2
dehydroascorbate + H2O
show the reaction diagram
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
?
show the reaction diagram
-
60.3% activity compared to L-ascorbate
-
-
?
dihydrorhodamine 123 + H2O2
?
show the reaction diagram
ethyl phenyl sulfide + H2O2
? + H2O
show the reaction diagram
-
-
-
-
?
ferrocyanide + H2O2
ferricyanide + H2O
show the reaction diagram
-
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
show the reaction diagram
GSSG + H2O2
?
show the reaction diagram
about 20% of the activity with L-ascorbate
-
-
?
guaiacol + H2O2
?
show the reaction diagram
guaiacol + H2O2
? + H2O
show the reaction diagram
iodide + H2O2
?
show the reaction diagram
-
2.3% activity relative to L-ascorbate
-
?
isopropyl phenyl sulfide + H2O2
? + H2O
show the reaction diagram
-
-
-
-
L-ascorbate + cumene hydroperoxide
?
show the reaction diagram
-
8.0% activity compared to H2O2
-
-
?
L-ascorbate + H2O2
? + H2O
show the reaction diagram
-
-
-
-
?
L-ascorbate + H2O2
dehydroascorbate + 2 H2O
show the reaction diagram
L-ascorbate + H2O2
dehydroascorbate + H2O
show the reaction diagram
L-ascorbate + tert-butyl hydroperoxide
?
show the reaction diagram
-
17.4% activity compared to H2O2
-
-
?
L-ascorbic acid + cumene hydroperoxide
dehydroascorbate + 1,1-dimethylbenzylalcohol + H2O
show the reaction diagram
L-ascorbic acid + tert-butylhydroperoxide
dehydroascorbate + tert-butylalcohol
show the reaction diagram
methyl naphthalene sulfide + H2O2
? + H2O
show the reaction diagram
-
-
-
?
methyl phenyl sulfide + H2O2
? + H2O
show the reaction diagram
-
-
-
?
n-propyl phenyl sulfide + H2O2
? + H2O
show the reaction diagram
-
-
-
?
NADH + H+ + H2O2
NAD+ + H2O
show the reaction diagram
-
10% of the activity with ascorbate, APX 1, 1% of the activity with ascorbate, APX 2
-
-
?
NADPH + H+ + H2O2
NADP+ + H2O
show the reaction diagram
-
27% of the activity with ascorbate, APX 1, 21% of the activity with ascorbate, APX 2
-
-
?
NADPH + H2O2
? + H2O
show the reaction diagram
o-dianisidine + H2O2
?
show the reaction diagram
p-chlorophenyl methyl sulfide + H2O2
? + H2O
show the reaction diagram
-
-
-
?
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
show the reaction diagram
-
-
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
show the reaction diagram
-
-
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
show the reaction diagram
-
-
-
?
pyrocatechol + H2O2
1,2-benzoquinone + H2O
show the reaction diagram
-
low activity compared to L-ascorbate
-
?
pyrogallol + H2O2
3-hydroxybenzo-1,2-quinone + H2O
show the reaction diagram
pyrogallol + H2O2
?
show the reaction diagram
pyrogallol + H2O2
? + H2O
show the reaction diagram
-
32% of the activity with ascorbate
-
-
?
reductic acid + H2O2
?
show the reaction diagram
-
i.e. 2,3-dihydroxy-2-cyclopenten-1-one, 7.1% activity relative to L-ascorbate
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-ascorbate + H2O2
dehydroascorbate + 2 H2O
show the reaction diagram
L-ascorbate + H2O2
dehydroascorbate + H2O
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Iron
-
predominantly five-coordinate high-spin iron
Ni2+
-
below 0.01 mM, activation, inhibition above
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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-mercaptoethanol
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
azide
beta-mercaptoethanol
-
29% inhibition at 3 mM
Br-
-
marked inhibition at 1 mM
CO
-
potent inhibitor
cysteine
diethylenetriamine pentaacetic acid
-
9% inhibition at 5 mM
dithioerythritol
dithiothreitol
Hg2+
-
complete inhibition at 1 mM
hydroxylamine
Hydroxyurea
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
iodoacetamide
iodoacetate
L-cysteine
-
28% inhibition at 3 mM
Mersalyl
-
58% inhibition at 0.005 mM, 100% inhibition at 0.05 mM
Mn2+
-
marked inhibition at 1 mM
N-ethylmaleimide
-
33% inhibition at 0.05 mM, 28% inhibition at 0.5 mM
Na2HAsO4
-
inhibition in the range of 0.01-0.5 mM
p-Aminophenol
p-chloromercuribenzoate
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
reduced glutathione
salicylic acid
Sodium azide
-
1 mM, 72% residual activity, APX 1, 55% residual activity, APX 2
sodium nitroprusside
-
partial
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
methyl jasmonate
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
nitric oxide
-
causes an increase in the total enzymatic activity of ascorbate peroxidase. The nitric oxide-induced changes in ascorbate peroxidase enzymatic activity are coupled to altered nodule H2O2 content. Enzymatic activity of the largest isoform, Apx1 is upregulated by 11% in response to 5 microM of nitric oxide donor DETA/NO and 21% in response to 10 microM DETA/NO. 5 microM of DETA/NO increase the enzymatic activity of the second largest isoform Apx2 by about 57%. Treatment of nodulated soybean with 5 microM DETA/NO upregulates the smallest nodule isoform Apx3 enzymatic activity by 228% compared to untreated controls
phenanthrene
-
exposure to 0.5 microM phenanthrene results in significant increase in the levels of both enzymatic and non-enzymatic antioxidants, with the levels of total glutathione and ascorbate doubling, the activitiy of APOX increasing by 2fold after 72 h of exposure to phenanthrene
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000043
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
pH 7.0, temperature not specified in the publication. Hill coefficient n is 1.0
0.07 - 6.5
ascorbate
0.025 - 6
cytochrome c
0.017 - 12.3
guaiacol
0.011 - 0.22
H2O2
0.041 - 0.804
L-ascorbate
0.41
L-ascorbic acid
-
-
2.4 - 9.6
pyrogallol
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.4
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
Panicum virgatum
-
pH 7.0, temperature not specified in the publication. Hill coefficient n is 1.0
0.2 - 696
ascorbate
1.83
cytochrome c
Leishmania major
-
25°C, wild-type enzyme
1.5 - 66
guaiacol
2.03 - 3410
H2O2
1.74 - 2833
L-ascorbate
160
pyrogallol
Pisum sativum
-
wild-type, Cys32Ser mutant and DTNB-modified enzyme
additional information
additional information
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
768 - 16500
H2O2
22
178 - 6600
L-ascorbate
548
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0308
hydroxylamine
-
0.0018 - 0.0083
KCN
0.059 - 0.085
NaN3
0.1905
salicylic acid
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.01
-
crude extract of root nodules, the activity is rapidly lost after extraction
0.092
-
crude extract of root nodules
0.096
-
crude extract of root nodules, cv Alaska
0.1
-
purified enzyme
0.11
-
crude extract of root nodules
0.161
-
crude extract of root nodules, cv Austrian winter
0.213
-
crude extract of root nodules
0.241
-
crude extract of root nodules
0.258
-
crude extract of root nodules
0.26
-
effect of abscisic acid and EGTA on APX activity, 1 day following chilling stress
0.27
-
effect of abscisic acid and EGTA on APX activity, 7 days, under normal temperature
0.28
-
effect of abscisic acid and EGTA on APX activity, 4 days following chilling stress; effect of abscisic acid and LaCl3 on APX activity, 4 days following chilling stress
0.284
-
crude extract of root nodules
0.3
-
effect of EGTA on APX activity, 4 days following chilling stress; in water, 4 days following chilling stress
0.31
-
effect of abscisic acid and EGTA on APX activity, 4 days, under normal temperature; effect of abscisic acid on APX activity, 7 days, under normal temperature; effect of LaCl3 on APX activity, 7 days, under normal temperature
0.32
-
effect of abscisic acid and LaCl3 on APX activity, 1 day following chilling stress; effect of EGTA on APX activity, 1 day following chilling stress; effect of LaCl3 on APX activity, 4 days following chilling stress; in water, 1 day following chilling stress
0.33
-
effect of abscisic acid and LaCl3 on APX activity, 4 days, under normal temperature; effect of abscisic acid and LaCl3 on APX activity, 7 days, under normal temperature; effect of EGTA on APX activity, 4 days, under normal temperature; effect of EGTA on APX activity, 7 days, under normal temperature; in water, 7 days, under normal temperature
0.35
-
in water, 4 days, under normal temperature
0.36
-
effect of abscisic acid on APX activity, 4 days following chilling stress; effect of LaCl3 on APX activity, 1 day following chilling stress
0.366
-
crude extract of root nodules
0.37
-
effect of LaCl3 on APX activity, 4 days, under normal temperature
0.4
-
effect of abscisic acid on APX activity, 1 day following chilling stress
0.45
-
effect of abscisic acid on APX activity, 4 days, under normal temperature
0.7684
-
crude extract
1.3
Chlamydomonas sp.
recombinant enzyme, soluble fraction, addition of 3% NaCl
1.6
-
crude extract, in 50 mM potassium phosphate (pH 7.0), at 22°C
2.8
-
purified enzyme, electron donor: glutathione, electron acceptor: H2O2
3 - 4
-
affinity purified preparation
3.3
-
cell extract
4.32
-
crude extract of root nodules, activity is only detected when soluble polyvinylpolypyrrolidone is included in the buffer and O2 is excluded by through degassing of buffers and performing all extraction steps under a vigorous stream of N2 gas
5.8
-
purified enzyme, electron donor: iodide, electron acceptor: H2O2
7.1
-
substrate: cumene hydroperoxide
9.4
-
recombinant enzyme 1, after DEAE-column chromatography
19.2
-
substrate: tert-butyl hydroperoxide
20.3
-
purified enzyme, electron donor: guaiacol, electron acceptor: H2O2
20.9
-
substrate: H2O2
31.7
-
purified recombinant enzyme
32
-
recombinant enzyme
34
-
wild-type enzyme
34.2
-
purified enzyme
36
-
purified enzyme
37
-
stress factor drought
46.7
-
partially purified enzyme
53
-
stress factors drought and heat
56
-
purified enzyme
63.6
-
recombinant enzyme 2, after chromatofocusing
100
-
cytosolic enzyme, in the presence and absence of salicylic acid
117
-
purified recombinant enzyme
132.2
-
purified enzyme, electron donor: L-ascorbic acid, electron acceptor: cumene hydroperoxide
142.1
-
purified enzyme, electron donor: D-araboascorbic acid, electron acceptor: H2O2
172.8
-
purified enzyme, electron donor: L-ascorbic acid, electron acceptor: tert-butyl hydroperoxide
185.5
-
purified enzyme, electron donor: pyrogallol, electron acceptor: H2O2
254
-
purified enzyme, electron donor: L-ascorbic acid, electron acceptor: H2O2
378
-
pH 7.5, 25°C
456
-
after 285fold purification, in 50 mM potassium phosphate (pH 7.0), at 22°C
561.1
-
purified enzyme
580
Chlamydomonas sp.
purified recombinant enzyme
636
Chlamydomonas sp.
purified native enzyme
1307
-
purified enzyme
1500
-
chloroplastic enzyme, in the presence and absence of salicylic acid
additional information
-
effects of media amendments
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5
-
assay at, thylakoid-bound chloroplastic isoenzyme
5 - 6
-
-
5.2
-
enzyme form B
5.9 - 7
-
-
6.3
-
assay at
6.4
in gel activity assay
6.8
Chlamydomonas sp.
-
7.4
-
activity assay
7.8
-
activity assay
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 7.8
activity 35 units mg-1 protein min-1 at pH 5.0 and pH 7.8
5 - 7.5
pH 5: about 50% of maximal activity, pH 7.5: about 50% of maximal activity
5 - 9
-
pH 5.0: 68% of maximal activity, pH 9.0: 23% of maximal activity
6 - 7.9
-
maximum activity maintained
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
-
activity assay
23
in gel activity assay at room temperature
30
-
peroxidase assay
32 - 34
-
-
42
Chlamydomonas sp.
-
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 55
-
20°C: about 65% of maximal activity, 55°C: about 40% of maximal activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.6
calculated
5.62
estimated isoelectric point
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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
Manually annotated by BRENDA team
-
55.6% relative activity to salivary gland
Manually annotated by BRENDA team
-
presence of two major non-plastid isozymes
Manually annotated by BRENDA team
-
31.1% relative activity to salivary gland
Manually annotated by BRENDA team
-
20% relative activity to salivary gland
Manually annotated by BRENDA team
-
highest activity
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information