Information on EC 1.2.3.7 - indole-3-acetaldehyde oxidase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.2.3.7
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RECOMMENDED NAME
GeneOntology No.
indole-3-acetaldehyde oxidase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(indol-3-yl)acetaldehyde + H2O + O2 = (indol-3-yl)acetate + H2O2
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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redox reaction
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reduction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
L-tryptophan degradation VI (via tryptamine)
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L-tryptophan degradation VII (via indole-3-pyruvate)
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Tryptophan metabolism
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tryptophan metabolism
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SYSTEMATIC NAME
IUBMB Comments
(indol-3-yl)acetaldehyde:oxygen oxidoreductase
A hemoprotein. This enzyme is an isoform of aldehyde oxidase (EC 1.2.3.1). It has a preference for aldehydes having an indole-ring structure as substrate [6,7]. It may play a role in plant hormone biosynthesis as its activity is higher in the auxin-overproducing mutant, super-root1, than in wild-type Arabidopsis thaliana [7]. While (indol-3-yl)acetaldehyde is the preferred substrate, it also oxidizes indole-3-carbaldehyde and acetaldehyde, but more slowly. The enzyme from maize contains FAD, iron and molybdenum [4].
CAS REGISTRY NUMBER
COMMENTARY hide
66082-22-2
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
abscisic aldehyde + oxidized 2,6-dichloroindophenol + H2O
abscisic acid + reduced 2,6-dichloroindophenol
show the reaction diagram
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-
-
?
acetaldehyde + O2 + H2O
acetate + H2O2
show the reaction diagram
benzaldehyde + oxidized 2,6-dichloroindophenol + H2O
benzoic acid + reduced 2,6-dichloroindophenol
show the reaction diagram
weak substrate
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?
heptaldehyde + oxidized 2,6-dichloroindophenol + H2O
heptanoic acid + reduced 2,6-dichloroindophenol
show the reaction diagram
weak substrate
-
-
?
indole-3-acetaldehyde + O2
indole-3-acetate + H2O2
show the reaction diagram
highly efficient conversion
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?
indole-3-acetaldehyde + O2 + H2O
indole-3-acetate + H2O2
show the reaction diagram
indole-3-acetaldehyde + oxidized 2,6-dichloroindophenol + H2O
indole-3-acetate + reduced 2,6-dichloroindophenol
show the reaction diagram
efficient substrate
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-
?
indole-3-acetaldehyde + phenazine methosulfate
indole-3-acetate + ?
show the reaction diagram
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?
indole-3-aldehyde + O2
3-carboxyindole + H2O
show the reaction diagram
phenylacetaldehyde + O2
phenylacetate + H2O
show the reaction diagram
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86% of the activity with indole-3-acetaldehyde
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?
additional information
?
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in addition to the two-electron reduction of molecular oxygen, isoform AAO1 also catalyzes a one-electron transfer to molecular oxygen, leading to the formation of O2-. However, the production of O2 appears to be less efficient than the production of H2O2
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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
indole-3-acetaldehyde + O2
indole-3-acetate + H2O2
show the reaction diagram
Q7G193
highly efficient conversion
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?
indole-3-acetaldehyde + O2 + H2O
indole-3-acetate + H2O2
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
flavin
heme
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contains a heme type iron component
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Iron
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contains a heme type iron component
MgCl2
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1 mM, activates
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,4-Dichlorophenol
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2,4-Dichlorophenoxyacetic acid
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2,4-dinitrophenol
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2-mercaptoethanol
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benzaldehyde
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cyanide
Dichlorophenoxyacetic acid
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diphenylene iodonium
strong inhibitor
Dithionite
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H2O2
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hydroxylamine
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indole-3-acetic acid
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feedback inhibition in vivo
iodoacetate
KCN
complete inhibition at 20 mM after 1 h incubation at room temperature
menadione
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slight
N-ethylmaleimide
p-hydroxymercuribenzoate
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p-nitrophenol
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phenylacetaldehyde
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additional information
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not: p-phenanthroline, diethyldithiocarbamate, xanthogenate, semicarbazide
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
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activates
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.345 - 1.4
Indole-3-acetaldehyde
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.093
using heptaldehyde as substrate, pH 7.5, temperature not specified in the publication
0.11
using benzaldehyde as substrate, pH 7.5, temperature not specified in the publication
0.515
using abscisic aldehyde as substrate, pH 7.5, temperature not specified in the publication
0.558
using indole-3-carbaldehyde as substrate, pH 7.5, temperature not specified in the publication
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.2
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crude extract
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2.9 - 5.5
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about 50% of maximal activity at pH 2.9 and at pH 5.5
5.8 - 6.8
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pH 5.8: about 40% of maximal activity, pH 6.8: about 25% of maximal activity, crude extract
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60 - 70
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50 - 80
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50C: about 50% of maximal activity, 80C: about 70% of maximal activity
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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Manually annotated by BRENDA team
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 9
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4C, 18 h, stable
390440
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0 - 30
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10 min, stable
40
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10 min, 41% loss of activity
additional information
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activated by heating at 60C, about 2 min
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
prolonged dialysis inactivates
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Ni-NTA agarose column chromatography, and Source 15Q colum chromatography
partial
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Pichia pastoris