Information on EC 1.2.3.14 - abscisic-aldehyde oxidase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.2.3.14
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RECOMMENDED NAME
GeneOntology No.
abscisic-aldehyde oxidase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
abscisic aldehyde + H2O + O2 = abscisate + H2O2
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
redox reaction
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reduction
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
abscisic acid biosynthesis
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Carotenoid biosynthesis
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Metabolic pathways
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Biosynthesis of secondary metabolites
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SYSTEMATIC NAME
IUBMB Comments
abscisic-aldehyde:oxygen oxidoreductase
Acts on both (+)- and (-)-abscisic aldehyde. Involved in the abscisic-acid biosynthesis pathway in plants, along with EC 1.1.1.288, (xanthoxin dehydrogenase), EC 1.13.11.51 (9-cis-epoxycarotenoid dioxygenase) and EC 1.14.13.93 [(+)-abscisic acid 8'-hydroxylase]. While abscisic aldehyde is the best substrate, the enzyme also acts with indole-3-aldehyde, 1-naphthaldehyde and benzaldehyde as substrates, but more slowly [3].
CAS REGISTRY NUMBER
COMMENTARY hide
129204-36-0
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9029-07-6
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
cv Viviani. Abscisic acid-deficient mutants, impaired in both abscisic-aldehyde oxidase and xanthine dehydrogenase activity
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
cultivars Kobomugi and GK Othalom
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
enzyme overexpression in nap leaves suppresses the stay-green phenotype under extended darkness
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1-naphthaldehyde + H2O + O2
naphthalene-1-carboxylate + H2O2
show the reaction diagram
-
substrate activity assay
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-
?
abscisic aldehyde + 2,6-dichloroindophenol
abscisic acid + H2O2
show the reaction diagram
-
2,6-dichloroindophenol i.e. DCIP used as electron acceptor, natural electron acceptor is oxygen
rate of H2O2 formation increases in the presence of superoxide dismutase, indicating that in addition to the two-electron reduction of molecular oxygen, AAO1 and AAO3 also catalyze a one-electron transfer to molecular oxygen, leading to the formation of superoxide ion, O2-
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?
abscisic aldehyde + H2O + O2
abscisate + H2O2
show the reaction diagram
benzaldehyde + 2,6-dichloroindophenol
benzoic acid + H2O2
show the reaction diagram
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2,6-dichloroindophenol i.e. DCIP used as electron acceptor, natural electron acceptor is oxygen
rate of H2O2 formation increases in the presence of superoxide dismutase, indicating that in addition to the two-electron reduction of molecular oxygen, AAO1 and AAO3 also catalyze a one-electron transfer to molecular oxygen, leading to the formation of superoxide ion, O2-
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?
heptaldehyde + 2,6-dichloroindophenol
heptanoic acid + H2O2
show the reaction diagram
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2,6-dichloroindophenol i.e. DCIP used as electron acceptor, natural electron acceptor is oxygen
rate of H2O2 formation increases in the presence of superoxide dismutase, indicating that in addition to the two-electron reduction of molecular oxygen, AAO1 and AAO3 also catalyze a one-electron transfer to molecular oxygen, leading to the formation of superoxide ion, O2-
-
?
indole-3-aldehyde + H2O + O2
indole-3-carboxylate + H2O2
show the reaction diagram
indole-3-carbaldehyde + 2,6-dichloroindophenol
indole-3-carboxylate + H2O2
show the reaction diagram
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2,6-dichloroindophenol i.e. DCIP used as electron acceptor, natural electron acceptor is oxygen
rate of H2O2 formation increases in the presence of superoxide dismutase, indicating that in addition to the two-electron reduction of molecular oxygen, AAO1 and AAO3 also catalyze a one-electron transfer to molecular oxygen, leading to the formation of superoxide ion, O2-
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?
NADH + O2
NAD+ + O2-
show the reaction diagram
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oxidation of NADH by AAO1 and AAO3, no oxidation of NADPH by AAO1 or AAO3
for confirmation, O2--dependent reduction of cytochrome c monitored, oxidation of NADH by AAO1 and AAO3 does not result in detectable levels of H2O2
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?
additional information
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confirmation of superoxide generation by AAO1 and AAO3 by monitoring the reduction of the tetrazolium salt XTT due to O2-
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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
abscisic aldehyde + H2O + O2
abscisate + H2O2
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
molybdenum cofactor
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additional information
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presence of all prosthetic groups confirmed by UV–vis spectroscopy
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Molybdenum
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MoCo-containing enzyme
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cyanide
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the ability of AAO1 and AAO3 to reduce 2,6-dichloroindophenol is abrogated when the enzymes are pre-treated with cyanide, NADH oxidation activity of AAO1 and AAO3 is highly sensitive to cyanide treatment
diphenylene iodonium
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DPI i.e. diphenylene iodonium, in the presence of DPI aldehyde oxidation activities of AAO1 and AAO3 are strongly reduced to 1–16%, NADH oxidation activity of AAO1 and AAO3 is highly sensitive to DPI treatment
diphenyleneiodonium
B0LB01;
16% residual activity at 0.05 mM
estradiol
B0LB01;
60% residual activity at 0.1 mM
menadione
B0LB01;
78% residual activity at 0.1 mM
methanol
B0LB01;
complete inhibition at 2% (v/v)
p-hydroxymercuribenzoate
B0LB01;
62% residual activity at 0.1 mM
potassium cyanide
B0LB01;
13% residual activity at 1 mM
additional information
B0LB01;
not inhibited by iodoacetamide and ethanol
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0051
abscisic aldehyde
B0LB01;
at pH 7.5 and 30°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.093
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heptaldehyde oxidation by AAO1, pH not specified in the publication, temperature not specified in the publication
0.11
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benzaldehyde oxidation by AAO1, pH not specified in the publication, temperature not specified in the publication
0.146
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benzaldehyde oxidation by AAO3, pH not specified in the publication, temperature not specified in the publication
0.204
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indole-3-carbaldehyde oxidation by AAO3, pH not specified in the publication, temperature not specified in the publication
0.215
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NADH oxidation by AAO1, pH not specified in the publication, temperature not specified in the publication
0.515
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abscisic aldehyde oxidation by AAO1, pH not specified in the publication, temperature not specified in the publication
0.517
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heptaldehyde oxidation by AAO3, pH not specified in the publication, temperature not specified in the publication
0.53
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NADH oxidation by AAO3, pH not specified in the publication, temperature not specified in the publication
0.558
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indole-3-carbaldehyde oxidation by AAO1, pH not specified in the publication, temperature not specified in the publication
0.635
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abscisic aldehyde oxidation by AAO3, pH not specified in the publication, temperature not specified in the publication
additional information
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in the presence of diphenylene iodonium, aldehyde oxidation activities of AAO1 and AAO3 are strongly reduced to 1–16%
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.5
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activity assay
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
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activity assay
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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AAO3 mRNA expression in guard cells of dehydrated rosette leaves
Manually annotated by BRENDA team
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extracts from drought stressed leaves, AAO3
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
150000
B0LB01;
2 * 150000, SDS-PAGE
302000
B0LB01;
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
B0LB01;
2 * 150000, SDS-PAGE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
by affinity chromatography with nickel-nitrilotriacetic acid-agarose under native conditions, further purification by anion exchange chromatography
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DEAE-Sepharose column chromatography, Ni-IDA resin column chromatography, and Superdex 200 gel filtration
B0LB01;
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cDNAs of AAO1 and AAO3 expressed in Pichia pastoris to obtain recombinant homodimeric AAO1 and AAO3 proteins with His6-tag
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expressed in Pichia pastoris strain KM71H
B0LB01;
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
during a progressively (but not rapidly) induced drought, the level of AO3 transcript increases significantly in the roots and leaves
B0LB01;
gene expression is induced by osmotic stress caused by treatment with PEG 6000 (100-400 mOsm)
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