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
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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-
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?
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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