Information on EC 1.2.3.14 - abscisic-aldehyde oxidase

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The expected taxonomic range for this enzyme is: Magnoliophyta

EC NUMBER
COMMENTARY
1.2.3.14
-
RECOMMENDED NAME
GeneOntology No.
abscisic-aldehyde oxidase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
abscisic aldehyde + H2O + O2 = abscisate + H2O2
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
oxidation
-
-
redox reaction
-
-
reduction
-
-
PATHWAY
KEGG Link
MetaCyc Link
abscisic acid biosynthesis
-
Biosynthesis of secondary metabolites
-
Carotenoid biosynthesis
-
Metabolic pathways
-
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].
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
AAO2
-
isozyme
AAO3
-
isozyme
ABA aldehyde oxidase
-
-
ABA aldehyde oxidase
-
-
abscisic aldehyde oxidase
-
-
abscisic aldehyde oxidase
-
-
abscisic aldehyde oxidase
-
-
abscisic aldehyde oxidase 3
-
-
AOdelta
-
-
Arabidopsis aldehyde oxidase 3
Q7G9P4
-
EC 1.2.3.1
-
formerly
CAS REGISTRY NUMBER
COMMENTARY
129204-36-0
-
9029-07-6
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
ecotype Columbia, molecular characterization of aao3-2 and aao-3-3 alleles
-
-
Manually annotated by BRENDA team
cv Viviani. Abscisic acid-deficient mutants, impaired in both abscisic-aldehyde oxidase and xanthine dehydrogenase activity
-
-
Manually annotated by BRENDA team
L. cv. Rio Fuego
-
-
Manually annotated by BRENDA team
mutant lacking ABA aldehydeoxidase
-
-
Manually annotated by BRENDA team
cultivars Kobomugi and GK Othalom
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1-naphthaldehyde + H2O + O2
naphthalene-1-carboxylate + H2O2
show the reaction diagram
-
substrate activity assay
-
-
?
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-
-
?
abscisic aldehyde + H2O + O2
abscisate + H2O2
show the reaction diagram
-
-
-
-
?
abscisic aldehyde + H2O + O2
abscisate + H2O2
show the reaction diagram
-
-
-
-
?
abscisic aldehyde + H2O + O2
abscisate + H2O2
show the reaction diagram
-
the AAO3 gene product plays a major role in abscisic acid biosynthesis in seed
-
-
?
abscisic aldehyde + H2O + O2
abscisate + H2O2
show the reaction diagram
-
the enzyme catalyzes the final step of abscisic acid biosynthesis, specifically in rosette leaves
-
-
?
abscisic aldehyde + H2O + O2
abscisate + H2O2
show the reaction diagram
-
the enzyme catalyzes the final step of abscisic acid biosynthesis. AAO3 is the AAO that plays a major role in abscisic acid biosynthesis in seeds as well as in leaves
-
-
?
abscisic aldehyde + H2O + O2
abscisate + H2O2
show the reaction diagram
Q7G9P4
the enzyme catalyzes the final step of abscisic acid biosynthesis. NO detectable activity in guard cells of nonstressed rosette or wet-control leaves
-
-
?
benzaldehyde + 2,6-dichloroindophenol
benzoic 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-
-
?
heptaldehyde + 2,6-dichloroindophenol
heptanoic 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-
-
?
indole-3-aldehyde + H2O + O2
indole-3-carboxylate + H2O2
show the reaction diagram
-
-
-
-
?
indole-3-aldehyde + H2O + O2
indole-3-carboxylate + H2O2
show the reaction diagram
-
substrate activity assay
-
-
?
NADH + O2
NAD+ + O2-
show the reaction diagram
-
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
-
?
indole-3-carbaldehyde + 2,6-dichloroindophenol
indole-3-carboxylate + 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-
-
?
additional information
?
-
-
confirmation of superoxide generation by AAO1 and AAO3 by monitoring the reduction of the tetrazolium salt XTT due to O2-
-
-
?
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
abscisic aldehyde + H2O + O2
abscisate + H2O2
show the reaction diagram
-
-
-
-
?
abscisic aldehyde + H2O + O2
abscisate + H2O2
show the reaction diagram
-
-
-
-
?
abscisic aldehyde + H2O + O2
abscisate + H2O2
show the reaction diagram
-
the AAO3 gene product plays a major role in abscisic acid biosynthesis in seed
-
-
?
abscisic aldehyde + H2O + O2
abscisate + H2O2
show the reaction diagram
-
the enzyme catalyzes the final step of abscisic acid biosynthesis, specifically in rosette leaves
-
-
?
abscisic aldehyde + H2O + O2
abscisate + H2O2
show the reaction diagram
-
the enzyme catalyzes the final step of abscisic acid biosynthesis. AAO3 is the AAO that plays a major role in abscisic acid biosynthesis in seeds as well as in leaves
-
-
?
abscisic aldehyde + H2O + O2
abscisate + H2O2
show the reaction diagram
Q7G9P4
the enzyme catalyzes the final step of abscisic acid biosynthesis. NO detectable activity in guard cells of nonstressed rosette or wet-control leaves
-
-
?
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
additional information
-
presence of all prosthetic groups confirmed by UV–vis spectroscopy
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Mo
-
MoCo-containing enzyme
Mo
-
molybdoenzyme
Molybdenum
-
MoCo-containing enzyme
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
cyanide
-
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
-
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
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.093
-
-
heptaldehyde oxidation by AAO1, pH not specified in the publication, temperature not specified in the publication
0.11
-
-
benzaldehyde oxidation by AAO1, pH not specified in the publication, temperature not specified in the publication
0.146
-
-
benzaldehyde oxidation by AAO3, pH not specified in the publication, temperature not specified in the publication
0.204
-
-
indole-3-carbaldehyde oxidation by AAO3, pH not specified in the publication, temperature not specified in the publication
0.215
-
-
NADH oxidation by AAO1, pH not specified in the publication, temperature not specified in the publication
0.515
-
-
abscisic aldehyde oxidation by AAO1, pH not specified in the publication, temperature not specified in the publication
0.517
-
-
heptaldehyde oxidation by AAO3, pH not specified in the publication, temperature not specified in the publication
0.53
-
-
NADH oxidation by AAO3, pH not specified in the publication, temperature not specified in the publication
0.558
-
-
indole-3-carbaldehyde oxidation by AAO1, pH not specified in the publication, temperature not specified in the publication
0.635
-
-
abscisic aldehyde oxidation by AAO3, pH not specified in the publication, temperature not specified in the publication
additional information
-
-
in the presence of diphenylene iodonium, aldehyde oxidation activities of AAO1 and AAO3 are strongly reduced to 1–16%
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
8.5
-
-
activity assay
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
-
activity assay
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
Q7G9P4
AAO3 mRNA expression in guard cells of dehydrated rosette leaves
Manually annotated by BRENDA team
Q7G9P4
AAO3 mRNA expression in guard cells of dehydrated rosette leaves
Manually annotated by BRENDA team
-
extracts from drought stressed leaves, AAO3
Manually annotated by BRENDA team
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
by affinity chromatography with nickel-nitrilotriacetic acid-agarose under native conditions, further purification by anion exchange chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
cDNAs of AAO1 and AAO3 expressed in Pichia pastoris to obtain recombinant homodimeric AAO1 and AAO3 proteins with His6-tag
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
gene expression is induced by osmotic stress caused by treatment with PEG 6000 (100-400 mOsm)
-