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Information on EC 1.2.3.14 - abscisic-aldehyde oxidase and Organism(s) Arabidopsis thaliana and UniProt Accession Q7G9P4

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IUBMB Comments
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 .
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Arabidopsis thaliana
UNIPROT: Q7G9P4
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Word Map
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
aodelta, arabidopsis aldehyde oxidase 3, abscisic aldehyde oxidase, aba aldehyde oxidase, abscisic aldehyde oxidase 3, abscisic-aldehyde oxidase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Arabidopsis aldehyde oxidase 3
-
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
-
9029-07-6
-
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 + 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
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-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-
-
?
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
-
?
additional information
?
-
confirmation of superoxide generation by AAO1 and AAO3 by monitoring the reduction of the tetrazolium salt XTT due to O2-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
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
-
additional information
presence of all prosthetic groups confirmed by UV–vis spectroscopy
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
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]
ORGANISM
UNIPROT
COMMENTARY hide
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%
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
enzyme overexpression in nap leaves suppresses the stay-green phenotype under extended darkness
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ALDO3_ARATH
1332
0
146701
Swiss-Prot
other Location (Reliability: 1)
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by affinity chromatography with nickel-nitrilotriacetic acid-agarose under native conditions, further purification by anion exchange chromatography
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Koiwai, H.; Nakaminami, K.; Seo, M.; Mitsuhashi, W.; Toyomasu, T.; Koshiba, T.
Tissue-specific localization of an abscisic acid biosynthetic enzyme, AAO3, in Arabidopsis
Plant Physiol.
134
1697-1707
2004
Arabidopsis thaliana (Q7G9P4)
Manually annotated by BRENDA team
Zarepour, M.; Simon, K.; Wilch, M.; Nielaender, U.; Koshiba, T.; Seo, M.; Lindel, T.; Bittner, F.
Identification of superoxide production by Arabidopsis thaliana aldehyde oxidases AAO1 and AAO3
Plant Mol. Biol.
80
659-671
2012
Arabidopsis thaliana (Q7G9P4)
Manually annotated by BRENDA team
Yang, J.; Worley, E.; Udvardi, M.
A NAP-AAO3 regulatory module promotes chlorophyll degradation via ABA biosynthesis in Arabidopsis leaves
Plant Cell
26
4862-4874
2014
Arabidopsis thaliana (Q7G9P4)
Manually annotated by BRENDA team