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Information on EC 1.2.3.14 - abscisic-aldehyde oxidase
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1.2.3.14 abscisic-aldehyde oxidaseIUBMB 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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Word Map
- 1.2.3.14
-
1.2.3.1
- moco
-
9-cis-epoxycarotenoid
- wilty
- indole-3-aldehyde
-
psaos
-
1.2.1.37
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
aodelta, abscisic aldehyde oxidase, arabidopsis aldehyde oxidase 3, aba aldehyde oxidase, abscisic-aldehyde oxidase, abscisic aldehyde oxidase 3, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AAO
AAO3
ABA aldehyde oxidase
abscisic aldehyde oxidase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
abscisic aldehyde + H2O + O2 = abscisate + H2O2
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
reduction
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PATHWAY SOURCE
PATHWAYS
MetaCyc
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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].
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CAS REGISTRY NUMBER
COMMENTARY
129204-36-0
-
9029-07-6
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1-naphthaldehyde + H2O + O2
naphthalene-1-carboxylate + H2O2
-
substrate activity assay
-
?
abscisic aldehyde + 2,6-dichloroindophenol
abscisic acid + H2O2
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-
?
benzaldehyde + 2,6-dichloroindophenol
benzoic acid + H2O2
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
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
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-
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-
-
?
abscisic aldehyde + H2O + O2
abscisate + H2O2
-
the AAO3 gene product plays a major role in abscisic acid biosynthesis in seed
-
?
abscisic aldehyde + H2O + O2
abscisate + H2O2
-
the enzyme catalyzes the final step of abscisic acid biosynthesis, specifically in rosette leaves
-
?
abscisic aldehyde + H2O + O2
abscisate + H2O2
-
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
the enzyme catalyzes the final step of abscisic acid biosynthesis. NO detectable activity in guard cells of nonstressed rosette or wet-control leaves
-
?
indole-3-aldehyde + H2O + O2
indole-3-carboxylate + H2O2
-
substrate activity assay
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
abscisic aldehyde + H2O + O2
abscisate + H2O2
-
the AAO3 gene product plays a major role in abscisic acid biosynthesis in seed
-
-
?
abscisic aldehyde + H2O + O2
abscisate + H2O2
-
the enzyme catalyzes the final step of abscisic acid biosynthesis, specifically in rosette leaves
-
-
?
abscisic aldehyde + H2O + O2
abscisate + H2O2
-
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
the enzyme catalyzes the final step of abscisic acid biosynthesis. NO detectable activity in guard cells of nonstressed rosette or wet-control leaves
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
presence of all prosthetic groups confirmed by UV–vis spectroscopy
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mo
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INHIBITOR
ORGANISM
UNIPROT
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
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
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%
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
cv Viviani. Abscisic acid-deficient mutants, impaired in both abscisic-aldehyde oxidase and xanthine dehydrogenase activity
-
-
brenda
ecotype Columbia, molecular characterization of aao3-2 and aao-3-3 alleles
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
AAO3 mRNA expression in guard cells of dehydrated rosette leaves
brenda
AAO3 mRNA expression in guard cells of dehydrated rosette leaves
brenda
-
the enzyme expression is highest in seeds of fully ripe berries
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
enzyme overexpression in nap leaves suppresses the stay-green phenotype under extended darkness
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). ALDO3_ARATH
1332
0
146701
Swiss-Prot
other Location (Reliability: 1)
A0A5B7BKW9_DAVIN
1380
0
151547
TrEMBL
other Location (Reliability: 3)
A0A0B2NV13_GLYSO
1370
0
150704
TrEMBL
other Location (Reliability: 2)
A0A151TVH6_CAJCA
1364
0
149985
TrEMBL
other Location (Reliability: 2)
A0A1S7RL53_9RHIZ
177
0
18827
TrEMBL
-
A0A2R4SC65_CAMSI
1348
0
147453
TrEMBL
other Location (Reliability: 4)
A0A1S7N1Z9_9RHIZ
177
0
18846
TrEMBL
-
B9SD65_RICCO
585
0
64796
TrEMBL
other Location (Reliability: 2)
A0A151TVQ2_CAJCA
1372
0
150225
TrEMBL
other Location (Reliability: 2)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by affinity chromatography with nickel-nitrilotriacetic acid-agarose under native conditions, further purification by anion exchange chromatography
DEAE-Sepharose column chromatography, Ni-IDA resin column chromatography, and Superdex 200 gel filtration
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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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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
during a progressively (but not rapidly) induced drought, the level of AO3 transcript increases significantly in the roots and leaves
gene expression is induced by osmotic stress caused by treatment with PEG 6000 (100-400 mOsm)
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Seo, M.; Peeters, A.J.M.; Koiwai, H.; Oritani, T.; Marion-Poll, A.; Zeevaart, J.A.D.; Koornneef, M.; Kamiya, Y.; Koshiba, T.
The Arabidopsis aldehyde oxidase 3 (AAO3) gene product catalyzes the final step in abscisic acid biosynthesis in leaves
Proc. Natl. Acad. Sci. USA
97
12908-12913
2000
Arabidopsis sp.
brenda
Leydecker, M.T.; Moureaux, T.; Kraepiel, Y.; Schnorr, K.; Caboche, M.
Molybdenum cofactor mutants, specifically impaired in xanthine dehydrogenase activity and abscisic acid biosynthesis, simultaneously overexpress nitrate reductase
Plant Physiol.
107
1427-1431
1995
Nicotiana plumbaginifolia
brenda
Zdunek, E.; Lips, S.H.
Transport and accumulation rates of abscisic acid and aldehyde oxidase activity in Pisum sativum L. in response to suboptimal growth conditions
J. Exp. Bot.
52
1269-1276
2001
Pisum sativum
brenda
Seo, M.; Aoki, H.; Koiwai, H.; Kamiya, Y.; Nambara, E.; Koshiba, T.
Comparative studies on the Arabidopsis aldehyde oxidase (AAO) gene family revealed a major role of AAO3 in ABA biosynthesis in seeds
Plant Cell Physiol.
45
1694-1703
2004
Arabidopsis sp.
brenda
Sagi, M.; Fluhr, R.; Lips, S.H.
Aldehyde oxidase and xanthine dehydrogenase in a flacca tomato mutant with deficient abscisic acid and wilty phenotype
Plant Physiol.
120
571-577
1999
Solanum lycopersicum
brenda
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)
brenda
Gonzalez-Guzman, M.; Abia, D.; Salinas, J.; Serrano, R.; Rodriguez, P.L.
Two new alleles of the abscisic aldehyde oxidase 3 gene reveal its role in abscisic acid biosynthesis in seeds
Plant Physiol.
135
325-333
2004
Arabidopsis sp.
brenda
Marin, E.; Marion-Poll, A.
Tomato flacca mutant is impaired in ABA aldehyde oxidase and xanthine dehydrogenase activities
Plant Physiol. Biochem.
35
369-372
1997
Solanum lycopersicum
-
brenda
Szepesi, A.; Csiszar, J.; Gemes, K.; Horvath, E.; Horvath, F.; Simon, M.L.; Tari, I.
Salicylic acid improves acclimation to salt stress by stimulating abscisic aldehyde oxidase activity and abscisic acid accumulation, and increases Na+ content in leaves without toxicity symptoms in Solanum lycopersicum L
J. Plant Physiol.
166
914-925
2009
Solanum lycopersicum
brenda
Galle, A.; Csiszar, J.; Benyo, D.; Laskay, G.; Leviczky, T.; Erdei, L.; Tari, I.
Isohydric and anisohydric strategies of wheat genotypes under osmotic stress: Biosynthesis and function of ABA in stress responses
J. Plant Physiol.
170
1389-1399
2013
Triticum aestivum
brenda
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)
brenda
Karppinen, K.; Hirvelae, E.; Nevala, T.; Sipari, N.; Suokas, M.; Jaakola, L.
Changes in the abscisic acid levels and related gene expression during fruit development and ripening in bilberry (Vaccinium myrtillus L.)
Phytochemistry
95
127-134
2013
Vaccinium myrtillus
brenda
Chen, Q.F.; Ya, H.Y.; Feng, Y.R.; Jiao, Z.
Expression of the key genes involved in ABA biosynthesis in rice implanted by ion beam
Appl. Biochem. Biotechnol.
173
239-247
2014
Oryza sativa
brenda
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)
brenda
Zdunek-Zastocka, E.; Sobczak, M.
Expression of Pisum sativum PsAO3 gene, which encodes an aldehyde oxidase utilizing abscisic aldehyde, is induced under progressively but not rapidly imposed drought stress
Plant Physiol. Biochem.
71
57-66
2013
Pisum sativum (B0LB01), Pisum sativum
brenda
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