Information on EC 1.1.1.288 - xanthoxin dehydrogenase

Word Map on EC 1.1.1.288
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)

The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.1.1.288
-
RECOMMENDED NAME
GeneOntology No.
xanthoxin dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
xanthoxin + NAD+ = abscisic aldehyde + NADH + H+
show the reaction diagram
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
abscisic acid biosynthesis
-
-
Carotenoid biosynthesis
-
-
Metabolic pathways
-
-
Biosynthesis of secondary metabolites
-
-
SYSTEMATIC NAME
IUBMB Comments
xanthoxin:NAD+ oxidoreductase
Requires a molybdenum cofactor for activity. NADP+ cannot replace NAD+ and short-chain alcohols such as ethanol, isopropanol, butanol and cyclohexanol cannot replace xanthoxin as substrate [3]. Involved in the abscisic-acid biosynthesis pathway in plants, along with EC 1.2.3.14 (abscisic-aldehyde oxidase), EC 1.13.11.51 (9-cis-epoxycarotenoid dioxygenase) and EC 1.14.13.93 [(+)-abscisic acid 8'-hydroxylase]. Abscisic acid is a sesquiterpenoid plant hormone that is involved in the control of a wide range of essential physiological processes, including seed development, germination and responses to stress [3].
CAS REGISTRY NUMBER
COMMENTARY hide
129204-37-1
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Duchesne
-
-
Manually annotated by BRENDA team
Duchesne
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
the aba2 mutant displays less seed dormancy, glucose insensitivity, small plat size, early flowering, and wiltness, no complementation by expression of AtSDR3, enotype, overview
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
xanthoxin + NAD+
abscisic aldehyde + NADH + H+
show the reaction diagram
additional information
?
-
different mutants: mutations in genes involved in the ethylene signal transduction pathway and a mutation at the start of exon 2
-
-
-
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
xanthoxin + NAD+
abscisic aldehyde + NADH + H+
show the reaction diagram
additional information
?
-
Q9C826
different mutants: mutations in genes involved in the ethylene signal transduction pathway and a mutation at the start of exon 2
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
2.1fold reduced expression in Arabidopsis thaliana mutant aba2 with a mutation at the the start of exon 2
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0202
xanthoxin
-
-
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
-
no significant activity is observed in chloroplast
-
Manually annotated by BRENDA team
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Pichia pastoris
-
gene ABA2, encodes a short-chain dehydrogenase/reductase1 (SDR1) that catalyzes the multistep conversion of xanthoxin to abscisic aldehyde during abscisic acid biosynthesis in Arabidopsis thalian, genotyping
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information