Information on EC 1.14.11.15 - gibberellin 3beta-dioxygenase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.14.11.15
-
RECOMMENDED NAME
GeneOntology No.
gibberellin 3beta-dioxygenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
gibberellin 20 + 2-oxoglutarate + O2 = gibberellin 1 + succinate + CO2
show the reaction diagram
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
gibberellin biosynthesis III (early C-13 hydroxylation)
-
-
Diterpenoid biosynthesis
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Metabolic pathways
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Biosynthesis of secondary metabolites
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SYSTEMATIC NAME
IUBMB Comments
(gibberellin-20),2-oxoglutarate:oxygen oxidoreductase (3beta-hydroxylating)
Requires Fe2+ and ascorbate.
CAS REGISTRY NUMBER
COMMENTARY hide
116036-68-1
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
gene GA4
SwissProt
Manually annotated by BRENDA team
gene GA4
-
-
Manually annotated by BRENDA team
cultivar Harrington
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
enzyme inhibition results in growth retardation, phenotype, 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
gibberellin 20 + 2-oxoglutarate + O2
gibberellin 1 + succinate + CO2
show the reaction diagram
-
-
-
-
?
gibberellin a15 + 2-oxoglutarate + O2
gibberellin a37 + succinate + CO2
show the reaction diagram
-
-
-
?
gibberellin A20 + 2-oxoglutarate + O2
gibberellin + succinate + CO2
show the reaction diagram
-
20-oxidation is the limiting step, rather than 3beta-hydroxylation, in the formation of gibberelin A1 in elongating shoots of hybrid aspen
-
-
?
gibberellin a20 + 2-oxoglutarate + O2
gibberellin a1 + succinate + CO2
show the reaction diagram
gibberellin a44 + 2-oxoglutarate + O2
gibberellin a38 + succinate + CO2
show the reaction diagram
-
-
-
?
gibberellin a5 + 2-oxoglutarate + O2
gibberellin a3 + succinate + CO2
show the reaction diagram
-
-
-
?
gibberellin A5 + 2-oxoglutarate + O2
gibberellin A6 + succinate + CO2
show the reaction diagram
-
-
-
-
?
gibberellin a9 + 2-oxoglutarate + O2
gibberellin a4 + succinate + CO2
show the reaction diagram
gibberellin a9 + 2-oxoglutarate + O2
gibberellin a5 + succinate + CO2
show the reaction diagram
-
-
-
?
additional information
?
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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
gibberellin 20 + 2-oxoglutarate + O2
gibberellin 1 + succinate + CO2
show the reaction diagram
-
-
-
-
?
gibberellin A20 + 2-oxoglutarate + O2
gibberellin + succinate + CO2
show the reaction diagram
-
20-oxidation is the limiting step, rather than 3beta-hydroxylation, in the formation of gibberelin A1 in elongating shoots of hybrid aspen
-
-
?
gibberellin a20 + 2-oxoglutarate + O2
gibberellin a1 + succinate + CO2
show the reaction diagram
gibberellin a9 + 2-oxoglutarate + O2
gibberellin a4 + succinate + CO2
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ascorbate
-
5 mM, 10fold stimulation
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe3+
-
activation in the presence of ascorbate
additional information
-
150 mM NaCl represses the gibberellin 3-oxidase 1 gene in the wild-type and in the NTL8-deficient mutant (NTL8 acts downstream of the gibberellin biosynthesis), repression is present but less significant in aba3-1 mutant, deficient in the stress hormone abscisic acid (independent pathway dominates), expression of GA3ox1 is recovered after a longer incubation in NaCl and leads to germination
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
13-O-acetyl-16,17-dihydrogibberellin A5
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competitive, 50% inhibition of activity with gibberellin A20: 0.008 mM
13-O-acetylgibberellin A5
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competitive, 50% inhibition of activity with gibberellin A20: 0.004 mM
16,17-dihydrogibberellin A20
-
competitive, 50% inhibition of activity with gibberellin A20: 0.05 mM
16,17-dihydrogibberellin A5
-
competitive, 50% inhibition of activity with gibberellin A20: 0.192 mM
16-Deoxo-2,3-di-dehydro-3-methyl-deoxygibberellin C
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16-Deoxo-deoxygibberellin C
17-ethyl-16,17-dihydrogibberellin A5
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competitive, 50% inhibition of activity with gibberellin A20: 0.009 mM
17-methyl-16,17-dihydrogibberellin A5
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competitive, 50% inhibition of activity with gibberellin A20: 0.002 mM
17-n-propyl-16,17-dihydrogibberellin A5
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competitive, 50% inhibition of activity with gibberellin A20: 0.007 mM
2,2'-bipyridyl
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2,3-Didehydro-3-methyl-deoxygibberellin C
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2,3-didehydro-3-methyl-gibberellin a9
2,3-methyl-gibberellin a5
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3-methyl-gibberellin a5
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Cd2+
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0.5 mM, strong
Co2+
-
0.5 mM, strong
Cu2+
-
0.5 mM, strong
Deoxygibberellin C
endo-16,17-dihydro gibberellin A5
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competitive inhibitor of 3beta-hydroxylation of gibberellin A20
exo-16,17-dihydro gibberellin A20
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competitive inhibitor of 3beta-hydroxylation of gibberellin A20
exo-16,17-dihydro gibberellin A5
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competitive inhibitor of 3beta-hydroxylation of gibberellin A20
gibberellin
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the enzyme is negatively feedback regulated by high total active gibberellin levels
gibberellin a15
-
inhibits 3beta-hydroxylation of gibberellin a20
gibberellin a20
gibberellin a4
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treatment causes down-regulation of gibberellin-insensitive dwarf 1, gibberellin A20 oxidase, and gibberellin 3beta-dioxygenase as well as degradation of DELLA1 protein
gibberellin a44
-
inhibits 3beta-hydroxylation of gibberellin a20
gibberellin a5
gibberellin a9
-
inhibits 3beta-hydroxylation of gibberellin a20
Hg2+
-
0.5 mM, strong
Hydrocinnamic acid
indole acetic acid
indole propionic acid
Mn2+
-
0.5 mM, strong
Ni2+
-
0.5 mM, strong
trinexapac ethyl
-
competitive, 50% inhibition of activity with gibberellin A20: 0.3 mM
Zn2+
-
0.5 mM, strong
additional information
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ascorbate
bovine serum albumin
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2 mg/ml, 30% activation of purified enzyme, stimulation by bovine serum albumin and catalase is additive and less pronounced in crude cell extract
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catalase
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0.5 mg/ml, 30% activation of purified enzyme, stimulation by catalase and bovine serum albumin is additive and less pronounced in crude cell extract
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DTT
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stimulates. Stimulation is negated when added together with DTT
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.25
2-oxoglutarate
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with gibberellin a20 as cosubstrate
0.0087
gibberellin a15
-
-
0.00029 - 0.01
gibberellin a20
0.00033 - 0.00125
gibberellin a9
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0216
wild type enzyme from soluble cell fraction, in 100 mM Tris-HCl pH 7.9 containing 4 mM ascorbate, 4 mM DTT, 4 mM 2-oxoglutarate, 0.5 mM FeSO4, 2 mg/ml bovine serum albumin and 1 mg/ml catalase
0.259
wild type enzyme after 12fold purification, in 100 mM Tris-HCl pH 7.9 containing 4 mM ascorbate, 4 mM DTT, 4 mM 2-oxoglutarate, 0.5 mM FeSO4, 2 mg/ml bovine serum albumin and 1 mg/ml catalase
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 9
-
activity is reduced appreciably below pH 6 and above pH 9
7 - 9
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about half-maximal activity at pH 7.0 and pH 9.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
mRNA level is minimally detectable in prepolinated pericarp, increases dramatically after polination, then decreases by by 1 day after anthesis. Expression is hormonally regulated; mRNA levels gradually increases from day 2 to 3 after anthesis when seeds are present. When seeds are removed the pericarp transcript level dramatically declines
Manually annotated by BRENDA team
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mRNA level is minimally detectable in prepolinated ovule, increases dramatically after polination, then decreases by by 1 day after anthesis
Manually annotated by BRENDA team
in internodes, as well as nodes and the ear of the elongating stem; in internodes, as well as nodes and the ear of the elongating stem; in internodes, as well as nodes and the ear of the elongating stem
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
39100
gel filtration
42000
-
gel filtration
58000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 40000-50000, SDS-PAGE
monomer
-
1 * 42000, SDS-PAGE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.3
80% activity in phosphate buffer at pH 6.3
672812
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
C18-reverse HPLC column chromatography
-
high performance liquid chromatography; high performance liquid chromatography; high performance liquid chromatography
immobilised metal affinity chromatography and Superdex 200 gel filtration
partial
recombinant maltose-binding protein-fused enzyme from Escherichia coli by amylose affinity chromatography
rosette leaves are frozen in liquid nitrogen and ground to a fine powder, protein extracted with 50 mM Tris-HCl, pH 8.0, containing 200 mM NaCl, 5 mM EDTA, 0.1% Tween 20 and a proteinase inhibitor mixture, SDS-PAGE
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transgenic plants are ground in liquid nitrogen, total cellular extracts suspended in 1X SDS-PAGE sample loading buffer
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
expressed in Escherichia coli strain BL21; expressed in Escherichia coli strain BL21; expressed in Escherichia coli strain BL21
expression as a GST-fusion protein in Escherichia coli
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expression in Escherichia coli
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for the NTL8 complementation test, a sequence containing the NTL8 gene with its promoter is subcloned into pKGWFS7 Gateway vector, for histochemical staining an NTL8 promoter region is transcriptionally fused to the GUS-coding sequence, the fusion product transformed into Arabidopsis
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gene GA4, expression as maltose-binding protein-fusion protein in Escherichia coli
overexpression in Nicotiana tabacum
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the anti gibberellin 24 single monoclonal antibody gene (anti-GA24 scFv) is PCR-amplified with plasmid pH1L24B and introduced into the binary vector pBI-ER-D, transferred into Agrobacterium tumefaciens strain LBA4404 to transform Arabidospsis thaliana, the antibody is fused with the green fluorescence protein (GFP), a c-myc epitope tag and KDEL ER-retention signal
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two gibberellin 3beta-hydroxylase genes, OsGA3ox1 and OsGA3ox2, expression in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
G126D
amino acid change responsible for dwarf phenotype. Exogenously added gibberellic acid restores normal growth
additional information