Information on EC 2.6.1.76 - diaminobutyrate-2-oxoglutarate transaminase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.6.1.76
-
RECOMMENDED NAME
GeneOntology No.
diaminobutyrate-2-oxoglutarate transaminase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-2,4-diaminobutanoate + 2-oxoglutarate = L-aspartate 4-semialdehyde + L-glutamate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amino group transfer
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
ectoine biosynthesis
-
-
ectoine degradation
-
-
Glycine, serine and threonine metabolism
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-
Metabolic pathways
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-
Microbial metabolism in diverse environments
-
-
norspermidine biosynthesis
-
-
pyoverdine I biosynthesis
-
-
rhizobactin 1021 biosynthesis
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threonine metabolism
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-
SYSTEMATIC NAME
IUBMB Comments
L-2,4-diaminobutanoate:2-oxoglutarate 4-aminotransferase
A pyridoxal-phosphate protein that requires potassium for activity [4]. In the proteobacterium Acinetobacter baumannii, this enzyme is cotranscribed with the neighbouring ddc gene that also encodes EC 4.1.1.86, diaminobutyrate decarboxylase. Differs from EC 2.6.1.46, diaminobutyrate---pyruvate transaminase, which has pyruvate as the amino-group acceptor. This is the first enzyme in the ectoine-biosynthesis pathway, the other enzymes involved being EC 2.3.1.178, diaminobutyrate acetyltransferase and EC 4.2.1.108, ectoine synthase [3,4].
CAS REGISTRY NUMBER
COMMENTARY hide
196622-96-5
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
3 ATCC 19004
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-
Manually annotated by BRENDA team
ATCC 17906
-
-
Manually annotated by BRENDA team
ATCC 17909
-
-
Manually annotated by BRENDA team
ATCC 17908
-
-
Manually annotated by BRENDA team
ATCC 15309
-
-
Manually annotated by BRENDA team
IAM13186
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-
Manually annotated by BRENDA team
Rd, types a, b, d, e, f
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-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-aminobutanoate + 2-oxoglutarate
? + L-glutamate
show the reaction diagram
beta-alanine + 2-oxoglutaric acid
?
show the reaction diagram
-
-
-
-
?
L-2,4-diaminobutanoate + 2-oxoglutarate
L-aspartate 4-semialdehyde + L-glutamate
show the reaction diagram
L-2,4-diaminobutyric acid + 2-oxoglutaric acid
L-glutamic acid + L-aspartic beta-semialdehyde
show the reaction diagram
L-aspartate 4-semialdehyde + L-glutamate
L-2,4-diaminobutanoate + 2-oxoglutarate
show the reaction diagram
L-aspartate 4-semialdehyde + L-homoserine
L-2,4-diaminobutanoate + 2-oxoglutarate
show the reaction diagram
about 5% of the activity with L-glutamate
-
-
r
L-glutamic acid + L-aspartic beta-semialdehyde
L-2,4-diaminobutyric acid + 2-oxoglutaric acid
show the reaction diagram
L-lysine + oxaloacetic acid
?
show the reaction diagram
-
-
-
-
?
L-ornithine + 2-oxoglutarate
? + L-glutamate
show the reaction diagram
L-ornithine + pyruvic acid
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K+
-
required
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.21 - 1.07
2-oxoglutarate
1.46
2-oxoglutaric acid
-
-
0.04 - 0.09
L-2,4-diaminobutanoate
4.3
L-2,4-diaminobutyric acid
-
-
4.5
L-aspartate 4-semialdehyde
-
pH 8.5, 25°C
9.1
L-glutamate
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pH 8.5, 25°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4.5 - 25.2
2-oxoglutarate
120 - 221
L-2,4-diaminobutanoate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4 - 120
2-oxoglutarate
34
1333 - 5535
L-2,4-diaminobutanoate
2561
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
12
-
pH 8.5, 25°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.2
-
isoelectric focussing
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
44000
-
6 * 44000, SDS-PAGE
45000
-
4 * 45000, SDS-PAGE
47420
-
deduced from nucleotide sequence
49400
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predicted from amino acid sequence, gene HI0949
56200
-
predicted from amino acid sequence, gene HI946
188000
-
native enzyme, gel filtration
260000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
tetramer
-
4 * 45000, SDS-PAGE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme, overexpressed in Escherichia coli
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Escherichia coli clone carrying the dat homolog of H. influenzae
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homologs of dat detected by PCR amplification
identification and analysis of the dat gene encoding L-2,4-diaminobutyrate:2-ketoglutarate 4-aminotransferase with Escherichia coli transformants
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D180V
-
about 2fold increase in ectoine production by strains harboring the ectABC gene cluster containing the mutant
D180V/E36V
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double mutant displays less activity than mutant D180V
D180V/F320Y/Q325R
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about 2.1-3.3fold increase in ectoine production by strains harboring the ectABC gene cluster containing the mutant
E36V
-
about 1.5fold increase in ectoine production by strains harboring the ectABC gene cluster containing the mutant
D180V
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about 2fold increase in ectoine production by strains harboring the ectABC gene cluster containing the mutant
-
D180V/E36V
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double mutant displays less activity than mutant D180V
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D180V/F320Y/Q325R
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about 2.1-3.3fold increase in ectoine production by strains harboring the ectABC gene cluster containing the mutant
-
E36V
-
about 1.5fold increase in ectoine production by strains harboring the ectABC gene cluster containing the mutant
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
synthesis
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