Information on EC 2.6.1.76 - diaminobutyrate-2-oxoglutarate transaminase

2,4-diaminobutyrate 4-aminotransferase

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2,4-diaminobutyrate aminotransferase

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DABA aminotransferase

DABA AT

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DABA-AT

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DABA:2-KG 4 aminotransferase

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Diaminobutyrate transaminase

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EctB

6 entries

L-2,4-diaminobutyrate:2-ketoglutarate 4-aminotransferase

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L-diaminobutyric acid transaminase

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additional information

Glycine, serine and threonine metabolism, Microbial metabolism in diverse environments

L-2,4-diaminobutanoate + 2-oxoglutarate = L-aspartate 4-semialdehyde + L-glutamate

Acinetobacter baumannii

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amino group transfer

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BRENDA

threonine metabolism

KEGG

MetaCyc

baumannoferrin biosynthesis, ectoine biosynthesis, ectoine degradation, norspermidine biosynthesis, pyoverdine I biosynthesis, rhizobactin 1021 biosynthesis

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].

196622-96-5

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4-aminobutanoate + 2-oxoglutarate

? + L-glutamate

about 60% of the activity with L-2,4-diaminobutanoate

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r

beta-alanine + 2-oxoglutaric acid

?

-

-

?

L-2,4-diaminobutanoate + 2-oxoglutarate

L-aspartate 4-semialdehyde + L-glutamate

7 entries

L-2,4-diaminobutyric acid + 2-oxoglutaric acid

L-glutamic acid + L-aspartic beta-semialdehyde

10 entries

L-aspartate 4-semialdehyde + L-glutamate

L-2,4-diaminobutanoate + 2-oxoglutarate

-

-

r

L-aspartate 4-semialdehyde + L-homoserine

L-2,4-diaminobutanoate + 4-hydroxy-2-oxobutanoic acid

about 5% of the activity with L-glutamate

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r

L-glutamic acid + L-aspartic beta-semialdehyde

L-2,4-diaminobutyric acid + 2-oxoglutaric acid

10 entries

L-lysine + oxaloacetic acid

?

-

-

?

L-ornithine + 2-oxoglutarate

? + L-glutamate

about 6% of the activity with L-2,4-diaminobutanoate

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r

L-ornithine + pyruvic acid

?

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-

?

additional information

?

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L-2,4-diaminobutanoate + 2-oxoglutarate

L-aspartate 4-semialdehyde + L-glutamate

pyridoxal 5'-phosphate

K+

required

KCl

activates slightly at up to 350 mM, inhibits by 50% at 1.5 M

NaCl

activates slightly at up to 350 mM, inhibits by 50% at 1.25 M

KCl

activates slightly at up to 350 mM, inhibits by 50% at 1.5 M

NaCl

activates slightly at up to 350 mM, inhibits by 50% at 1.25 M

0.21 - 9.01

2-oxoglutarate

4 entries

1.46

2-oxoglutaric acid

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0.04 - 0.43

L-2,4-diaminobutanoate

4 entries

4.3

L-2,4-diaminobutyric acid

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4.5

L-aspartate 4-semialdehyde

pH 8.5, 25Â°C

9.1

L-glutamate

pH 8.5, 25Â°C

additional information

Michaelis-Menten kinetics

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4.5 - 25.2

2-oxoglutarate

120 - 221

L-2,4-diaminobutanoate

4 - 120

2-oxoglutarate

1333 - 5535

L-2,4-diaminobutanoate

12

pH 8.5, 25Â°C

6.5

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8.25 - 8.75

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8.5

MH020163

assay at

8.6

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5.5 - 10

40% of maximal activity within this range

20

MH020163

assay at

25

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45

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10 - 60

activity range, profile overview

6.2

isoelectric focussing

Acinetobacter calcoaceticus

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288731, 288732

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Acinetobacter genospecies

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3 ATCC 19004

Acinetobacter haemolyticus

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ATCC 17906

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Acinetobacter johnsonii

ATCC 17909

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Acinetobacter junii

ATCC 17908

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Acinetobacter lwoffii

ATCC 15309

Acinetobacter radioresistens

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IAM13186

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Acinetobacter radioresistens IAM13186

IAM13186

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756904

MH020163

GenBank

Alkalihalobacillus clausii NIOT-DSB04

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756904

MH020163

GenBank

Rd, types a, b, d, e, f

288732

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CGMCC 1.6329

UniProt

isolated from the effluent of a hot spring in the Yellowstone National Park (United States)

UniProt

Paenibacillus lautus Y412MC10

isolated from the effluent of a hot spring in the Yellowstone National Park (United States)

UniProt

metabolism

evolution

additional information

Chromohalobacter salexigens DSM 3043

6rl5, download, 3D-view

SCOPe (6rl5)

CATH (6rl5)

Q9ZEU7

188000

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native enzyme, gel filtration

200000

about, recombinant Strep II-tagged enzyme, gel filtration

260000

gel filtration

44000

6 * 44000, SDS-PAGE

45000

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4 * 45000, SDS-PAGE

47420

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deduced from nucleotide sequence

49400

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predicted from amino acid sequence, gene HI0949

288732

56200

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predicted from amino acid sequence, gene HI946

hexamer

6 * 44000, SDS-PAGE

homotetramer

tetramer

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4 * 45000, SDS-PAGE

E36V

about 1.5fold increase in ectoine production by strains harboring the ectABC gene cluster containing the mutant

D180V

about 2fold increase in ectoine production by strains harboring the ectABC gene cluster containing the mutant

D180V/E36V

double mutant displays less activity than mutant D180V

D180V/F320Y/Q325R

about 2.1-3.3fold increase in ectoine production by strains harboring the ectABC gene cluster containing the mutant

E36V

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about 1.5fold increase in ectoine production by strains harboring the ectABC gene cluster containing the mutant

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D180V

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about 2fold increase in ectoine production by strains harboring the ectABC gene cluster containing the mutant

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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

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K274A

site-directed mutagenesis, the mutant is unable to bind cofactor PLP and ins catalytically inactive

K274R

site-directed mutagenesis, the mutant is unable to bind cofactor PLP and ins catalytically inactive

K274H

site-directed mutagenesis, the mutant is unable to bind cofactor PLP and ins catalytically inactive. This amino acid substitution does not affect the quaternary assembly of the mutant protein

K274A

Paenibacillus lautus Y412MC10

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site-directed mutagenesis, the mutant is unable to bind cofactor PLP and ins catalytically inactive

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K274R

Paenibacillus lautus Y412MC10

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site-directed mutagenesis, the mutant is unable to bind cofactor PLP and ins catalytically inactive

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K274H

Paenibacillus lautus Y412MC10

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site-directed mutagenesis, the mutant is unable to bind cofactor PLP and ins catalytically inactive. This amino acid substitution does not affect the quaternary assembly of the mutant protein

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recombinant enzyme, overexpressed in Escherichia coli

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recombinant Strep II-tagged enzyme from Escherichia coli by streptavidin-affinity chromatography

cloned into the expression vector pQE30 with a 6His-tag and expressed in Escherichia coli JM109 M15 cells

MH020163

756904

Escherichia coli clone carrying the dat homolog of H. influenzae

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288732

gene ectB, genetic structure, recombinant overexpression of codon-optimized version of (Pl)ectB as N-terminally Strep II-tagged protein from modified plasmid pLC52 in Escherichia coli strain BL21 and TOP 10 cells

homologs of dat detected by PCR amplification

7 entries

identification and analysis of the dat gene encoding L-2,4-diaminobutyrate:2-ketoglutarate 4-aminotransferase with Escherichia coli transformants

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