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Information on EC 2.6.1.42 - branched-chain-amino-acid transaminase and Organism(s) Escherichia coli and UniProt Accession P0AB80

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EC Tree
     2 Transferases
         2.6 Transferring nitrogenous groups
             2.6.1 Transaminases
                2.6.1.42 branched-chain-amino-acid transaminase
IUBMB Comments
Also acts on L-isoleucine and L-valine, and thereby differs from EC 2.6.1.6, leucine transaminase, which does not. It also differs from EC 2.6.1.66, valine---pyruvate transaminase.
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This record set is specific for:
Escherichia coli
UNIPROT: P0AB80
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The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
bcat1, bcatm, branched-chain aminotransferase, bcatc, bcat2, branched-chain amino acid aminotransferase, branched chain aminotransferase, hbcat, hbcatm, branched-chain amino acid transaminase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
branched chain aminotransferase
-
branched-chain amino acid aminotransferase
-
branched chain aminotransferase
-
-
branched-chain amino acid aminotransferase
-
-
-
-
branched-chain amino acid-glutamate transaminase
-
-
-
-
branched-chain aminotransferase
glutamate-branched-chain amino acid transaminase
-
-
-
-
L-branched chain amino acid aminotransferase
-
-
-
-
transaminase B
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-leucine + 2-oxoglutarate = 4-methyl-2-oxopentanoate + L-glutamate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amino group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
branched-chain-amino-acid:2-oxoglutarate aminotransferase
Also acts on L-isoleucine and L-valine, and thereby differs from EC 2.6.1.6, leucine transaminase, which does not. It also differs from EC 2.6.1.66, valine---pyruvate transaminase.
CAS REGISTRY NUMBER
COMMENTARY hide
9054-65-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-oxobutyrate + L-glutamate
2-aminobutyrate + 2-oxoglutarate
show the reaction diagram
-
-
-
r
2-oxohexanoate + L-glutamate
L-norleucine + 2-oxoglutarate
show the reaction diagram
-
-
-
?
2-oxohexanoate + L-glutamate
norleucine + 2-oxoglutarate
show the reaction diagram
-
-
-
r
2-oxoisocaproate + L-glutamate
L-leucine + 2-oxoglutarate
show the reaction diagram
-
-
-
?
2-oxoisovalerate + L-glutamate
L-valine + 2-oxoglutarate
show the reaction diagram
-
-
-
?
2-oxovalerate + L-glutamate
L-norvaline + 2-oxoglutarate
show the reaction diagram
-
-
-
?
2-oxovalerate + L-glutamate
norvaline + 2-oxoglutarate
show the reaction diagram
-
-
-
r
3-methyl-2-oxopentanoate + L-glutamate
L-isoleucine + 2-oxoglutarate
show the reaction diagram
4,4-dimethyl-2-oxopentanoate + L-glutamate
L-neopentylglycine + 2-oxoglutarate
show the reaction diagram
-
-
-
?
4,4-dimethyl-2-oxovalerate + L-glutamate
L-neopentylglycine + 2-oxoglutarate
show the reaction diagram
-
-
-
r
4-methyl-2-oxopentanoate + L-glutamate
L-leucine + 2-oxoglutarate
show the reaction diagram
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
show the reaction diagram
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
show the reaction diagram
-
-
-
r
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
show the reaction diagram
-
-
-
r
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
show the reaction diagram
-
-
-
r
L-tryptophan + 2-oxoglutarate
2-oxo-3-indolylpropanoate + L-glutamate
show the reaction diagram
-
-
-
r
L-tyrosine + 2-oxoglutarate
4-hydroxyphenylpyruvate + L-glutamate
show the reaction diagram
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
show the reaction diagram
-
-
-
r
trimethylpyruvate + L-glutamate
L-tert-Leu + 2-oxoglutarate
show the reaction diagram
-
-
-
r
2-(3-hydroxy-1-adamantyl)-2-oxoethanoic acid + L-glutamate
3-hydroxyadamantylglycine + 2-oxoglutarate
show the reaction diagram
-
-
-
-
?
2-oxo-6-hydroxyhexanoic acid + L-glutamate
L-6-hydroxynorleucine + 2-oxoglutarate
show the reaction diagram
-
-
-
-
?
3-methyl-2-oxobutyric acid + L-glutamate
L-valine + 2-oxoglutarate
show the reaction diagram
-
-
-
-
?
3-methyl-2-oxovaleric acid + L-glutamate
L-isoleucine + 2-oxoglutarate
show the reaction diagram
-
-
-
-
?
4-methyl-2-oxovaleric acid + L-glutamate
L-leucine + 2-oxoglutarate
show the reaction diagram
-
-
-
-
?
L-isoleucine + 2-oxobutanoate
3-methyl-2-oxopentanoate + 2-aminobutanoate
show the reaction diagram
-
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
show the reaction diagram
-
-
-
-
r
L-isoleucine + 3-methyl-2-oxobutanoate
3-methyl-2-oxopentanoate + L-valine
show the reaction diagram
-
-
-
-
r
L-isoleucine + 3-methylthio-2-oxobutanoate
3-methyl-2-oxopentanoate + 2-amino-3-methylthiobutanoate
show the reaction diagram
-
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
show the reaction diagram
L-leucine + 3-methyl-2-oxobutanoate
4-methyl-2-oxopentanoate + L-valine
show the reaction diagram
-
-
-
-
r
L-leucine + 3-methyl-2-oxopentanoate
4-methyl-2-oxopentanoate + L-isoleucine
show the reaction diagram
-
-
-
-
r
L-methionine + 2-oxoglutarate
4-methylsulfanyl-2-oxobutanoate + L-glutamate
show the reaction diagram
L-norleucine + 2-oxoglutarate
2-oxohexanoate + L-glutamate
show the reaction diagram
-
-
-
r
L-norvaline + 2-oxoglutarate
2-oxopentanoate + L-glutamate
show the reaction diagram
-
-
-
-
r
L-phenylalanine + 2-oxoglutarate
phenylpyruvate + L-glutamate
show the reaction diagram
-
-
-
-
r
L-tryptophan + 2-oxoglutarate
2-oxo-3-indolylpropanoate + L-glutamate
show the reaction diagram
-
-
-
-
r
L-tyrosine + 2-oxoglutarate
p-hydroxyphenylpyruvate + L-glutamate
show the reaction diagram
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
show the reaction diagram
-
-
-
-
r
L-valine + 3-methyl-2-oxopentanoate
3-methyl-2-oxobutanoate + L-isoleucine
show the reaction diagram
-
-
-
-
r
trimethylpyruvate + L-glutamate
L-tert-leucine + 2-oxoglutarate
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
show the reaction diagram
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
show the reaction diagram
-
-
-
r
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
show the reaction diagram
-
-
-
r
L-isoleucine + 2-oxoglutarate
3-methyl-2-oxopentanoate + L-glutamate
show the reaction diagram
-
-
-
-
r
L-leucine + 2-oxoglutarate
4-methyl-2-oxopentanoate + L-glutamate
show the reaction diagram
L-valine + 2-oxoglutarate
3-methyl-2-oxobutanoate + L-glutamate
show the reaction diagram
-
-
-
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
pyridoxal 5'-phosphate
-
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-Oxohexanoate
inhibition of transamination by the oxo substrate at below 10 mM
4,4-dimethyl-2-oxovalerate
inhibition of transamination by the oxo substrate at below 10 mM
4-methyl-2-oxovalerate
inhibition of transamination by the oxo substrate at below 10 mM
L-glutamate
inhibition of transamination by the oxo substrate at above 200 mM
2-Ketoglutarate
2-oxoglutarate
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.6
2-oxoglutarate
pH 8.0, 25°C
0.22
2-Oxohexanoate
pH 8.0, 37°C
0.08
2-oxoisocaproate
pH 8.0, 37°C
0.2
2-oxoisovalerate
pH 8.0, 37°C
0.6
2-oxovalerate
pH 8.0, 37°C
0.07
3-methyl-2-oxopentanoate
pH 8.0, 37°C
0.08
4,4-dimethyl-2-oxopentanoate
pH 8.0, 37°C
20.9 - 26.5
L-glutamate
0.42
L-leucine
pH 8.0, 25°C
7.38
2-(3-hydroxy-1-adamantyl)-2-oxoethanoic acid
-
pH 8.0, 37°C
0.24 - 6.6
2-oxoglutarate
0.56
2-Oxoisohexanoate
-
pH 8.0, 37°C
0.56
2-oxoisopentanoate
-
pH 8.0, 37°C
1.64
3-methyl-2-oxobutyric acid
-
pH 8.0, 37°C
0.99
3-methyl-2-oxovaleric acid
-
pH 8.0, 37°C
0.42
4-methyl-2-oxovaleric acid
-
pH 8.0, 37°C
0.2
DL-2-oxo-3-methyl-n-pentanoate
-
pH 8.0, 37°C
0.42 - 2.7
L-isoleucine
0.58 - 2.2
L-leucine
19
L-methionine
-
pH 8.0, 25°C, 2-oxoglutarate as amino group acceptor
0.89
L-phenylalanine
72
L-tryptophan
-
pH 8.0, 25°C, 2-oxoglutarate as amino group acceptor
7
L-tyrosine
-
pH 8.0, 25°C, 2-oxoglutarate as amino group acceptor
2.7 - 3.13
L-valine
0.09
trimethylpyruvate
-
pH 8.0, 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.37
2-oxobutyrate
pH 8.0, 25°C
0.22 - 23.1
2-Oxohexanoate
24.7
2-oxoisocaproate
pH 8.0, 37°C
10.5
2-oxoisovalerate
pH 8.0, 37°C
0.6 - 25.9
2-oxovalerate
0.2
3-methyl-2-oxobutanoate
pH 8.0, 25°C
0.07 - 23
3-methyl-2-oxopentanoate
12.4
4,4-dimethyl-2-oxopentanoate
pH 8.0, 37°C
0.08
4,4-dimethyl-2-oxovalerate
pH 8.0, 25°C
0.08
4-methyl-2-oxopentanoate
pH 8.0, 25°C
48
L-isoleucine
pH 8.0, 25°C
48
L-leucine
pH 8.0, 25°C
56
pyruvate
pH 8.0, 25°C
0.15
trimethylpyruvate
pH 8.0, 25°C
4.11
2-(3-hydroxy-1-adamantyl)-2-oxoethanoic acid
-
pH 8.0, 37°C
16.84
3-methyl-2-oxobutyric acid
-
pH 8.0, 37°C
13.75
3-methyl-2-oxovaleric acid
-
pH 8.0, 37°C
6.61
4-methyl-2-oxovaleric acid
-
pH 8.0, 37°C
48
L-isoleucine
-
pH 8.0, 25°C
78
L-leucine
-
pH 8.0, 25°C
17
L-methionine
-
pH 8.0, 25°C
2.9
L-phenylalanine
-
pH 8.0, 25°C
3.7
L-tryptophan
-
pH 8.0, 25°C
2.2
L-tyrosine
-
pH 8.0, 25°C
19
L-valine
-
pH 8.0, 25°C
2.2
trimethylpyruvate
-
pH 8.0, 37°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
105
2-Oxohexanoate
pH 8.0, 37°C
309
2-oxoisocaproate
pH 8.0, 37°C
52.5
2-oxoisovalerate
pH 8.0, 37°C
43.2
2-oxovalerate
pH 8.0, 37°C
329
3-methyl-2-oxopentanoate
pH 8.0, 37°C
155
4,4-dimethyl-2-oxopentanoate
pH 8.0, 37°C
0.56
2-(3-hydroxy-1-adamantyl)-2-oxoethanoic acid
-
pH 8.0, 37°C
10.27
3-methyl-2-oxobutyric acid
-
pH 8.0, 37°C
13.89
3-methyl-2-oxovaleric acid
-
pH 8.0, 37°C
15.74
4-methyl-2-oxovaleric acid
-
pH 8.0, 37°C
24.44
trimethylpyruvate
-
pH 8.0, 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
23.9
pH 8.0, 25°C, substrate L-leucine
15.9
-
substrate L-valine + 2-oxoglutarate
27.3
-
substrate L-isoleucine + 2-oxoglutarate
additional information
-
final preparation, specific activity 23.9 U/mg
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.6 - 9
-
-
6 - 9
-
58% activity at pH 6.0, 78% activity at pH 9.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
branched-chain amino acid aminotransferases (BCATs) differ from other (S)-selective transaminases (TAs) in 3D-structure and organization of the PLP-binding domain. Unlike other (S)-selective TAs, BCATs belong to the PLP fold type IV and are characterized by the proton transfer on the re-face of PLP, in contrast to the si-specificity of proton transfer in fold type I (S)-selective TAs. Moreover, BCATs are the only (S)-selective enzymes within fold type IV TAs. Dual substrate recognition in BCATs is implemented via the lock and key mechanism without side-chain rearrangements of the active site residues. Another feature of the active site organization in BCATs is the binding of the substrate alpha-COOH group on the P-side of the active site near the PLP phosphate group. Close localization of two charged groups seems to increase the effectiveness of external aldimine formation in BCAT catalysis
metabolism
BCAT are the key enzymes of BCAA metabolism in all organisms
physiological function
branched-chain amino acid aminotransferases (BCATs) catalyze reversible stereoselective transamination of branched-chain amino acids (BCAAs) L-leucine, L-isoleucine, and L-valine. The catalysis proceeds through the ping-pong mechanism with the assistance of the cofactor pyridoxal 5'-phosphate (PLP)
additional information
structure-function analysis and substrate specificity, comparisons, overview
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
31500
6 * 31500, trimer of dimers
35000
x * 35000, SDS-PAGE
180000
-
gel filtration
182300
-
sedimentation equilibrium centrifugation
185000
-
gel filtration
195000
-
gel filtration combined with angle laser light scattering technique
197000
-
sedimentation equilibrium
31500
-
6 * 31500, SDS-PAGE
33960
-
6 * 33960
34000
-
6 * 34000, SDS-PAGE
36500
-
x * 36500, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 35000, SDS-PAGE
hexamer
6 * 31500, trimer of dimers
homohexamer
6 * 34000, SDS-PAGE
?
-
x * 36500, SDS-PAGE
hexamer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
molecular modelling of substrate binding. The inner side of the active site pocket binds the hydrophobic side chain and the alpha-carboxylate group of the substrates
space group C2
space group C222(1)
crystallized in 2 crystal systems, monoclinic by sitting drop crystallization and tetragonal by hanging drop, monoclinic space group C2, a=93.9, b=143.6, c=143.9 and beta=134.3°, tetragonal space group P422 or P4(1)22 and cell dimensions of a=b=101 A and c=249 A
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
Pichia pastoris strain CBS7435 MutS is used as parent strain for BCAT expressions. The improved BCAT secretion by OCH1 knockout in Pichia pastoris, provides a good system for efficient chiral amine production. Method improvement leads to increase of the extracellular BCAT production, but also to achieve a more homogenous product in terms of glycosylation, identification of a deletion strain that counteracts typical cell clustering in the Pichia pastoris DELTAoch1 strain. The knockout of the locus OCH1, strain FWK3, leads to a more homogenous glycosylation: more Man8 than Man10 N-glycans are added during the mannosylation process, facilitating for example the handling for downstream processes, since hypermannosylation and non homogenous glycosylation can be largely avoided
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.6 - 9
-
almost insensitive to the pH of the medium
640002
5 - 10
-
stable within 10 min
640012
6.5 - 9
-
stable for 24 h at 25°
640012
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
immobilized metal ion affinity chromatography (Ni2+)
-
recombinant enzyme
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene BCAT, recombinant expression in a Pichia pastoris strains (DELTAcwp1, DELTAscw10 resulting in deletio of cell wall proteins) OCH1 knockout strain FWK3, the recombinant Escherichia coli enzyme is secreted. Method development and optimization, detailed overview
cloning of ilv gene, Escherichia coli AB2227 transformed
-
His-tagged protein expressed in Escherichia coli BL21
-
ilvE gene of Escherichia coli is inserted into the region downstream of the tac-promotor, enzyme overproduced by about a 100fold in Escherichia coli W3110
-
K-12 strain carries the ilvE gene both on the host chromosome and on a plasmid
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
development of a coupled assay, employing (R)-hydroxyglutarate dehydrogenase from Acidaminococcus fermentans as an auxiliary enzyme, to provide accurate and reliable kinetic constants
synthesis
enzyme can be used for asymmetric synthesis of a range of non-natural amino acids such as L-norleucine, L-norvaline and L-neopentylglycine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Rudman, D.; Meister, A.
Transamination in Escherichia coli
J. Biol. Chem.
200
591-604
1953
Escherichia coli
Manually annotated by BRENDA team
Monnier, N.; Montmitonnet, A.; Chesne, S.; Pelmont, J.
Transaminase B from Escherichia coli. I.-Purification and first properties
Biochimie
58
663-675
1976
Escherichia coli
Manually annotated by BRENDA team
Lee-Peng, F.C.; Hermodson, M.A.; Kohlhaw, G.B.
Transaminase B from Escherichia coli: quaternary structure, amino-terminal sequence, substrate specificity, and absence of a separate valine-alpha-ketoglutarate activity
J. Bacteriol.
139
339-345
1979
Escherichia coli
Manually annotated by BRENDA team
Inoue, K.; Kuramitsu, S.; Aki, K.; Watanabe, Y.; Takagi, T.; Nishigai, M.; Ikai, A.; Kagamiyama, H.
Branched-chain amino acid aminotransferase of Escherichia coli: overproduction and properties
J. Biochem.
104
777-784
1988
Escherichia coli, Escherichia coli W3110 / ATCC 27325
Manually annotated by BRENDA team
Kamitori, S.; Odagaki, Y.; Inoue, K.; Kuramitsu, S.; Kagamiyama, H.; Matsuura, Y.; Higuchi, T.
Crystallization and preliminary X-ray characterization of branched-chain amino acid aminotransferase from Escherichia coli
J. Biochem.
105
671-672
1989
Escherichia coli
Manually annotated by BRENDA team
Kagamiyama, H.; Hayashi, H.
Branched-chain amino-acid aminotransferase of Escherichia coli
Methods Enzymol.
324
103-113
2000
Escherichia coli, Escherichia coli W3110 / ATCC 27325
Manually annotated by BRENDA team
Okada, K.; Hirotsu, K.; Hayashi, H.; Kagamiyama, H.
Structures of Escherichia coli branched-chain amino acid aminotransferase and its complexes with 4-methylvalerate and 2-methylleucine: Induced fit and substrate recognition of the enzyme
Biochemistry
40
7453-7463
2001
Escherichia coli (P0AB80), Escherichia coli
Manually annotated by BRENDA team
Goto, M.; Miyahara, I.; Hayashi, H.; Kagamiyama, H.; Hirotsu, K.
Crystal structures of branched-chain amino acid aminotransferase complexed with glutamate and glutarate: True reaction intermediate and double substrate recognition of the enzyme
Biochemistry
42
3725-3733
2003
Rattus norvegicus, Escherichia coli (P0AB80), Escherichia coli
Manually annotated by BRENDA team
Seo, Y.; Kim, A.; Bea, H.; Lee, S.; Yun, H.
Asymmetric synthesis of L-6-hydroxynorleucine from 2-keto-6-hydroxyhexanoic acid using a branched-chain aminotransferase
Biocatal. Biotransform.
30
171-176
2012
Escherichia coli
-
Manually annotated by BRENDA team
Seo, Y.M.; Yun, H.
Enzymatic synthesis of L-tert-leucine with branched chain aminotransferase
J. Microbiol. Biotechnol.
21
1049-1052
2011
Escherichia coli
Manually annotated by BRENDA team
Hong, E.; Cha, M.; Yun, H.; Kim, B.
Asymmetric synthesis of L-tert-leucine and L-3-hydroxyadamantylglycine using branched chain aminotransferase
J. Mol. Catal. B
66
228-233
2010
Escherichia coli, Enterobacter sp., Enterobacter sp. TL3
-
Manually annotated by BRENDA team
Yu, X.; Wang, X.; Engel, P.C.
The specificity and kinetic mechanism of branched-chain amino acid aminotransferase from Escherichiacoli studied with a new improved coupled assay procedure and the enzymes potential for biocatalysis
FEBS J.
281
391-400
2014
Escherichia coli (P0AB80), Escherichia coli
Manually annotated by BRENDA team
Bezsudnova, E.Y.; Boyko, K.M.; Popov, V.O.
Properties of bacterial and archaeal branched-chain amino acid aminotransferases
Biochemistry (Moscow)
82
1572-1591
2017
Brevibacillus brevis (A0A2Z4MEX9), Escherichia coli (P0AB80), Gluconobacter oxydans (Q5FTR3), Gluconobacter oxydans 621H (Q5FTR3), Helicobacter pylori (O26004), Helicobacter pylori 26695 (O26004), Helicobacter pylori ATCC 700392 (O26004), Lacticaseibacillus paracasei (A0A5Q8BPF5), Lactococcus lactis, Methanococcus aeolicus (A6UWA0), Methanococcus aeolicus ATCC BAA-1280 (A6UWA0), Methanococcus aeolicus DSM 17508 (A6UWA0), Methanococcus aeolicus Nankai-3 (A6UWA0), Methanococcus aeolicus OCM 812 (A6UWA0), Mycobacterium tuberculosis (P9WQ75), Mycobacterium tuberculosis ATCC 25618 (P9WQ75), Mycobacterium tuberculosis H37Rv (P9WQ75), Pseudomonas aeruginosa (O86428), Pseudomonas aeruginosa 1C (O86428), Pseudomonas aeruginosa ATCC 15692 (O86428), Pseudomonas aeruginosa CIP 104116 (O86428), Pseudomonas aeruginosa DSM 22644 (O86428), Pseudomonas aeruginosa JCM 14847 (O86428), Pseudomonas aeruginosa LMG 12228 (O86428), Pseudomonas aeruginosa PRS 101 (O86428), Pseudomonas sp., Thermococcus sp. CKU-1, Thermoproteus uzoniensis (F2L0W0), Thermoproteus uzoniensis 768-20 (F2L0W0), Vulcanisaeta moutnovskia (F0QW25), Vulcanisaeta moutnovskia 768-28 (F0QW25)
Manually annotated by BRENDA team
Weinhandl, K.; Ballach, M.; Winkler, M.; Ahmad, M.; Glieder, A.; Birner-Gruenberger, R.; Fotheringham, I.; Escalettes, F.; Camattari, A.
Pichia pastoris mutants as host strains for efficient secretion of recombinant branched chain aminotransferase (BCAT)
J. Biotechnol.
235
84-91
2016
Escherichia coli (P0AB80)
Manually annotated by BRENDA team