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Literature summary for 2.6.1.19 extracted from

  • Shi, F.; Si, H.; Ni, Y.; Zhang, L.; Li, Y.
    Transaminase encoded by NCgl2515 gene of Corynebacterium glutamicum ATCC13032 is involved in gamma-aminobutyric acid decomposition (2017), Process Biochem., 55, 55-60 .
No PubMed abstract available

Cloned(Commentary)

Cloned (Comment) Organism
gene gabT, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3) Corynebacterium glutamicum
gene NCgl2515, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3) Corynebacterium glutamicum

Protein Variants

Protein Variants Comment Organism
additional information construction of the gabT NCgl2515-deleted GAD strain SYN203, deletion of the gabT gene encoding GABA-T, and deletion of the additional transaminase gene, NCgl2515, in a gabT-deleted GAD strain Corynebacterium glutamicum
additional information construction of the gabT-deleted GAD strain SYN201, deletion of the gabT gene encoding GABA-T, and deletion of the additional transaminase gene, NCgl2515, in a gabT-deleted GAD strain Corynebacterium glutamicum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
9.21
-
2-oxoglutarate recombinant enzyme GabT, pH 7.8, 30°C Corynebacterium glutamicum
10.63
-
4-aminobutanoate recombinant enzyme GabT, pH 7.8, 30°C Corynebacterium glutamicum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4-aminobutanoate + 2-oxoglutarate Corynebacterium glutamicum
-
succinate semialdehyde + L-glutamate
-
r
4-aminobutanoate + 2-oxoglutarate Corynebacterium glutamicum LMG 3730
-
succinate semialdehyde + L-glutamate
-
r
4-aminobutanoate + 2-oxoglutarate Corynebacterium glutamicum BCRC 11384
-
succinate semialdehyde + L-glutamate
-
r
4-aminobutanoate + 2-oxoglutarate Corynebacterium glutamicum ATCC 13032
-
succinate semialdehyde + L-glutamate
-
r
4-aminobutanoate + 2-oxoglutarate Corynebacterium glutamicum JCM 1318
-
succinate semialdehyde + L-glutamate
-
r
4-aminobutanoate + 2-oxoglutarate Corynebacterium glutamicum NCIMB 10025
-
succinate semialdehyde + L-glutamate
-
r
4-aminobutanoate + 2-oxoglutarate Corynebacterium glutamicum DSM 20300
-
succinate semialdehyde + L-glutamate
-
r
4-aminobutanoate + pyruvate Corynebacterium glutamicum
-
succinate semialdehyde + L-alanine
-
r
4-aminobutanoate + pyruvate Corynebacterium glutamicum LMG 3730
-
succinate semialdehyde + L-alanine
-
r
4-aminobutanoate + pyruvate Corynebacterium glutamicum BCRC 11384
-
succinate semialdehyde + L-alanine
-
r
4-aminobutanoate + pyruvate Corynebacterium glutamicum ATCC 13032
-
succinate semialdehyde + L-alanine
-
r
4-aminobutanoate + pyruvate Corynebacterium glutamicum JCM 1318
-
succinate semialdehyde + L-alanine
-
r
4-aminobutanoate + pyruvate Corynebacterium glutamicum NCIMB 10025
-
succinate semialdehyde + L-alanine
-
r
4-aminobutanoate + pyruvate Corynebacterium glutamicum DSM 20300
-
succinate semialdehyde + L-alanine
-
r

Organism

Organism UniProt Comment Textmining
Corynebacterium glutamicum P46395
-
-
Corynebacterium glutamicum Q8NT48
-
-
Corynebacterium glutamicum ATCC 13032 P46395
-
-
Corynebacterium glutamicum ATCC 13032 Q8NT48
-
-
Corynebacterium glutamicum BCRC 11384 P46395
-
-
Corynebacterium glutamicum BCRC 11384 Q8NT48
-
-
Corynebacterium glutamicum DSM 20300 P46395
-
-
Corynebacterium glutamicum DSM 20300 Q8NT48
-
-
Corynebacterium glutamicum JCM 1318 P46395
-
-
Corynebacterium glutamicum JCM 1318 Q8NT48
-
-
Corynebacterium glutamicum LMG 3730 P46395
-
-
Corynebacterium glutamicum LMG 3730 Q8NT48
-
-
Corynebacterium glutamicum NCIMB 10025 P46395
-
-
Corynebacterium glutamicum NCIMB 10025 Q8NT48
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography Corynebacterium glutamicum

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.03
-
NCgl2515 activity, with substrate 4-aminobutanoate, pH 8.0, 30°C Corynebacterium glutamicum
1.34
-
GABA-T activity, with substrate 4-aminobutanoate, pH 7.8, 30°C Corynebacterium glutamicum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-aminobutanoate + 2-oxoglutarate
-
Corynebacterium glutamicum succinate semialdehyde + L-glutamate
-
r
4-aminobutanoate + 2-oxoglutarate
-
Corynebacterium glutamicum LMG 3730 succinate semialdehyde + L-glutamate
-
r
4-aminobutanoate + 2-oxoglutarate
-
Corynebacterium glutamicum BCRC 11384 succinate semialdehyde + L-glutamate
-
r
4-aminobutanoate + 2-oxoglutarate
-
Corynebacterium glutamicum ATCC 13032 succinate semialdehyde + L-glutamate
-
r
4-aminobutanoate + 2-oxoglutarate
-
Corynebacterium glutamicum JCM 1318 succinate semialdehyde + L-glutamate
-
r
4-aminobutanoate + 2-oxoglutarate
-
Corynebacterium glutamicum NCIMB 10025 succinate semialdehyde + L-glutamate
-
r
4-aminobutanoate + 2-oxoglutarate
-
Corynebacterium glutamicum DSM 20300 succinate semialdehyde + L-glutamate
-
r
4-aminobutanoate + pyruvate
-
Corynebacterium glutamicum succinate semialdehyde + L-alanine
-
r
4-aminobutanoate + pyruvate
-
Corynebacterium glutamicum LMG 3730 succinate semialdehyde + L-alanine
-
r
4-aminobutanoate + pyruvate
-
Corynebacterium glutamicum BCRC 11384 succinate semialdehyde + L-alanine
-
r
4-aminobutanoate + pyruvate
-
Corynebacterium glutamicum ATCC 13032 succinate semialdehyde + L-alanine
-
r
4-aminobutanoate + pyruvate
-
Corynebacterium glutamicum JCM 1318 succinate semialdehyde + L-alanine
-
r
4-aminobutanoate + pyruvate
-
Corynebacterium glutamicum NCIMB 10025 succinate semialdehyde + L-alanine
-
r
4-aminobutanoate + pyruvate
-
Corynebacterium glutamicum DSM 20300 succinate semialdehyde + L-alanine
-
r
additional information substrate specificity analysis. GABA-T-SSADH coupling activity of GabT-GabD proteins is analyzed and compared with that of NCgl2515-GabD proteins. The GabT-GabD exhibits much higher levels of 2-oxo-dependent GABA-T-SSADH activity (1.25 U/mg) than NCgl2515-GabD, no pyruvate-dependent GABA-T-SSADH activity is detected Corynebacterium glutamicum ?
-
-
additional information substrate specificity analysis. GABA-T-SSADH coupling activity of GabT-GabD proteins is analyzed and compared with that of NCgl2515-GabD proteins. The GabT-GabD exhibits much higher levels of 2-oxo-dependent GABA-T-SSADH activity (1.25 U/mg) than NCgl2515-GabD, no pyruvate-dependent GABA-T-SSADH activity is detected Corynebacterium glutamicum LMG 3730 ?
-
-
additional information substrate specificity analysis. GABA-T-SSADH coupling activity of GabT-GabD proteins is analyzed and compared with that of NCgl2515-GabD proteins. The GabT-GabD exhibits much higher levels of 2-oxo-dependent GABA-T-SSADH activity (1.25 U/mg) than NCgl2515-GabD, no pyruvate-dependent GABA-T-SSADH activity is detected Corynebacterium glutamicum BCRC 11384 ?
-
-
additional information substrate specificity analysis. GABA-T-SSADH coupling activity of GabT-GabD proteins is analyzed and compared with that of NCgl2515-GabD proteins. The GabT-GabD exhibits much higher levels of 2-oxo-dependent GABA-T-SSADH activity (1.25 U/mg) than NCgl2515-GabD, no pyruvate-dependent GABA-T-SSADH activity is detected Corynebacterium glutamicum ATCC 13032 ?
-
-
additional information substrate specificity analysis. GABA-T-SSADH coupling activity of GabT-GabD proteins is analyzed and compared with that of NCgl2515-GabD proteins. The GabT-GabD exhibits much higher levels of 2-oxo-dependent GABA-T-SSADH activity (1.25 U/mg) than NCgl2515-GabD, no pyruvate-dependent GABA-T-SSADH activity is detected Corynebacterium glutamicum JCM 1318 ?
-
-
additional information substrate specificity analysis. GABA-T-SSADH coupling activity of GabT-GabD proteins is analyzed and compared with that of NCgl2515-GabD proteins. The GabT-GabD exhibits much higher levels of 2-oxo-dependent GABA-T-SSADH activity (1.25 U/mg) than NCgl2515-GabD, no pyruvate-dependent GABA-T-SSADH activity is detected Corynebacterium glutamicum NCIMB 10025 ?
-
-
additional information substrate specificity analysis. GABA-T-SSADH coupling activity of GabT-GabD proteins is analyzed and compared with that of NCgl2515-GabD proteins. The GabT-GabD exhibits much higher levels of 2-oxo-dependent GABA-T-SSADH activity (1.25 U/mg) than NCgl2515-GabD, no pyruvate-dependent GABA-T-SSADH activity is detected Corynebacterium glutamicum DSM 20300 ?
-
-

Synonyms

Synonyms Comment Organism
bioA
-
Corynebacterium glutamicum
GABA transaminase
-
Corynebacterium glutamicum
GABA-T
-
Corynebacterium glutamicum
GabT
-
Corynebacterium glutamicum
More cf. EC 2.6.1.62, adenosylmethionine-8-amino-7-oxononanoate aminotransferase Corynebacterium glutamicum
NCgl0462
-
Corynebacterium glutamicum
NCgl2515
-
Corynebacterium glutamicum

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
assay at Corynebacterium glutamicum

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.34
-
2-oxoglutarate recombinant enzyme GabT, pH 7.8, 30°C Corynebacterium glutamicum
3.77
-
4-aminobutanoate recombinant enzyme GabT, pH 7.8, 30°C Corynebacterium glutamicum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.8
-
recombinant GabT Corynebacterium glutamicum
8
-
assay at Corynebacterium glutamicum

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate PLP Corynebacterium glutamicum

General Information

General Information Comment Organism
malfunction deletion of the gabT gene encoding GABA-T cannot prevent GABA from decomposing at neutral pH. An additional transaminase gene, NCgl2515, is deleted in a gabT-deleted GAD strain, but the GABA concentration in this gabT NCgl2515-deleted GAD strain remains unaltered when pH is maintained at pH 7.5-7.8, demonstrating that GABA decomposition is reduced Corynebacterium glutamicum
malfunction deletion of the gabT gene encoding GABA-T cannot prevent GABA from decomposing at neutral pH. An additional transaminase gene, NCgl2515, is deleted in a gabT-deleted GAD strain, but the GABA concentration in this gabT-deleted GAD strain NCgl2515 remains unaltered when pH is maintained at pH 7.5-8.0, demonstrating that GABA decomposition is reduced Corynebacterium glutamicum
metabolism unlike GabT, which exhibits high GABA-T activity and utilizes only 2-oxoglutarate as amino acceptor, the purified NCgl2515 protein exhibits very low GABA-T activity only when coupled with succinate-semialdehyde dehydrogenase (SSADH) GabD, but can utilize both 2-oxoglutarate and pyruvate as amino acceptor Corynebacterium glutamicum
metabolism unlike GabT, which exhibits high GABA-T activity and utilizes only 2-oxoglutarate as amino acceptor, the purified NCgl2515 protein exhibits very low GABA-T activity only when coupled with succinate-semialdehyde dehydrogenase (SSADH), GabD, but can utilize both 2-oxoglutarate and pyruvate as amino acceptor Corynebacterium glutamicum

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.037
-
2-oxoglutarate recombinant enzyme GabT, pH 7.8, 30°C Corynebacterium glutamicum
0.36
-
4-aminobutanoate recombinant enzyme GabT, pH 7.8, 30°C Corynebacterium glutamicum