EC Number |
Substrates |
Organism |
Products |
Reversibility |
---|
2.6.1.19 | more |
(Pl)EctB also preferably catalyzes a EctB-type reaction, EC 2.6.1.76 |
Paenibacillus lautus |
? |
- |
- |
2.6.1.19 | more |
N-acetylornithine aminotransferase is a bifunctional enzyme that has both N-acetylornithine aminotransferase (EC 2.6.1.11) and GABA aminotransferase activities |
Synechococcus sp. PCC 7002 |
? |
- |
- |
2.6.1.19 | more |
N-acetylornithine aminotransferase is a bifunctional enzyme that has both N-acetylornithine aminotransferase (EC 2.6.1.11) and GABA aminotransferase activities |
Synechococcus sp. PCC 6803 |
? |
- |
- |
2.6.1.19 | more |
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 |
? |
- |
- |
2.6.1.19 | more |
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 |
? |
- |
- |
2.6.1.19 | more |
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 |
? |
- |
- |
2.6.1.19 | more |
(Pl)EctB also preferably catalyzes a EctB-type reaction, EC 2.6.1.76 |
Paenibacillus lautus Y412MC10 |
? |
- |
- |
2.6.1.19 | more |
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 |
? |
- |
- |
2.6.1.19 | more |
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 |
? |
- |
- |
2.6.1.19 | more |
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 |
? |
- |
- |