Any feedback?
Literature summary for 2.6.1.62 extracted from
- 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 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 |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Corynebacterium glutamicum | P46395 | - |
- |
| Corynebacterium glutamicum ATCC 13032 | P46395 | - |
- |
| Corynebacterium glutamicum BCRC 11384 | P46395 | - |
- |
| Corynebacterium glutamicum DSM 20300 | P46395 | - |
- |
| Corynebacterium glutamicum JCM 1318 | P46395 | - |
- |
| Corynebacterium glutamicum LMG 3730 | P46395 | - |
- |
| Corynebacterium glutamicum NCIMB 10025 | P46395 | - |
- |
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 |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | the enzyme also catalzes the reaction of EC 2.6.1.19, the 4-aminobutanoate transaminase reaction, but with much less activity compared to the adenosylmethionine-8-amino-7-oxononanoate aminotransferase activity. Substrate specificity analysis | Corynebacterium glutamicum | ? | - |
- |
 |
| additional information | the enzyme also catalzes the reaction of EC 2.6.1.19, the 4-aminobutanoate transaminase reaction, but with much less activity compared to the adenosylmethionine-8-amino-7-oxononanoate aminotransferase activity. Substrate specificity analysis | Corynebacterium glutamicum LMG 3730 | ? | - |
- |
|
| additional information | the enzyme also catalzes the reaction of EC 2.6.1.19, the 4-aminobutanoate transaminase reaction, but with much less activity compared to the adenosylmethionine-8-amino-7-oxononanoate aminotransferase activity. Substrate specificity analysis | Corynebacterium glutamicum BCRC 11384 | ? | - |
- |
|
| additional information | the enzyme also catalzes the reaction of EC 2.6.1.19, the 4-aminobutanoate transaminase reaction, but with much less activity compared to the adenosylmethionine-8-amino-7-oxononanoate aminotransferase activity. Substrate specificity analysis | Corynebacterium glutamicum ATCC 13032 | ? | - |
- |
|
| additional information | the enzyme also catalzes the reaction of EC 2.6.1.19, the 4-aminobutanoate transaminase reaction, but with much less activity compared to the adenosylmethionine-8-amino-7-oxononanoate aminotransferase activity. Substrate specificity analysis | Corynebacterium glutamicum JCM 1318 | ? | - |
- |
|
| additional information | the enzyme also catalzes the reaction of EC 2.6.1.19, the 4-aminobutanoate transaminase reaction, but with much less activity compared to the adenosylmethionine-8-amino-7-oxononanoate aminotransferase activity. Substrate specificity analysis | Corynebacterium glutamicum NCIMB 10025 | ? | - |
- |
|
| additional information | the enzyme also catalzes the reaction of EC 2.6.1.19, the 4-aminobutanoate transaminase reaction, but with much less activity compared to the adenosylmethionine-8-amino-7-oxononanoate aminotransferase activity. Substrate specificity analysis | Corynebacterium glutamicum DSM 20300 | ? | - |
- |
|
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| bioA | - |
Corynebacterium glutamicum |
| More | cf. EC 2.6.1.19, 4-aminobutyrate aminotransferase | Corynebacterium glutamicum |
| NCgl2515 | - |
Corynebacterium glutamicum |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | - |
assay at | Corynebacterium glutamicum |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 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-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 (EC 2.6.1.19), 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 |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
