Any feedback?
Literature summary for 2.6.1.17 extracted from
- The redundant aminotransferases in lysine and arginine synthesis and the extent of aminotransferase redundancy in Escherichia coli (2014), Mol. Microbiol., 94, 843-856.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| SDAT-AT | - |
Escherichia coli |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | in Escherichia coli, the major enzymes with N-succinyl-L,L-diaminopimelate aminotransferase (SDAP-AT) activity in lysine synthesis are ArgD, AstC, and SerC. Lysine availability does not regulate synthesis of the major SDAP-ATs. Complementation analysis of mutants lacking aminotransferases shows that the SDAP-ATs and alanine aminotransferases are exceptionally redundant, and this redundancy may ensure peptidoglycan synthesis | Escherichia coli |
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
