| EC |
6.3.2.48 |
| Accepted name: |
L-arginine-specific L-amino acid ligase |
| Reaction: |
ATP + L-arginine + an L-amino acid = ADP + phosphate + an L-arginyl-L-amino acid
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| Other name(s): |
RizA; L-amino acid ligase RizA |
| Systematic name: |
L-arginine:L-amino acid ligase (ADP-forming) |
| Comments: |
The enzyme, characterized from the bacterium Bacillus subtilis, requires Mn2+ for activity. It shows strict substrate specificity toward L-arginine as the first (N-terminal) amino acid of the product. The second amino acid could be any standard protein-building amino acid except for L-proline. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
| References: |
| 1. |
Kino, K., Kotanaka, Y., Arai, T. and Yagasaki, M. A novel L-amino acid ligase from Bacillus subtilis NBRC3134, a microorganism producing peptide-antibiotic rhizocticin. Biosci. Biotechnol. Biochem. 73 (2009) 901–907. [DOI] [PMID: 19352016] |
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| [EC 6.3.2.48 created 2015] |
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