L-amino-acid alpha-ligase
| L-amino-acid alpha-ligase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 6.3.2.28 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
In enzymology, an L-amino-acid alpha-ligase (EC 6.3.2.28) is an enzyme that catalyzes the chemical reaction
- ATP + an L-amino acid + an L-amino acid ADP + phosphate + L-aminoacyl-L-amino acid
Thus, the two substrates of this enzyme are ATP and L-amino acid, whereas its 3 products are ADP, phosphate, and L-aminoacyl-L-amino acid.
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-amino-acid ligases (peptide synthases). The systematic name of this enzyme class is L-amino acid:L-amino acid ligase (ADP-forming). Other names in common use include L-amino acid alpha-ligase, bacilysin synthetase, YwfE, and L-amino acid ligase.
References
- Tabata K, Ikeda H, Hashimoto S (2005). "ywfE in Bacillus subtilis codes for a novel enzyme, L-amino acid ligase". J. Bacteriol. 187 (15): 5195–202. doi:10.1128/JB.187.15.5195-5202.2005. PMC 1196041
. PMID 16030213.
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