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Entry
EC 6.3.2.48                 Enzyme                                 

Name
L-arginine-specific L-amino acid ligase;
RizA;
L-amino acid ligase RizA
Class
Ligases;
Forming carbon-nitrogen bonds;
Acid-D-amino-acid ligases (peptide synthases)
BRITE hierarchy
Sysname
L-arginine:L-amino acid ligase (ADP-forming)
Reaction(IUBMB)
ATP + L-arginine + an L-amino acid = ADP + phosphate + an L-arginyl-L-amino acid [RN:R11085]
Reaction(KEGG)
Substrate
ATP [CPD:C00002];
L-arginine [CPD:C00062];
L-amino acid [CPD:C00151]
Product
ADP [CPD:C00008];
phosphate [CPD:C00009];
L-arginyl-L-amino acid [CPD:C21099]
Comment
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.
History
EC 6.3.2.48 created 2015
Orthology
K22115  
L-arginine-specific L-amino acid ligase
Genes
BSS: 
Taxonomy
Reference
1  [PMID:19352016]
  Authors
Kino K, Kotanaka Y, Arai T, Yagasaki M
  Title
A novel L-amino acid ligase from Bacillus subtilis NBRC3134, a microorganism producing peptide-antibiotic rhizocticin.
  Journal
Biosci. Biotechnol. Biochem. 73 (2009) 901-7.
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 

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