L-amino-acid alpha-ligase;
L-amino acid alpha-ligase;
bacilysin synthetase;
YwfE;
L-amino acid ligase

Ligases;
Forming carbon-nitrogen bonds;
Acid-D-amino-acid ligases (peptide synthases)

L-amino acid:L-amino acid ligase (ADP-forming)

ATP + an L-amino acid + an L-amino acid = ADP + phosphate + L-aminoacyl-L-amino acid [RN:R07642]

R07642

ATP [CPD:C00002];
L-amino acid [CPD:C00151]

The enzyme from Bacillus sp. requires Mg2+ or Mn2+ for activity. While the enzyme has extremely broad substrate specificity, it does not accept highly charged amino acids, such as Lys, Arg, Glu and Asp, nor does it react with secondary amines such as Pro. The N-terminal residue of the alpha-dipeptide formed seems to be limited to Ala, Gly, Ser, Thr and Met (with Ala and Ser being the most preferred), whereas the C-terminal residue seems to allow for a wider variety of amino acids (but with a preference for Met and Phe). However, not all combinations or dipeptides are formed. For example, while Ser is acceptable for the N-terminus and Thr for the C-terminus, a Ser-Thr dipeptide is not formed. D-Ala, D-Ser and D-Phe are not substrates. Belongs in the ATP-dependent carboxylate-amine/thiol ligase superfamily.

1  [PMID:16030213]

Tabata K, Ikeda H, Hashimoto S.

ywfE in Bacillus subtilis codes for a novel enzyme, L-amino acid ligase.

J. Bacteriol. 187 (2005) 5195-202.

Bacillus subtilis [GN:bsu]

BSU: BSU37710