| Official Name |
| L-amino-acid alpha-ligase.
|
| Alternative Name(s) |
| Bacilysin synthetase. |
| L-amino acid alpha-ligase. |
| L-amino acid ligase. |
| Reaction catalysed |
| ATP + an L-amino acid + an L-amino acid <=> ADP + phosphate + L-aminoacyl-L-amino acid |
| Cofactor(s) |
| Magnesium or manganese.
|
| Comment(s) |
- 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.
|
| Cross-references |
| BRENDA | 6.3.2.28 |
| PUMA2 | 6.3.2.28 |
| PRIAM enzyme-specific profiles | 6.3.2.28 |
| KEGG Ligand Database for Enzyme Nomenclature | 6.3.2.28 |
| IUBMB Enzyme Nomenclature | 6.3.2.28 |
| IntEnz | 6.3.2.28 |
| MEDLINE | Find literature relating to 6.3.2.28 |
| MetaCyc | 6.3.2.28 |
| UniProtKB/Swiss-Prot |
|