PMID:8112463
| Citation |
Leguina, JI, Quintela, JC and de Pedro, MA (1994) Substrate specificity of Escherichia coli LD-carboxypeptidase on biosynthetically modified muropeptides. FEBS Lett. 339:249-52 |
|---|---|
| Abstract |
Escherichia coli murein can be biosynthetically modified. Amino acids at positions 3 and 4 (m-diaminopimelic acid and D-alanine, respectively) on the peptide moieties can be changed under appropriate growth conditions. The activity of E. coli LD-carboxypeptidase on biosynthetically modified substrates has been studied in vitro. The enzyme hydrolysed all tested disaccharide-tetrapeptide monomeric muropeptides modified at position 4. Monomers with m-lanthionine, but not with L-ornithine, instead of m-diaminopimelic acid at position 3 were accepted. However, neither cross-linked muropeptides nor macromolecular murein were substrates for the reaction. Our observations argue against a direct effect of LD-carboxypeptidase on macromolecular murein metabolism. |
| Links | |
| Keywords |
Alanine; Amino Acid Sequence; Carboxypeptidases/metabolism; Diaminopimelic Acid; Escherichia coli/enzymology; Molecular Sequence Data; Peptides/chemistry; Peptides/metabolism; Peptidoglycan/chemistry; Peptidoglycan/metabolism; Structure-Activity Relationship; Substrate Specificity |
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