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LD-carboxypeptidase C-terminal domain
Muramoyl-tetrapeptide carboxypeptidase hydrolyses a peptide bond between a di-basic amino acid and the C-terminal D-alanine in the tetrapeptide moiety in peptidoglycan. This cleaves the bond between an L- and a D-amino acid. The function of this activity is in murein recycling. This family also includes the microcin c7 self-immunity protein Swiss:Q47511. This family corresponds to Merops family S66. [1]. 8522520. Structure and organization of plasmid genes required to produce the translation inhibitor microcin C7. Gonzalez-Pastor JE, San Millan JL, Castilla MA, Moreno F;. J Bacteriol 1995;177:7131-7140. [2]. 7559516. Chemical structure and translation inhibition studies of the antibiotic microcin C7. Guijarro JI, Gonzalez-Pastor JE, Baleux F, San Millan JL, Castilla MA, Rico M, Moreno F, Delepierre M;. J Biol Chem 1995;270:23520-23532. [3]. 10428950. A defect in cell wall recycling triggers autolysis during the stationary growth phase of Escherichia coli. Templin MF, Ursinus A, Holtje JV;. EMBO J 1999;18:4108-4117. [4]. 16162494. P. aeruginosa LD-carboxypeptidase: A serine peptidase with a Ser-His-Glu triad and a nucleophilic elbow. Korza HJ, Bochtler M;. J Biol Chem 2005; [Epub ahead of print] (from Pfam)
LD-carboxypeptidase
LD-carboxypeptidase, a S66 family peptidase, cleaves amide bonds between L- and D-amino acids, which occur in bacterial peptidoglycan
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