AmpH, a Bifunctional dd -Endopeptidase and dd -Carboxypeptidase of Escherichia coli

AmpH, a bifunctional DD-endopeptidase and DD-carboxypeptidase of Escherichia coli.

In Escherichia coli, low-molecular-mass penicillin-binding proteins (LMM PBPs) are important for correct cell morphogenesis. These enzymes display DD-carboxypeptidase and/or dd-endopeptidase activities associated with maturation and remodeling of peptidoglycan (PG). AmpH has been classified as an AmpH-type class C LMM PBP, a group closely related to AmpC β-lactamases. AmpH has been associated w...

DD-carboxypeptidase and peptidoglycan transpeptidase from Pseudomonas aeruginosa.

Peptidoglycan transpeptidase and dd-carboxypeptidase have been detected in isolated membranes of Pseudomonas aeruginosa. Cephalosporins and penicillins fail to inhibit the transpeptidase at concentrations as high as 100 mug/ml. dd-Carboxypeptidase, on the other hand, is sensitive to inhibition by beta-lactam antibiotics. The presence of dimethyl sulfoxide in the reaction mixture results in a tw...

Molecular cloning, sequence analysis, and characterization of a penicillin-resistant DD-carboxypeptidase of Myxococcus xanthus.

We have cloned a gene, pdcA, from the genomic library of Myxococcus xanthus with an oligonucleotide probe representing conserved regions of penicillin-resistant DD-carboxypeptidases. The amino- and carboxy-terminal halves of the predicted pdcA gene product showed significant sequence similarity to N-acetylmuramoyl-L-alanine amidase and penicillin-resistant DD-carboxypeptidase, respectively. The...

The exocellular DD-carboxypeptidase of Streptomyces albus G: a metallo (Zn2+) enzyme.

A Nonoverlapping Characteristic Dd Method