| Type: | Domain | Name: | D-aminopeptidase, domain B/C |
| Description: | Beta-Lactam antibiotics interfere with the biosynthesis of peptidoglycans in the bacterial cell wall by inactivating the penicillin-binding proteins dd-transpeptidases. Bacterial resistance to beta-lactam occurs through the synthesis of beta-lactmases that hydrolyse beta-lactam rings. D-aminopeptidase (DAP) is inhibited by beta-lactam antibiotics, and shares a low sequence identity with class C beta-lactamases and R61 DD-carboxypeptidase. DAP consists of three domains: the N-terminal domain A contains catalytic residues and displays a beta-lactamase-like fold (), domains B (middle) and C (C-terminal) domains are structurally similar, displaying an eight-stranded beta barrel []. Domain C is responsible for substrate and inhibitor specificity. | Short Name: | D_amino_pept_B/C |
