EC Number   |
|---|
    3.4.16.4 | - |
| 3.4.16.4 | 1.2 A resolution X-ray structure of cephalosporin bound to the active site of the bifunctional serine type D-alanyl-D-alanine carboxypeptidase/transpeptidase |
| 3.4.16.4 | by hanging drop vapor diffusion, at 1.8 A and 2.4 A resolution, R39 structure is composed of one penicillin binding domain and two unknown domains, the R39 active site does not undergo a great structural deformation upon beta-lactam binding |
| 3.4.16.4 | by hanging drop vapor diffusion, to 1.1 A resolution |
| 3.4.16.4 | by hanging drop vapor diffusion, to 2.8 A resolution, PBP3 folds into an NH2-terminal,D,D-carboxypeptidase-like domain and a COOH-terminal, elongated beta-rich region |
| 3.4.16.4 | by hanging-drop, vapor-diffusion method, to 1.5 A resolution, X-ray structure of non-covalent and covalent complexes of beta-lactams with DD-peptidase |
| 3.4.16.4 | characterization of the noncovalent interactions based on cocrystallized structures of benzylpenicillin and perfect penicillin covalently bound to DD-peptidase by computational methods. Benzylpenicillins phenyl group forms an extended pi?pi network with Phe120 and Trp233 that contributes significantly to its efficacy in DD-peptidase. This aromatic stabilization is conserved in beta-lactamases. Interactions between the protein and the peptidomimetic tail region, particularly carboxylate 2 and the terminal N4H3+ unit, form unique hydrogen bonding and strong electrostatic interactions. Between Asp217 and the N4H3+ there is a water mediated salt bridge |
| 3.4.16.4 | crystal structure at 1.6 A resolution of PBP5 in complex with a substrate-like peptide boronic acid, suggesting a hydrogen-bonding network, involving Lys-213, Ser-110, and a bridging water molecule, to polarize the hydrolytic water molecule |
| 3.4.16.4 | crystal structures of VanXY mutant D59S and VanXY wild-type in apo and transition state analog-bound forms and of the mutant in complex with the D-Ala-D-Ala substrate and D-Ala product. Structural and biochemical analysis identifies the molecular determinants of VanXY dual specificity acting on dipeptide D-Ala-D-Ala or pentapeptide UDP-MurNac-L-Ala-D-Glu-L-Lys-D-Ala-D-Ala, respectively. VanXY residues 110-115 form a mobile cap over the catalytic site, whose flexibility is involved in the switch between di- and pentapeptide hydrolysis. VanY pentapeptidases lack this element, which promotes binding of the penta- rather than that of the dipeptide |
| 3.4.16.4 | hanging drop vapor diffusion method. Mutant enzymes S96A, K38H, C98A and C98N are produced in culture medium of Streptomyces lividans |
