EC Number   |
Reaction |
Reference |
|---|
   3.5.2.6 | a beta-lactam + H2O = a substituted beta-amino acid |
- |
- |
| 3.5.2.6 | a beta-lactam + H2O = a substituted beta-amino acid |
2-step mechanism: in the first step, the catalytic Ser64 attacks the carbonyl carbon of the beta-lactam ring, forming an acyl intermediate, in the second step, a deacylating water hydrolyzes the ester bond to regenerate the enzyme and the reaction product, hydrolyzed antibiotic |
-, 654608 |
| 3.5.2.6 | a beta-lactam + H2O = a substituted beta-amino acid |
active site, Asp120 is important for catalysis, as well as substrate and Zn2+ binding |
656274 |
| 3.5.2.6 | a beta-lactam + H2O = a substituted beta-amino acid |
Arg234 is involved in catalysis |
654597 |
| 3.5.2.6 | a beta-lactam + H2O = a substituted beta-amino acid |
catalytic mechanism of enzyme class D, unique in comparison with classes A and C, active site structure with elements S-X-X-K, S-X-N, and K-T/S-G |
656855 |
| 3.5.2.6 | a beta-lactam + H2O = a substituted beta-amino acid |
enzyme-ligand interaction-structure, computational analysis, residues K67, N152, Y150, and K315 are involved in substrate binding, tetrahedral intermediate |
-, 654948 |
| 3.5.2.6 | a beta-lactam + H2O = a substituted beta-amino acid |
Glu166 is important for catalysis, mechanism |
654635 |
| 3.5.2.6 | a beta-lactam + H2O = a substituted beta-amino acid |
overall mechanism for beta-lactamase-inhibitor reaction, Quantum mechanical/molecular mechanical calculations and Raman spectral analysis, overview |
734294 |
| 3.5.2.6 | a beta-lactam + H2O = a substituted beta-amino acid |
overall mechanism for beta-lactamase-inhibitor reaction, Quantum mechanical/molecular mechanical calculations and Raman spectral analysis, overview. The protonation of the zeta-nitrogen leads to a barrierless decarboxylation of the lysine carbamate |
734294 |
| 3.5.2.6 | a beta-lactam + H2O = a substituted beta-amino acid |
reaction and kinetic mechanism |
-, 654742 |
