EC Number   |
Protein Variants |
Reference |
|---|
    3.4.16.4 | C98A |
half-life at 72°C increases to 13 min, compared to 10 min for the wild-type enzyme. Half-life at 60°C increases to 220 min compared to 170 min for the wild-type enzyme. The value of the second-order acylation rate constant is not very different from those of the wild-type enzyme with the exception of the cephalotin, oxacillin and piperacillin values which are increased 5-10fold |
650206 |
| 3.4.16.4 | C98N |
half-life at 72°C decreases to 6 min, compared to 10 min for the wild-type enzyme. Half-life at 60°C decreases to 30 min compared to 170 min for the wild-type enzyme. The acylation rate constants by most of the beta-lactams are increased 10-70fold compared to the wild-type enzyme. The deacylation rate constant values als increases |
650206 |
| 3.4.16.4 | D155A |
mutant, constructed for the demonstration of the relative importance of residue Asp155 |
696317 |
| 3.4.16.4 | DELTA74-90 |
deletion of the 74-90 loop markedly diminishes the deacylation rate of penicillin G with a minimal impact on acylation, and abolishes D-alanine carboxypeptidase activity |
652495 |
| 3.4.16.4 | F160A |
mutant, constructed for the demonstration of the relative importance of residue Phe160 |
696317 |
| 3.4.16.4 | G105D |
mutation markedly impairs deacylation with only minor effects on acylation, and abolishes D-alanine carboxypeptidase activity |
652495 |
| 3.4.16.4 | G105D |
mutation markedly impairs the beta-lactamase activity, with only minor effects on acylation, and promotes accumulation of a covalent complex with peptide substrates |
652213 |
| 3.4.16.4 | K38H |
half-life at 72°C decreases to 3.5 min, compared to 10 min for the wild-type enzyme. The mutant enzyme fails to bind beta-lactams |
650206 |
| 3.4.16.4 | L684P |
about 50% of wild-type activity |
-, 755422 |
| 3.4.16.4 | more |
PBP3 mutant, rings of high-molecular-weight PBPs and that of FtsZ are no longer co-localized, the co-ordination is necessary for membrane invagination |
670303 |
