EC Number   |
Protein Variants |
Reference |
|---|
   3.5.2.6 | C221S |
mutant catalytic activity on the burst phase is similar to that of the wild type BcII |
-, 699013 |
| 3.5.2.6 | C69F |
random mutagenesis |
733117 |
| 3.5.2.6 | C69Y |
random mutagenesis |
733117 |
| 3.5.2.6 | D104A |
km for benzylpenicillin and methicillin increased 2 fold, no change in catalytic activity |
-, 209347 |
| 3.5.2.6 | D104E |
mutation results in a 1000fold enhancement in binding affinity to beta-lactamase inhibitor protein BLIP, as it restores a salt bridge to BLIP. Mutation of a neighboring residue, BLIP E73M, results in salt bridge formation between SHV-1 D104 and BLIP K74 and a 400fold increase in binding affinity. BLIP F142 cooperatively stabilizes both interactions |
721004 |
| 3.5.2.6 | D120A |
kcat/KM is up to 425000fold lower than the wild-type enzyme. Ki-value for phosphate is 450fold lower than wild-type value |
665627 |
| 3.5.2.6 | D120A |
site-directed mutant of CphA, generated and characterized |
696094 |
| 3.5.2.6 | D120C |
site-directed mutagenesis, reduced activity and metal binding compared to the wild-type enzyme |
656274 |
| 3.5.2.6 | D120E |
kcat/KM is up to 136000fold lower than the wild-type enzyme. the Zn-Zn distance is increased by 0.3 A compared with wild-type enzyme |
665627 |
| 3.5.2.6 | D120N |
site-directed mutagenesis, reduced activity and metal binding compared to the wild-type enzyme |
656274 |
