EC Number |
Protein Variants |
Reference |
---|
3.5.2.6 | E104K/G238S |
- |
-, 209359 |
3.5.2.6 | more |
a VIM-2 enzyme inserted in integron In58, in an isolate from a female cystic fibrosis patient, is resistant to all antimicrobial agents tested except colistin, this isolate presented a unique random amplified polymorphic DNA, RAPD, type, overview |
692627 |
3.5.2.6 | W290F |
activity and spectroscopic properties of the mutant enzyme does not differ significantly from those of the wild type, indicating that the mutation has only a very limited effect on the structure of the protein. The stability of the folded protein is reduced, however, by 5-10 kJ mol-1 relative to that of the molten globule intermediate (H), but the values of the folding rate constants are unchanged, suggesting that Trp290 becomes organized in its native like environment only after the rate-limiting step, i.e., the C-terminal region of the enzyme folds very late |
-, 696228 |
3.5.2.6 | D179G |
activity unchanged or enhanced |
-, 209346 |
3.5.2.6 | D179N |
activity unchanged or enhanced |
-, 209346 |
3.5.2.6 | R164N |
activity unchanged or enhanced |
-, 209346 |
3.5.2.6 | R164S |
activity unchanged or enhanced |
-, 209346 |
3.5.2.6 | more |
analysis of 516 mutated enzymes that acquired the ceftazidime-hydrolyzing activity, and identification of twelve positions with single amino acid substitutions, co-localized at the active-site pocket area. single amino acid substitutions are found at positions C89, N136, L162, R164, E166, L169, N170, T171, A172, P174, D176, D179. All substitutions cause a congruent effect, expanding the space in a conserved structure called the omega loop, which in turn increased flexibility at the active site |
720866 |
3.5.2.6 | R61H/E64H/43H |
circularly permuted enzyme, created by rational design. Mutant shows little regulation upon metal ion binding except for a weak activation with Zn2+ |
720961 |
3.5.2.6 | more |
construction of diverse mutant of the beta-lactamase inhibitor protein BLIP by alanine scanning mutation |
656249 |