EC Number   |
Protein Variants |
Reference |
|---|
   5.6.1.7 | A109C |
the mutant is defective in ring separation and exchange |
750256 |
| 5.6.1.7 | A109S |
the mutant shows mixed-ring formation like the wild type enzyme |
750256 |
| 5.6.1.7 | A399T |
site-diretected mutagenesis, the mutation weakens the affinity for GroES by about 90fold |
733278 |
| 5.6.1.7 | A92T |
site-diretected mutagenesis, the mutation weakens the affinity for GroES by about 1600fold |
733278 |
| 5.6.1.7 | C138S/C458S/C519S/D83C/K327C |
conformational change, in reduced state similar ATP hydrolysis and ATP binding to wild-type GroEL |
701081 |
| 5.6.1.7 | C138W |
at 37°C, the mutant enzyme is indistinguishable in all aspects from the wild type, however, at 25°C, steric hindrances cause the chaperonin to be arrested in a ternary complex form, with both unfolded protein and GroES bound to the same ring of the enzyme. An increase in temperature to more than 30°C is sufficient to restart both target protein refolding and ATPase activity in the mutant enzyme |
750069 |
| 5.6.1.7 | C51A |
wild-type HpGroES binds two Zn2+ per monomer. H45A, C51A, and C53A decrease to 0.3-0.5 Zn2+ per monomer |
713424 |
| 5.6.1.7 | C51A/C53A |
the double-cysteine mutant gives only 0.12 Zn2+ per monomer |
713424 |
| 5.6.1.7 | C53A |
wild-type HpGroES binds two Zn2+ per monomer. H45A, C51A, and C53A decrease to 0.3-0.5 Zn2+ per monomer |
713424 |
| 5.6.1.7 | D115N |
site-diretected mutagenesis, the mutation weakens the affinity for GroES by about 50fold |
733278 |
