EC Number |
Protein Variants |
Reference |
---|
3.6.4.B10 | C450Y |
naturally occuring mutation in subunit CCT4 |
-, 749858 |
3.6.4.B10 | D386A |
site-directed mutagenesis, introduction of D386A into Mm-cpn significantly reduces its ability to complement for loss of GroES and GroEL, loss of ATPase activity severely affects the complementing ability of the wild-type and mutant Mm-cpn proteins |
757098 |
3.6.4.B10 | D545G |
site-directed mutagenesis, the mutant shows a stabilities similar to the wild-type CpkA |
734095 |
3.6.4.B10 | D545M |
site-directed mutagenesis, the mutant shows slightly higher stabilities than that of wild-type CpkA |
734095 |
3.6.4.B10 | D64A/D393A |
site-directed mutagenesis, an ATPase-deficient mutant, the mutant also does not exhibit ATPase-dependent conformational change |
-, 734484 |
3.6.4.B10 | D64A/D393A/K485W |
site-directed mutagenesis, an ATPase-deficient mutant, the mutant also does not exhibit ATPase-dependent conformational change, the mutant lacks ATP-dependent refolding activity, nucleotide binding and ATP-dependent conformational change kinetics, overview |
-, 734484 |
3.6.4.B10 | E530G |
site-directed mutagenesis, the mutant strain DA4 shows increased ATPase activity. The CpkA-E530G mutation prevents cold denaturation of proteins under cold-stress conditions, thereby enabling cells to grow in cooler environments |
734095 |
3.6.4.B10 | E530M |
site-directed mutagenesis, the mutant shows a stabilities similar to the wild-type CpkA |
734095 |
3.6.4.B10 | G160S |
the TRiC-like mutant G160S of MmCpn has a drastically slower rate of ATP hydrolysis, roughly equivalent to the steady-state hydrolysis of eukaryotic TRiC |
734489 |
3.6.4.B10 | G345D |
site-directed mutagenesis in subunit CCT4 decreases cooperativity in ATP binding compared to wild-type |
-, 751330 |