Crystallization (Comment) | Organism |
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crystals of the mutant G268N are successfully raised to study the fine structural change around the active site. Results show that one residue mutation in can cause the mutant G268N to exhibit cold-adapted enzyme properties comparable to those of Cyprinus carpio M1-creatine kinase | Oryctolagus cuniculus |
Protein Variants | Comment | Organism |
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A267H | at pH 7.1 mutant shows 30% higher specific activity than the wild-type at 35°C, in contrast to mutant G268N this mutant shows no cold-adapted characteristics | Oryctolagus cuniculus |
G286N | Km values of the rabbit creatine kinase G268N mutant are similar to those of the wild-type rabbit enzyme, circular dichroism spectra show that the overall secondary structures of the mutant enzyme, at pH 8.0 and 5 °C, are almost identical to the carp M1-creatine kinase enzyme. At pH 7.4-8.0 and 35-10 °C, with a smaller substrate, dADP, specific activities of the mutant enzyme are consistently higher than the wild-type rabbit enzyme. At pH 7.1 mutant shows 23% higher specific activity than the wild-type at 35°C. At pH 7.7 and pH 8.0 at 10°C mutant G268N exhibits 2 to 2.5fold higher specific activity than the wild-type, comparable to Cyprinus carpio M1-creatine kinase. Km and kcat values similar to wild-type | Oryctolagus cuniculus |
P270G | at pH 7.1 mutant shows 30% higher specific activity than the wild-type at 35°C, in contrast to mutant G268N this mutant shows no cold-adapted characteristics | Oryctolagus cuniculus |
Localization | Comment | Organism | GeneOntology No. | Textmining |
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Organism | UniProt | Comment | Textmining |
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Oryctolagus cuniculus | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
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ADP + phosphocreatine | - |
Oryctolagus cuniculus | ATP + creatine | - |
? | |
dADP + phosphocreatine | - |
Oryctolagus cuniculus | ? | - |
? |
Synonyms | Comment | Organism |
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creatinine kinase | - |
Oryctolagus cuniculus |