Protein Variants | Comment | Organism |
---|---|---|
T298A | mutation of the proton donor, mutant is enzymatically active, with decrease in kcat, Km, altered dissociation constants of ligands | Saccharomyces cerevisiae |
T298A | Tl+ can activate wild-type enzyme to 85% the activity in the presence of K+. With T298S, Tl+ is about 1.5fold better activator than is K+ based on the measured turnover number values. Mutation decreases turnover number value upon activation by Tl+ and by K+ | Saccharomyces cerevisiae |
T298C | Tl+ can activate wild-type enzyme to 85% the activity in the presence of K+. With T298S, Tl+ is about 1.5fold better activator than is K+ based on the measured turnover number values. Mutation decreases turnover number value upon activation by Tl+ and by K+ | Saccharomyces cerevisiae |
T298S | mutation of the proton donor, mutant is enzymatically active, with decrease in kcat, Km, altered dissociation constants of ligands | Saccharomyces cerevisiae |
T298S | Tl+ can activate wild-type enzyme to 85% the activity in the presence of K+. With T298S, Tl+ is about 1.5fold better activator than is K+ based on the measured turnover number values. Mutation decreases turnover number value upon activation by Tl+ and by K+ | Saccharomyces cerevisiae |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
K+ | wild-type enzyme and the three mutant enzymes T298S, T298C and T298A show no measurable activity in the presence of K+ or Tl+ | Saccharomyces cerevisiae | |
Tl+ | wild-type enzyme and the three mutant enzymes T298S, T298C and T298A show no measurable activity in the presence of K+ or Tl+. Tl+ can activate wild-type enzyme to 85% the activity in the presence of K+. With T298S, T298, and T298A, Tl+ is 1.2-1.8fold better activator than is K+ based on the measured turnover number values | Saccharomyces cerevisiae |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ADP + phosphoenolpyruvate | - |
Saccharomyces cerevisiae | ATP + pyruvate | - |
? |
Synonyms | Comment | Organism |
---|---|---|
YPK | - |
Saccharomyces cerevisiae |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
1.97 | - |
phosphoenolpyruvate | mutant enzyme T298A, activated be Tl+ and Mn2+ | Saccharomyces cerevisiae | |
12.2 | - |
phosphoenolpyruvate | mutant enzyme T298C, activated be Tl+ and Mn2+ | Saccharomyces cerevisiae | |
21.5 | - |
phosphoenolpyruvate | mutant enzyme T298S, activated be Tl+ and Mn2+ | Saccharomyces cerevisiae |