Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.7.1.40 extracted from

  • Susan-Resiga, D.; Nowak, T.
    The Proton Transfer Step Catalyzed by Yeast Pyruvate Kinase (2003), J. Biol. Chem., 278, 12660-12671.
    View publication on PubMed

Protein Variants

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

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

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ADP + phosphoenolpyruvate
-
Saccharomyces cerevisiae ATP + pyruvate
-
?

Synonyms

Synonyms Comment Organism
YPK
-
Saccharomyces cerevisiae

Turnover Number [1/s]

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