Secondary kinase reactions catalyzed by yeast pyruvate kinase.
Biochim Biophys Acta, 1976/6/07;438(1):108-18.
PMID: 7314
Abstract
1. Yeast pyruvate kinase (EC 2.7.1.40) catalyzes, in addition to the primary, physiologically important reaction, three secondary kinase reactions, the ATP-dependent phosphorylations of fluoride (fluorokinase), hydroxylamine (hydroxylamine kinase) and glycolate (glycolate kinase). 2. These reactions are accelerated by fructose-1,6-bisphosphate, the allosteric activator of the primary reaction. Wth Mg2+ as the required divalent cation, none of these reactions are observed in the absence of fructose-biphosphate. With Mn2+, fructose-bisphosphate is required for the glycolate kinase reaction, but merely stimulates the other reactions. 3. The effect of other divalent cations and pH on three secondary kinase reactions was also examined. 4. Results are compared with those obtained from muscle pyruvate kinase and the implications of the results for the mechanism of the yeast enzyme are discussed.
MeSH terms
Adenosine Triphosphate; Allosteric Regulation; Cobalt; Fluorides; Fructosephosphates; Glycolates; Hydrogen-Ion Concentration; Hydroxylamines; Kinetics; Magnesium; Manganese; Nickel; Pyruvate Kinase; Saccharomyces cerevisiae; Zinc
More resources
EndNote: Download