Chemical specificity of pyruvate kinase from yeast.
Biochim Biophys Acta
; 384(1): 120-6, 1975 Mar 28.
Article
em En
| MEDLINE
| ID: mdl-1093568
ABSTRACT
Three analogs of phosphoenolpyruvic acid (Z)-phosphoenol-3-fluoropyruvate, (Z)-phosphoenol-3-bromopyruvate and (Z)-phosphoenol-alpha-ketobutyrate were found to be substrates for yeast pyruvate kinase (ATP pyruvate (Z)-O-phosphotransferase, EC 2.7.1.40)with maximal velocities much greater than those found for rabbit muscle pyruvate kinase. The analogs exhibited sigmoidal kinetics, which become hyperbolic upon addition of the allosteric effector, fructose 1,6-diphosphate. Moreover, the reaction of (Z)-phosphoenol-3-bromopyruvate with ADP to produce bromopyruvic acid and ATP irreversibly inhibited the enzyme with a half-life of 32 min.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Piruvato Quinase
/
Saccharomyces cerevisiae
Idioma:
En
Revista:
Biochim Biophys Acta
Ano de publicação:
1975
Tipo de documento:
Article