The regulatory properties of yeast pyruvate kinase.

تأثیر استرس اکسیداتیو حاصل از مصرف سیگار بر فعالیت آنزیم‌های گلیکولیزی هگزوکیناز و پیروات کیناز در اریتروسیت‌های افراد سیگاری

    Background & Aim: Hexokinase and pyruvate kinase are two regulatory enzymes of glycolytic pathway in erythrocytes. Increasing evidence suggests that cigarette smoking which produces free radicals and oxidative stress can cause damage to body macromolecules such as proteins and enzymes. The aim of the present study was to investigate the susceptibility of key enzymes of erythrocytes glycolyt...

Probing Conformational Feature of a Recombinant Pyruvate Kinase by Limited Proteolysis

Pyruvate kinase is a key enzyme in glycolytic pathway that catalyzes the transphosphorylation between phosphoenolpyruvate and ADP to yield ATP and Pyruvate. Geobacillus stearothermophillus has a stable pyruvate kinase with determined crystal structure that composed of four separate domains. Given that limited proteolysis experiments can be successfully used to probe conformational features of p...

Prevalence of Pyruvate Kinase Deficiency among the Newborns (Shiraz-Iran)

Background: The frequency of pyruvate kinase (PK) deficiency, an autosomal recessive defect, is approximately 3 per 10,000 individuals in Shiraz and surrounding areas, and is increased due to high consanguinity marriage frequency. The purpose of this study is to obtain data on the frequency and spectrum of gene mutation of PK in newborns, from Shiraz and surrounding areas. Materials and Methods...

Yeast pyruvate kinase. I. Purification and some chemical properties.

Yeast Pyruvate Kinase

The kinetic properties of purified yeast pyruvate kinase were investigated. The enzyme showed cooperative kinetics toward the essential activating monovalent cations K+ and NH4+, Mg2+, and phosphoenolpyruvate. Fructose 1,6diphosphate, which yielded homotropic cooperative kinetics and did not affect maximal velocity, transformed the sigmoidal kinetics of Kf and NH4+, Mgz+, and phosphoenolpyruvat...

The characterization and regulatory properties of pyruvate kinase from cotton seeds.

Pyruvate kinase (ATP: pyruvate phosphotransferase, EC 2.7.1.40) was partially purified from cotton seeds. The enzyme shows normal kinetics toward phosphoenolpyruvate, ADP, and magnesium or manganese. Of nearly 50 metabolites tested, the enzyme is inhibited only by ATP, UTP, citrate, and malate, and activated by AMP, GMP, and fumarate. The inhibition by citrate and ATP is not due to metal chelat...