Yeast pyruvate kinase. I. Purification and some chemical properties.
نویسندگان
چکیده
منابع مشابه
Properties and function of yeast pyruvate carboxylase.
Cannata and Stoppani (1, 2) found that bakers’ yeast contains an adenosine diphosphate-dependent phosphoenolpyruvate carboxykinase, and they ascribed the essential physiological role of oxaloacetate synthesis to it. Doubts concerning their interpretation arose, however, when it was revealed (3, 4) that cellfree preparations of the same microorganism could catalyze the direct carboxylation of py...
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The dimorphic phycomycete Mucor racemosus was found to contain up to five electrophoretic forms of pyruvate kinase (ATP: pyruvate 2-O-phosphotransferase, EC 2.7.1.40) depending on growth conditions. M. racemosus hyphal cells grown on glutamic acid as the carbon source contained only the fastest electrophoretic form, designated PK1, while yeast cells grown on glucose contained only the slowest e...
متن کاملProbing 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...
متن کاملPurification and properties of rat brain pyruvate carboxylase.
Rat brain pyruvate carboxylase was purified 2000-fold and some of its properties and kinetic parameters were investigated. The use of (NH4)2SO4 gradient solubilization on a Celite column and precipitation with polyethylene glycol permitted purification to an estimated 20% purity. Except for a few subtle kinetic differences this enzyme is indistinguishable from rat liver pyruvate carboxylase.
متن کاملYeast 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...
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ورودعنوان ژورنال:
- The Journal of biological chemistry
دوره 244 18 شماره
صفحات -
تاریخ انتشار 1969