May 17, 1976

Studies on the active site of yeast hexokinase. Specific phosphorylation of a serine residue induced by D-xylose and ATPMg

European Journal of Biochemistry
L C Menezes, J Pudles

Abstract

Yeast hexokinase A(ATP:D-hexose 6-phosphotransferase) is inactivated when incubated in the presence of xylose and ATPMg, or in the presence of D-lyxose in a reaction medium in which ATPMg is being continuously regenerated (phosphoenolpyruvate and pyruvate kinase). The inactivation is due to the phorphorylation of the protein. A linear relationship was observed between the inactivation and the incorporation of 32P from [gamma-32P] ATP. All hexokinase and ATPase activity of the enzyme is lost when one phosphoryl group is incorporated per enzyme subunit (molecular weight 51,000). The phosphoryl group is covalently bound by a ester linkage with a serine residue of the protein.

Mentioned in this Paper

Hexokinase A
lyxose
Protein Phosphorylation
Pyruvate Kinase
Hexokinase
Plasma Protein Binding Capacity
Hexokinase 2
Protein Conformation
Pyruvate Kinase Measurement
Xylose

About this Paper

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