descriptionPublicationkeyboard_double_arrow_right Article 01 Apr 1976 English Publisher:Elsevier BVJournal:Clinica Chimica Acta, volume 68, pages 11-15 (issn: 0009-8981,

Authors: A.M.C. Vlug; M.L. Hamelink; R.P. Ceerdink; G.E.J. Staal;

doi: 10.1016/0009-8981(76)90283-7

pmid: 1261049

Defective erythrocyte pyruvate kinase

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Abstract

A defective pyruvate kinase (EC 2.7.1.40) is described. The abnormal PK is characterized by a shift in the R in equilibrium T equilibrium to the T-state. The Ko.5 for the substrate phosphoenol pyruvate is about 6 times higher than for the normal enzyme, while the KM value for the positive effector Fru-1, 6-P2 is increased. In agreement with a shift to the T-state is the increased affinity of the abnormal enzyme for the negative effectors ATP and alanine. The results are discussed in relation to other abnormal pyruvate kinases.

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Keywords

Adult, Male, Alanine, Erythrocytes, Pyruvate Kinase, Fructosephosphates, Phosphoenolpyruvate, Kinetics, Adenosine Triphosphate, Humans, Hexosediphosphates, Carbohydrate Metabolism, Inborn Errors

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