Apr 25, 1976

A kinetic study of glucose-6-phosphate dehydrogenase

The Journal of Biological Chemistry
M I KanjiW R Carper


The steady state kinetics of pig liver glucose-6-phosphate dehydrogenase is consistent with an ordered, sequential mechanism in which NADP is bound first and NADPH released last. Kia is 9.0 muM, Ka is 4.8 muM, and Kb is 36 muM. Glucosamine 6-phosphate, a substrate analogue and competitive inhibitor, is used to help rule out a possible random mechanism. ADP is seen to form a complex with the free form of the enzyme whereas ATP forms a complex with both the free and E-NADP forms of the enzyme. The KI for the E-ADP complex is 1.9 mM, while the Ki values for the E-ATP and E-NADP-ATP complexes are 7.2 and 4.5 mM, respectively.

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Mentioned in this Paper

Complex (molecular entity)
Glucosamine 6-phosphate
Glucosephosphate Dehydrogenase
Glucose-6-phosphate Dehydrogenase Measurement, Quantitative
Glucose-6-phosphate Dehydrogenase Measurement
Adenosine Triphosphate, Chromium Ammonium Salt

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