PMID: 9071Aug 1, 1976

Kinetic mechanism from steady-state kinetics of the reaction catalysed by baker's-yeast glucose 6-phosphate dehydrogenase in solution and covalently attached to sepharose

The Biochemical Journal
B J Gould, M A Goheer

Abstract

1. The reaction catalysed by glucose 6-phosphate dehydrogenase (D-glucose 6-phosphate-NADP+ oxidoreductase, EC 1.1.1.49) from baker's yeast was studied in 42mM-glycylglycine buffer, pH7.4 at 25 degrees C, by initial-velocity studies and by the use of NADPH as a product inhibitor. 2. The reactions catalysed by both the soluble enzyme and a stable enzyme covalently attached to CNBr-activated Sepharose 4B probably follow an ordered reaction mechanism with NADP+ and NADPH as the leading reactants. 3. The kinetic constants obtained for the soluble enzyme lere: KNADP+m, 19 muM; KNADP+s, 23 muM; KNADPHs, 15 muM. Similar values were obtained for the immobilized enzyme. 4. The assay of the immobilized enzyme was done by using a micro packed-bed recirculation reactor, and the advantages of this technique are discussed.

Citations

Jan 1, 2009·Biomicrofluidics·Yegermal Tesfaw AtalayJeroen Lammertyn
Mar 14, 2009·Angewandte Chemie·Michael KirschThomas Schrader

Related Concepts

Cyanogen Bromide
Glucosephosphate Dehydrogenase
NADP
Saccharomyces cerevisiae
Sepharose

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