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- W2081907145 abstract "Murine hexose-6-phosphate dehydrogenase has been purified from liver microsomes by affinity chromatography on 2′,5′-ADP–Sepharose. The purified enzyme has 6-phosphogluconolactonase activity and glucose-6-phosphate dehydrogenase activity and has a native molecular mass of 178 kDa and a subunit molecular mass of 89 kDa. Glucose 6-phosphate, galactose 6-phosphate, 2-deoxyglucose 6-phosphate, glucosamine 6-phosphate, and glucose 6-sulfate are substrates for murine hexose-6-phosphate dehydrogenase, with either NADP or deamino-NADP as coenzyme. This study confirms that hexose-6-phosphate dehydrogenase is a bifunctional enzyme which can catalyze the first two reactions of the pentose phosphate pathway." @default.
- W2081907145 created "2016-06-24" @default.
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- W2081907145 date "2003-07-01" @default.
- W2081907145 modified "2023-09-28" @default.
- W2081907145 title "Murine hexose-6-phosphate dehydrogenase: a bifunctional enzyme with broad substrate specificity and 6-phosphogluconolactonase activity" @default.
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- W2081907145 doi "https://doi.org/10.1016/s0003-9861(03)00229-7" @default.
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