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.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Carbohydrate Dehydrogenases / chemistry*
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Carbohydrate Dehydrogenases / isolation & purification*
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Carbohydrate Dehydrogenases / metabolism
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Carboxylic Ester Hydrolases / chemistry*
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Coenzymes
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Enzyme Activation
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Glucose / chemistry
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Glucosephosphates / chemistry
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Mice
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Mice, Inbred C57BL
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Microsomes, Liver / chemistry*
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Microsomes, Liver / enzymology
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Molecular Sequence Data
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Molecular Weight
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NADP / chemistry
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Pentose Phosphate Pathway
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Substrate Specificity
Substances
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Coenzymes
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Glucosephosphates
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glucose 6-(hydrogen sulfate)
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NADP
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Carbohydrate Dehydrogenases
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galactose-6-phosphate dehydrogenase
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Carboxylic Ester Hydrolases
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6-phosphogluconolactonase
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Glucose