Murine hexose-6-phosphate dehydrogenase: a bifunctional enzyme with broad substrate specificity and 6-phosphogluconolactonase activity
| Autor: | Philip J. Mason, Julia L. Clarke |
|---|---|
| Rok vydání: | 2003 |
| Předmět: |
Molecular Sequence Data
Biophysics Coenzymes Dehydrogenase Pentose phosphate pathway Biochemistry Cofactor Substrate Specificity Pentose Phosphate Pathway Mice Affinity chromatography Animals Phosphofructokinase 2 Amino Acid Sequence Molecular Biology chemistry.chemical_classification biology Molecular mass Glucosephosphates Molecular biology Enzyme Activation Mice Inbred C57BL Molecular Weight Enzyme Glucose chemistry biology.protein Microsomes Liver Carbohydrate Dehydrogenases Branched-chain alpha-keto acid dehydrogenase complex Carboxylic Ester Hydrolases NADP |
| Zdroj: | Archives of biochemistry and biophysics. 415(2) |
| ISSN: | 0003-9861 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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