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Purification and some properties of a hepatic NADPH-dependent reductase that specifically acts on 1,5-anhydro-D-fructose

Sakuma, M ; Kametani, S ; Akanuma, H

Journal of biochemistry (Tokyo), 1998, Vol.123 (1), p.189-193 [Periódico revisado por pares]

England: Oxford University Press

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Título:
Purification and some properties of a hepatic NADPH-dependent reductase that specifically acts on 1,5-anhydro-D-fructose
Autor: Sakuma, M ; Kametani, S ; Akanuma, H
Assuntos: 1,5-anhydro-d-fructose reductase ; 1,5-anhydro-d-glucitol ; 5-anhydro-D-fructose ; 5-anhydro-D-fructose reductase ; 5-anhydro-D-glucitol ; alcohol oxidoreductases ; Amino Acid Sequence ; Animals ; Catalysis ; enzyme activity ; Enzyme Inhibitors ; Fructose - analogs & derivatives ; Fructose - metabolism ; glycogen ; glycogenolysis ; hexuloses ; Kinetics ; liver ; Liver - enzymology ; Molecular Sequence Data ; molecular weight ; purification ; reduction ; Substrate Specificity ; Sugar Alcohol Dehydrogenases - antagonists & inhibitors ; Sugar Alcohol Dehydrogenases - isolation & purification ; Sugar Alcohol Dehydrogenases - metabolism ; Swine ; Temperature
É parte de: Journal of biochemistry (Tokyo), 1998, Vol.123 (1), p.189-193
Notas: 2To whom correspondence should be addressed. Fax: +81-3-3485-2904, Tel: +81-3-5454-6584
1Present address: Biophysical Pharmaceutics Lab., Medicinal Research Laboratories, Taisho Pharmaceutical Co., Ltd., Yoshino, Ohmiya, Saitama 330.
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ArticleID:123.1.189
ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
Descrição: Glycogen gives rise to 1,5-anhydro-D-fructose (AF), which is then reduced to 1,5-anhydro-D-glucitol (AG) in animal livers. An enzyme that catalyzes NADPH-dependent reduction of AF to AG was isolated and purified to homogeneity from porcine liver. Its apparent molecular mass was about 38 kDa on the basis of SDS-PAGE, and its monomeric dispersion in aqueous solution was indicated by gel filtration on a Superose 12 column. Amino acid sequences were determined for four peptides obtained from the purified enzyme. The resulting sequences covered about 50% of the whole sequence and indicated a remarkable similarity between the enzyme and aldose reductase. The purified enzyme showed molecular activity of 8.7 s−1 on the basis of a molecular mass of 38 kDa, and a Km value of 0.44 mM for AF at the optimum pH of 7.0. It reduced pyridine-3-aldehyde and 2, 3-butanedione effectively, acetaldehyde, glucosone, and glucuronic acid poorly and showed no detectable action on glucose, mannose and fructose. It was inactivated by p-chloromercuribenzoic acid to a considerable extent, and the inactivation was partially reversed by 2-mercaptoethanol treatment. It was also sparingly inhibited by relatively high concentrations of glucose, glucose-1(6)-phosphate and 1,5-anhydroglucitol. The reverse reaction, i.e., NADP+ -dependent AG oxidation, was not observed. The observed catalytic properties and partial amino acid sequences rule out the possibility that the isolated protein is identical with any known reductase.
Editor: England: Oxford University Press
Idioma: Inglês

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Purification and some properties of a hepatic NADPH-dependent reductase that specifically acts on 1,5-anhydro-D-fructose

Sakuma, M ; Kametani, S ; Akanuma, H

England: Oxford University Press

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