Chirality of the Hydrogen Transfer to the Coenzyme Catalyzed by Ribitol Dehydrogenase from Klebsiella Pneumoniae and D-Mannitol 1-Phosphate Dehydrogenase from Escherichia coli

Chirality of the Hydrogen Transfer to the Coenzyme Catalyzed by Ribitol Dehydrogenase from... Hoppe-Seyler's Z. Physiol. Chem. Bd. 357, S. 1163 -1169, August 1976 Chirality of the Hydrogen Transfer to the Coenzyme Catalyzed by Ribitol Dehydrogenase from Klebsiella Pneumoniae and D-Mannitol 1-Phosphate Dehydrogenase from Escherichia coli Miguel A. ALIZADE , Karl GAEDE and Klaus BRENDEL Departamento de Bioquimica, Institute Venezolano de Investigaciones Cientificas, and Department of Pharmacology, College of Medicine, The University of Arizona (Received 14 May 1976) Herrn Prof. Dr. Joachim Kuehnau zum 75. Geburtstag in Verehrung gewidmet Summary: The stereochemistry of the hydrogen transfer to NAD catalyzed by ribitol dehydrogenase (ribitol: N AD® 2-oxidoreductase, EC 1.1.1.56) from Klebsiella pneumoniae and D-mannitol-1-phosphate dehydrogenase (o-mannitol-1-phosphate:NAD® 2-oxidoreductase, EC 1.1.1.17) from Escherichia coli was investigated. [4-3H]NAD was enzymatically reduced with nonlabelled ribitol in the presence of ribitol dehydrogenase and with nonlabelled D -mannitol 1-phosphate and D-mannitol 1-phosphate dehydrogenase, respectively. In both cases the [4-3H]NADH produced was isolated and the chirality at the C-4 position determined. It was found that after the transfer of hydride, the label was in both reactions exclusively confined to the (4R ) position of the newly formed [4-3H]NADH. In order to explain these results, the hydrogen transferred from the nonlabelled substrates to [4-3H]NAD must have entered the (45) position http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png hoppe-seyler's zeitschrift für physiologische chemie de Gruyter

Chirality of the Hydrogen Transfer to the Coenzyme Catalyzed by Ribitol Dehydrogenase from Klebsiella Pneumoniae and D-Mannitol 1-Phosphate Dehydrogenase from Escherichia coli

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Publisher
de Gruyter
Copyright
Copyright © 1976 by the
ISSN
0018-4888
eISSN
1437-4315
DOI
10.1515/bchm2.1976.357.2.1163
Publisher site
See Article on Publisher Site

Abstract

Hoppe-Seyler's Z. Physiol. Chem. Bd. 357, S. 1163 -1169, August 1976 Chirality of the Hydrogen Transfer to the Coenzyme Catalyzed by Ribitol Dehydrogenase from Klebsiella Pneumoniae and D-Mannitol 1-Phosphate Dehydrogenase from Escherichia coli Miguel A. ALIZADE , Karl GAEDE and Klaus BRENDEL Departamento de Bioquimica, Institute Venezolano de Investigaciones Cientificas, and Department of Pharmacology, College of Medicine, The University of Arizona (Received 14 May 1976) Herrn Prof. Dr. Joachim Kuehnau zum 75. Geburtstag in Verehrung gewidmet Summary: The stereochemistry of the hydrogen transfer to NAD catalyzed by ribitol dehydrogenase (ribitol: N AD® 2-oxidoreductase, EC 1.1.1.56) from Klebsiella pneumoniae and D-mannitol-1-phosphate dehydrogenase (o-mannitol-1-phosphate:NAD® 2-oxidoreductase, EC 1.1.1.17) from Escherichia coli was investigated. [4-3H]NAD was enzymatically reduced with nonlabelled ribitol in the presence of ribitol dehydrogenase and with nonlabelled D -mannitol 1-phosphate and D-mannitol 1-phosphate dehydrogenase, respectively. In both cases the [4-3H]NADH produced was isolated and the chirality at the C-4 position determined. It was found that after the transfer of hydride, the label was in both reactions exclusively confined to the (4R ) position of the newly formed [4-3H]NADH. In order to explain these results, the hydrogen transferred from the nonlabelled substrates to [4-3H]NAD must have entered the (45) position

Journal

hoppe-seyler's zeitschrift für physiologische chemiede Gruyter

Published: Jan 1, 1976

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