Interaction between dehydrogenases and a new NAD⊕-isomer

  • A new NAD⊕-isomer was prepared, in which the ᴅ-ribose of the adenosine moiety was sub­ stituted by the enantiomeric ʟ-ribose. As compared to nicotinamide-adenine-dinucleotide (NAD⊕) and NADH the coenzyme isomer (ᴅ,ʟ)-NAD⊕ and its dihydroform (ᴅ,ʟ)-NADH are far less tightly bound to lactate dehydrogenase and alcohol dehydrogenase from horse liver. In the presence of the second substrate (ᴅ,ʟ)-NAD⊕ and (ᴅ,ʟ)-NADH act as hydrogen acceptor and hydrogen donator, respectively, with lactate dehydrogenase and alcohol dehydrogenases from horse liver and yeast. Compared to NAD⊕ and NADH the Michaelis constants are always increased, the catalytic constants (V/Et) were found to be decreased except for the dihydroform reacting with alcohol dehydrogenase from liver.

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Metadaten
Author:Reinhard JeckGND, Christoph Woenckhaus, Antonin Holý
URN:urn:nbn:de:hebis:30:3-721419
DOI:https://doi.org/10.1515/znc-1975-11-1207
ISSN:0939-5075
ISSN:1865-7125
Parent Title (German):Zeitschrift für Naturforschung, C
Publisher:Verlag der Zeitschrift für Naturforschung
Place of publication:Tübingen
Document Type:Article
Language:English
Date of Publication (online):2014/06/02
Year of first Publication:1975
Publishing Institution:Universitätsbibliothek Johann Christian Senckenberg
Release Date:2024/01/30
Tag:Complex Formation; Dehydrogenase; NAD⊕-Isomer
Volume:30.1975
Issue:11-12
Page Number:5
First Page:734
Last Page:738
Institutes:Medizin
Biochemie, Chemie und Pharmazie / Biochemie und Chemie
Dewey Decimal Classification:5 Naturwissenschaften und Mathematik / 54 Chemie / 540 Chemie und zugeordnete Wissenschaften
5 Naturwissenschaften und Mathematik / 57 Biowissenschaften; Biologie / 570 Biowissenschaften; Biologie
Sammlungen:Universitätspublikationen
Licence (German):License LogoCreative Commons - Namensnennung-Nicht kommerziell-Keine Bearbeitung 3.0