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.
Author: | Reinhard JeckGND, Christoph Woenckhaus, Antonin Holý |
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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): | Creative Commons - Namensnennung-Nicht kommerziell-Keine Bearbeitung 3.0 |