TY  - JOUR
A1  - Jeck, Reinhard
A1  - Woenckhaus, Christoph
A1  - Holý, Antonin
T1  - Interaction between dehydrogenases and a new NAD⊕-isomer
T2  - Zeitschrift für Naturforschung, C
N2  - 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.
KW  - NAD⊕-Isomer
KW  - Dehydrogenase
KW  - Complex Formation
Y1  - 2014
UR  - http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/72141
UR  - https://nbn-resolving.org/urn:nbn:de:hebis:30:3-721419
SN  - 0939-5075
SN  - 1865-7125
VL  - 30.1975
IS  - 11-12
SP  - 734
EP  - 738
PB  - Verlag der Zeitschrift für Naturforschung
CY  - Tübingen
ER  -