TY  - JOUR
A1  - Jeck, Reinhard
T1  - Eigenschaften der [ω-(3-Acetylpyridinium)-n-alkyl]-adenosin-pyrophosphate als Strukturanaloge des Coenzyms NAD
T1  - The properties of [ω-(3-Acetylpyridinio)-n-alkyl] adenosine pyrophosphates, structural analogs of the coenzyme NAD
T2  - Zeitschrift für Naturforschung, C
N2  - [ω- (3-Acetylpyridinio) -n-alkyl] adenosine pyrophosphates are coenzyme analogs of NAD⊕. The adenosine pyrophosphate moiety and the 3-acetylpyridine ring of the analogs are connected by n-alkyl chains of different lengths (ethyl -hexyl). The analogs form strong dissociating complexes with lactate dehydrogenase. The complex formation is predominantly achieved by interaction of the ADP moiety with its respective binding domain at the active site.
The redox potentials of the analogs and NAD are of similar magnitude. The coenzyme function of the analogs depends upon the length of the hydrocarbon chain. Lactate dehydrogenase and alcohol dehydrogenases from yeast and horse liver do not catalize hydrogen transfer from their substrates to any other alkyl analog but [4- (3-acetylpyridinio)-n-butyl] adenosine pyrophosphate, aldehyde dehydrogenase from horse liver catalizes hydrogen transfer from acetaldehyde to the pentyl derivative and glyceraldehyde-3-phosphate dehydrogenase catalizes hydrogen transfer to both analogs. In no case, hydrogen transfer from or to one of the 3-acetylpyridine-n-alkyl analogs proceeded with a velocity comparable to NAD or its 3-acetylpyridine analog. The results show that the nicotinamide bound ribose in NAD is involved in the binding and the activation of the coenzyme.
KW  - NAD Analogs
KW  - Substitution of Ribose
KW  - Dehydrogenases
KW  - Complex Formation
Y1  - 2014
UR  - http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/71946
UR  - https://nbn-resolving.org/urn:nbn:de:hebis:30:3-719465
SN  - 0939-5075
SN  - 1865-7125
VL  - 32.1977
IS  - 7-8
SP  - 550
EP  - 556
PB  - Verlag der Zeitschrift für Naturforschung
CY  - Tübingen
ER  -