TY  - JOUR
A1  - Ehrenfeld, Michael
A1  - Jeck, Reinhard
A1  - Klatte, Walter
A1  - Kühn, Norbert
A1  - Woenckhaus, Christoph
T1  - Halbseiten-Reaktivität der Glycerinaldehyd-3-phosphat Dehydrogenase aus Kaninchen-Skelettmuskel mit Strukturanalogen von NAD
T1  - Half-of-the-sites reactivity of glycerraldehyde-3 phosphate dehydrogenase from rabbit muscle with structural analogs of NAD
T2  - Zeitschrift für Naturforschung, C
N2  - Alkylating NAD-Analogs, Glyceraldehyde-3 Phosphate Dehydrogenase, Half-of-the-Sites Reactivity co-(3-Bromoacetylpyridinio)alkyldiphosphoadenosines with alkyl chain lengths of 2 -6 me­ thylene groups inactivate glyceraldehyde-3 phosphate dehydrogenase from rabbit muscle. Half-of-the-Sites reactivity is observed in each case: The analogs are covalently bound to highly reactive cysteine residues in two of the four subunits. The remaining two subunits still bind N AD and the reactive SH-groups, although modified by SH-reagents of low molecular weight are not labeled by any of the brominated coenzyme models. This behaviour may be explained by the assumption, that the modification of 2 subunits induces structural changes in the neighboured unoccupied subunits which prevent any attack on reactive cysteine residues caused by fixation and orientation of the bromoketo-coenzyme analog when bound to the active center. Structural similarities of the covalently bound coenzyme analogs in the active center and the native ternary GAPDH-NAD-substrate complex suggest that half-of-the-sites reactivity is a natural characteristic of the enzymes catalytic mechanism.
KW  - Alkylating NAD-Analogs
KW  - Glyceraldehyde-3 Phosphate Dehydrogenase
KW  - Half-of-the-Sites  Reactivity
Y1  - 2014
UR  - http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/71387
UR  - https://nbn-resolving.org/urn:nbn:de:hebis:30:3-713872
SN  - 0939-5075
SN  - 1865-7125
VL  - 36.1981
IS  - 7-8
SP  - 545
EP  - 551
PB  - Verlag der Zeitschrift für Naturforschung
CY  - Tübingen
ER  -