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Importance of the position of the adenosine linkage in nad for its coenzyme activity via lactate dehydrogenase ec 1.1.1.27

Schlimme, E.R.M.; Schott, E.

Zeitschrift fuer Naturforschung Section C Journal of Biosciences 37(3-4): 342-344

1982

Accession: 005640589
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The chemical preparation of the NAD+ analog P1, P2-(5'-.beta.-nicotinamideribofuranosyl-3"-adenosyl)-diphosphate (N3"AD+) by applying the 1,1'carbonyldiimidazole activation method is reported. The importance of how adenosine is linked to the NMN phosphoriboside moiety is discussed with respect to the coenzyme activity in the lactate dehydrogenase catalyzed reaction.

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Related References

Schlimme, E.; Mattern, R.; Schott, E. 1982: The importance of the position of the adenosine linkage in NAD+ for its coenzyme activity via lactate dehydrogenase Zeitschrift für Naturforschung. Section C Biosciences 37(3-4): 342-344
Holbrook, J.J. 1966: The importance of SH-groups for enzymic activity. V. the coenzyme-binding capacity of pig heart lactate dehydrogenase, isozyme I, after inhibition by various maleinimides Biochemische Zeitschrift 344(2): 141-152
Duffy, P.; Sanderson, J.C. 1971: Studies on the control of lactate dehydrogenase activity in mammalian cells. II. Demonstration of rapid continuous variations in lactate dehydrogenase activity in humans erythrocytes and their relation to a biological activator and an inhibitor of lactate dehydrogenase Biochimica et Biophysica Acta 244(3): 613-617
Siebert, G.; Baessler, K.H.; Schmitt, A. 1962: Apparent irreversibility of TPNH oxidation by lactate dehydrogenase. a contribution to coenzyme specificity of lactate dehydrogenase from rabbit muscle Biochemische Zeitschrift 336: 402-420
Duffy, P. 1971: Studies on the control of lactate dehydrogenase activity in mammalian cells. I. Demonstration of rapid continuous variations in lactate dehydrogenase activity in cultured cells and their relation to a biological activator and an inhibitor of lactate dehydrogenase Biochimica et Biophysica Acta 244(3): 606-612
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