Abstract
Enzymes with tightly bound NAD(P), acting as cofactor, have been described in the past. Well known examples include UDP-galactose 4-epimerase from E. coli (Wilson and Hogness, 1964) and lactate-oxaloacetate transhydrogenase from V. alcalescens (Allen, 1966). Recently enzymes have been discovered in which the bound NAD(P) acts as cofactor in the oxidation/reduction of alcohols/aldehydes and the reducing equivalents do not exchange with the cytosolic NAD(P) pool but are probably transferred to the respiratory chain (Arfman, 1991, Bystrykh, 1993, van Ophem, 1993). These enzymes operate in the same way as, e.g., flavoprotein or quinoprotein alcohol dehydrogenases and are clearly distinct from the NAD(P)(H) dependent alcohol/aldehyde oxidoreductases in a physiological sense. In the latter case nicotinamide pyridine dinucleotide acts as coenzyme (i.e. as co-substrate) and forms part of the cytosolic NAD(H) pool. We have introduced the name nicotinoproteins for this new group of NAD(P)(H) containing enzymes (van Ophem, 1993). Nicotinoproteins are proteins which contain NAD(P)(H) as tightly bound, redox active cofactor. The pyridine dinucleotide in these enzymes is strongly but not covalently bound and does not exchange with the cytosolic NAD(P) pool. In Table 1 enzymological data of some of the nicotinoproteins known presently is summarised.
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Piersma, S.R., de Vries, S., Duine, J.A. (1996). Nicotinoprotein Alcohol/Aldehyde Oxidoreductases. In: Weiner, H., Lindahl, R., Crabb, D.W., Flynn, T.G. (eds) Enzymology and Molecular Biology of Carbonyl Metabolism 6. Advances in Experimental Medicine and Biology, vol 414. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-5871-2_48
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