Abstract
The catalytic activity of AdoHcy hydrolase requires formation of a stable complex with the cofactor NAD (Palmer and Abeles, 1976). In addition to NAD, Hershfield and Kredich (1978) identified AdoHcyase as the so-called ’cAMP-Ado’ or ’adenine analogue’ binding protein that had been isolated by a number of investigators (Yuh and Tao, 1974; Sugden and Corbin, 1976; Ueland and Doskeland, 1977; Olsson, 1978). The ability to form stable complexes with NAD, Ado and its analogs, and cAMP raises questions regarding the relationship of AdoHcyase to other proteins that bind these ligands, and possible functions of ligand binding, which might be related or unrelated to the role of this enzyme in metabolism.
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Hershfield, M.S., Aiyar, V.N., Chaffee, S., Curtis, S., Greenberg, M.L. (1986). Probes for Examining the Structure and Function of Human S-Adenosylhomocysteine Hydrolase, and for Isolation of cDNA. In: Borchardt, R.T., Creveling, C.R., Ueland, P.M. (eds) Biological Methylation and Drug Design. Experimental Biology and Medicine, vol 12. Humana Press. https://doi.org/10.1007/978-1-4612-5012-8_21
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DOI: https://doi.org/10.1007/978-1-4612-5012-8_21
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