Abstract
A broad family of NADPH-dependent oxidoreductases catalyze the reduction of various aldehydes and ketones to their corresponding alcohols. Members include the enzymes aldose reductase (EC 1.1.1.21), aldehyde reductase (EC 1.1.1.2) and carbonyl reductase (EC 1.1.1.184). Aldose reductase and aldehyde reductase, discovered by Hers (1960) in the late 1950’s, were named for their ability to reduce aldonic sugars versus aliphatic and aromatic aldehydes (Felsted and Bachur, 1980; Turner and Flynn, 1982). Aldehyde reductase, however, is also known as L-hexonate dehydrogenase (EC 1.1.1.19) because of its ability to utilize NADP+ to oxidize aldonic acids such as L-gulonate to D-glucuronate (Mano et al., 1961). Carbonyl reductase was first described in the 1970’s as “aromatic aldehyde and ketone reductase” by Culp and McMahon (1968). More recently, it has been referred to as carbonyl reductase (Wermuth, 1981) .
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© 1990 Plenum Press, New York
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Sato, S. (1990). Purification of Aldose and Aldehyde Reductases from Dog Kidney. In: Weiner, H., Wermuth, B., Crabb, D.W. (eds) Enzymology and Molecular Biology of Carbonyl Metabolism 3. Advances in Experimental Medicine and Biology, vol 284. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-5901-2_18
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DOI: https://doi.org/10.1007/978-1-4684-5901-2_18
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