Abstract
Tetrameric carbonyl reductase (CR, EC 1.1.1.184) of guinea-pig, mouse and pig lung differs from CRs of other mammalian tissues in subunit structure, broad substrate specificity for aromatic and aliphatic carbonyl compounds, reversibility of the reaction and sensitivity to pyrazole (Nakayama et al., 1982, 1986; Oritani et al., 1992). It is also uniquely activated by fatty acids and dipyridyl compounds (Hara et al., 1992a, 1993). The cDNA for pig lung has been cloned (Nakanishi et al., 1993). The enzyme is composed of 244 amino acids, and is structurally related to members of the short-chain alcohol dehydrogenase (SCAD) family, which includes eucaryotic and procaryotic enzymes with different substrate specificity (Persson et al., 1990; Neidle et al, 1992; Krozowski, 1992).
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Deyashiki, Y., Nakanishi, M., Sakai, M., Hara, A. (1995). Lysine Residues in the Coenzyme-Binding Region of Mouse Lung Carbonyl Reductase. In: Weiner, H., Holmes, R.S., Wermuth, B. (eds) Enzymology and Molecular Biology of Carbonyl Metabolism 5. Advances in Experimental Medicine and Biology, vol 372. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-1965-2_30
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DOI: https://doi.org/10.1007/978-1-4615-1965-2_30
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