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Differences in protein structure and similarities in catalytic function of two L-stereoselective carbonyl reductases
N Nakajima1, K Ishihara, S Kondo
1Department of Biochemistry and Molecular Biology, Colorado State University, Fort Collins 80523.
Bioscience, Biotechnology, and Biochemistry
|November 1, 1994
Abstract:
We purified and studied two L-stereoselective carbonyl reductases from bakers' yeast (Saccharomyces cerevisiae). One catalyzed exclusively the enantioselective reduction of carbonyl compounds such as beta-keto esters and the other acted on alpha-acetoxy ketones and beta-keto esters. The enzymes had identical molecular weights and catalyzed the L-stereoselective reduction of various carbonyl compounds with similar substrate specificity, but they were different proteins coded by different genes.