Differences in protein structure and similarities in catalytic function of two L-stereoselective carbonyl reductases from bakers' yeast.
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.
Nakajima
N
N
Department of Biochemistry and Molecular Biology, Colorado State University, Fort Collins 80523.
Ishihara
K
K
Kondo
S
S
Tsuboi
S
S
Utaka
M
M
Nakamura
K
K
D000429:Alcohol Oxidoreductases / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D000595:Amino Acid Sequence; D002384:Catalysis; D007527:Isoenzymes / Q000737:chemistry / Q000378:metabolism*; D008969:Molecular Sequence Data; D011487:Protein Conformation; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D013379:Substrate Specificity
D007527:Isoenzymes; D000429:Alcohol Oxidoreductases