Purification and characterization of alpha-keto amide reductase from Saccharomyces cerevisiae.
An NADPH-dependent alpha-keto amide reductase was purified from Saccharomyces cerevisiae. The molecular mass of the native enzyme was estimated to be 33 and 36 kDa by gel filtration chromatography and SDS-polyacrylamide gel electrophoresis, respectively. The purified enzyme showed a reducing activity not only for aromatic alpha-keto amides but also for aliphatic and aromatic alpha-keto esters. The internal sequence of the enzyme was identical with that of a hypothetical protein (ORF YDL 124w) coded by yeast chromosome IV.
Ishihara
Kohji
K
Department of Life Science, Okayama University of Science, Okayama, Japan. ishihara@das.ous.ac.jp
Yamamoto
Hiroaki
H
Mitsuhashi
Kazuya
K
Nishikawa
Kazuyoshi
K
Tsuboi
Sadao
S
Tsuji
Hideaki
H
Nakajima
Nobuyoshi
N
D000429:Alcohol Oxidoreductases / Q000737:chemistry* / Q000302:isolation & purification; D000645:Ammonium Sulfate; D004952:Esters / Q000737:chemistry; D006863:Hydrogen-Ion Concentration; D007202:Indicators and Reagents; D007651:Keto Acids / Q000737:chemistry; D007700:Kinetics; D008968:Molecular Conformation; D008970:Molecular Weight; D010084:Oxidation-Reduction; D011479:Protamines; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry* / Q000302:isolation & purification; D013237:Stereoisomerism; D013379:Substrate Specificity; D013696:Temperature
D004952:Esters; D007202:Indicators and Reagents; D007651:Keto Acids; D011479:Protamines; D029701:Saccharomyces cerevisiae Proteins; D000429:Alcohol Oxidoreductases; C500714:YDL124W protein, S cerevisiae; D000645:Ammonium Sulfate