A novel zinc-containing alpha-keto ester reductase from actinomycete: An approach based on protein chemistry and bioinformatics

• Published in: Bioscience, biotechnology, and biochemistry biotechnology, and biochemistry, 2004, Vol.68 (10), p.2120-2127
• Main Authors: Ishihara, K. (Okayama Univ. of Science (Japan)), Yamaguchi, H, Omori, T, Uemura, T, Nakajima, N, Esaki, N
• Format: Article
• Language: English
• Subjects: ACTINOMYCETALES; Alcohol Dehydrogenase - metabolism; Alcohol Oxidoreductases - metabolism; AMINO ACID SEQUENCES; Biological and medical sciences; CELL CULTURE; Cloning, Molecular; Computational Biology; enzyme purification; ESTERS; Fundamental and applied biological sciences. Psychology; INFORMATION SCIENCE; keto ester; OXIDOREDUCTASES; PURIFICATION; reductase; SELECTION; STREPTOMYCES; Streptomyces coelicolor - enzymology; Substrate Specificity - physiology; ZINC; Zinc - metabolism; α-hydroxy ester producing enzyme
• ISSN: 0916-8451; 1347-6947
• DOI: 10.1271/bbb.68.2120

We have achieved the purlacatloll of an alpha-keto esterreductase(SCKER)fromS.coelior A3(2) whole cells.SCKER proved to be a homotetramer or 132 kDacontaining one equivalent of zinc ion per subunit.Theenzyme differed from other alpha-keto ester reductasesfrom microorganisms wlth regard to subunjt struetureand metal ion dependency. From a computer searchusing the protein data banks, the N-terminal amino acidsequence of SCKER was consistent with that of apossible zinc containing alcohol dehydrogenase inS,coelicoler A3(2).None of three hypothetical proteins of S.coelocor A3(2)having a high homology sequence with those of already purified a-keto ester reductases from S.thermacyaneoviolacceus [Yamaguchi, H.,el., Biosci Biotechnol. Biochem., 66, 588-597(2002)] was identical with that of SCKER.