Abstract: The present invention relates to a polypeptide having an activity to asymmetrically reduce (3S)-1-chloro-3-tert-butoxycarbonylamino-4-phenyl-2-butanone to produce (2R,3S)-1-chloro-3-tert-butoxycarbonylamino-4-phenyl-2-butanol isolated from a microorganism belonging to the genus Ogataea, a DNA encoding the polypeptide and a transformant that produces the polypeptide. The present invention moreover relates to a method of producing (2R,3S)-1-chloro-3-tert-butoxycarbonylamino-4-phenyl-2-butanol utilizing the polypeptide or the transformant. Using the polypeptide or transformant of the present invention, optically active alcohols such as (2R,3S)-1-chloro-3-tert-butoxycarbonylamino-4-phenyl-2-butanol and the like can be produced efficiently.

Abstract: The present invention relates to a polypeptide having an activity to asymmetrically reduce (3S)-1-chloro-3-tert-butoxycarbonylamino-4-phenyl-2-butanone to produce (2R,3S)-1-chloro-3-tert-butoxycarbonylamino-4-phenyl-2-butanol isolated from a microorganism belonging to the genus Ogataea, a DNA encoding the polypeptide and a transformant that produces the polypeptide. The present invention moreover relates to a method of producing (2R,3S)-1-chloro-3-tert-butoxycarbonylamino-4-phenyl-2-butanol utilizing the polypeptide or the transformant. Using the polypeptide or transformant of the present invention, optically active alcohols such as (2R,3S)-1-chloro-3-tert-butoxycarbonylamino-4-phenyl-2-butanol and the like can be produced efficiently.

Abstract: The present invention relates to a polypeptide having an activity to asymmetrically reduce (3S)-1-chloro-3-tert-butoxycarbonylamino-4-phenyl-2-butanone to produce (2R,3S)-1-chloro-3-tert-butoxycarbonylamino-4-phenyl-2-butanol isolated from a microorganism belonging to the genus Ogataea, a DNA encoding the polypeptide and a transformant that produces the polypeptide. The present invention moreover relates to a method of producing (2R,3S)-1-chloro-3-tert-butoxycarbonylamino-4-phenyl-2-butanol utilizing the polypeptide or the transformant. Using the polypeptide or transformant of the present invention, optically active alcohols such as (2R,3S)-1-chloro-3-tert-butoxycarbonylamino-4-phenyl-2-butanol and the like can be produced efficiently.

Abstract: Disclosed is an isolated DNA comprising a nucleotide sequence coding for an enzyme having enone reductase activity wherein the enzyme is characterized by the following physico-chemical properties: (a) molecular mass: 61,300±5,000 Da (estimated using gel filtration, consisting of one subunit); (b) co-factor: NADPH and NADH; (c) substrate specificity: active on ?,?-unsaturated ketons; (d) optimum temperature: 55-60° C. at pH 7.4; and (e) optimum pH: pH 4.5-8.5.

Abstract: It has been required to economically produce a large amount of optically active ?-lactone derivatives (for example, pantolactone), which are useful as intermediates in synthesizing useful substances such as pharmaceutical drugs. To achieve this object, it is advantageous to employ an enzymatic technique of asymmetric hydrolysis with a hydrolyzing enzyme lactonase. However, it remains troublesome to prepare the enzyme or utilize a microorganism capable of producing the enzyme. Also, it is difficult to obtain a sufficient and stable enzymatic activity in the case of using recombination techniques. In producing lactonase, which asymmetrically hydrolyzes a ?-lactone derivative such as racemic pantolactone selectively, by a recombination technique, both mature lactonase DNA and signal peptide region DNA are transferred into a host.

Abstract: The present invention relates to a polypeptide having an activity to asymmetrically reduce (3S)-1-chloro-3-tert-butoxycarbonylamino-4-phenyl-2-butanone to produce (2R,3S)-1-chloro-3-tert-butoxycarbonylamino-4-phenyl-2-butanol isolated from a microorganism belonging to the genus Ogataea, a DNA encoding the polypeptide and a transformant that produces the polypeptide. The present invention moreover relates to a method of producing (2R,3S)-1-chloro-3-tert-butoxycarbonylamino-4-phenyl-2-butanol utilizing the polypeptide or the transformant. Using the polypeptide or transformant of the present invention, optically active alcohols such as (2R,3S)-1-chloro-3-tert-butoxycarbonylamino-4-phenyl-2-butanol and the like can be produced efficiently.

Abstract: It has been required to economically produce a large amount of optically active ?-lactone derivatives (for example, pantolactone), which are useful as intermediates in synthesizing useful substances such as pharmaceutical drugs. To achieve this object, it is advantageous to employ an enzymatic technique of asymmetric hydrolysis with a hydrolyzing enzyme lactonase. However, it remains troublesome to prepare the enzyme or utilize a microorganism capable of producing the enzyme. Also, it is difficult to obtain a sufficient and stable enzymatic activity in the case of using recombination techniques. In producing lactonase, which asymmetrically hydrolyzes a ?-lactone derivative such as racemic pantolactone selectively, by a recombination technique, both mature lactonase DNA and signal peptide region DNA are transferred into a host.

Abstract: An isolated enone reductase characterized by a molecular mass of 61300+/?5000 Da; NADPH and NADPH as co-factor; a temperature optimum of 55–60° C. at pH 7.4; a pH optimum of 4.5–8.5 and substrate specificity on ?,?-unsatured ketones; a process for producing it from a microorganism and a process for producing levodione from ketoisophorone using such reductase.

Abstract: A protein, which is an aminoketone asymmetric reductase, having an effect of producing d-pseudoephedrine by acting on 1-2-methylaminopropiophenone, and having the following physiochemical properties: substrate: 1-2-methylaminopropiophenone optimum pH: pH 8.1 optimum temperature: 55° C. coenzyme: NADP molecular weight: about 28500 Da homotetramer and a nucleic acid coding the protein.

Abstract: Disclosed is an isolated DNA comprising a nucleotide sequence coding for an enzyme having enone reductase activity wherein the enzyme is characterized by the following physico-chemical properties: (a) molecular mass: 61,300±5,000 Da (estimated using gel filtration, consisting of one subunit); (b) co-factor: NADPH and NADH; (c) substrate specificity: active on ?,?-unsaturated ketons; (d) optimum temperature: 55-60° C. at pH 7.4; and (e) optimum pH: pH 4.5-8.5.

Abstract: An isolated enone reductase characterized by a molecular mass of 61300+/?5000 Da; NADPH and NADPH as co-factor; a temperature optimum of 55-60° C. at pH 7.4; a pH optimum of 4.5-8.5 and substrate specificity on ?,?-unsatured ketones; a process for producing it from a microorganism and a process for producing levodione from ketoisophorone using such reductase.

Abstract: A process for producing an optical active &bgr;-amino alcohol, the method comprising the step of allowing at least one microorganism selected from the group consisting of microorganisms belonging to the genus Morganella and others, to act on an enantiomeric mixture of an &agr;-aminoketone or a salt thereof having the general formula (I): to produce an optical active &bgr;-amino alcohol with the desired optical activity having the general formula (II) described below in a high yield as well as in a highly selective manner:

Abstract: A protein, which is an aminoketone asymmetric reductase, having an effect of producing d-pseudoephedrine by acting on l-2-methylaminopropiophenone, and having the following physiochemical properties:

Abstract: The present invention discloses a process for efficiently producing, on an industrial scale, optically active (R)-2-chloro-1-(3′-chlorophenyl)ethanol which is useful as a raw material for the synthesis of medicines, agricultural chemicals, etc.

Abstract: A process for producing an optical active &bgr;-amino alcohol, the method comprising the step of allowing at least one microorganism selected from the group consisting of microorganisms belonging to the genus Morganella and others, to act on an enantiomeric mixture of an &agr;-aminoketone or a salt thereof having the general formula (I): 1

Abstract: An enzyme having carbonyl reduction activity of reducing a carbonyl compound asymmetrically to produce an optically active alcohol, a DNA coding the enzyme, a plasmid having the DNA, a transformant which is a cell transformed with the plasmid, and a production method of an optically active alcohol using the enzyme and/or the transformed cell are provided.

Abstract: An enzyme having carbonyl reduction activity of reducing a carbonyl compound asymmetrically to produce an optically active alcohol, a DNA coding the enzyme, a plasmid having the DNA, a transformant which is a cell transformed with the plasmid, and a production method of an optically active alcohol using the enzyme and/or the transformed cell are provided.

Abstract: An enzyme having carbonyl reduction activity of reducing a carbonyl compound asymmetrically to produce an optically active alcohol, a DNA coding the enzyme, a plasmid having the DNA, a transformant which is a cell transformed with the plasmid, and a production method of an optically active alcohol using the enzyme and/or the transformed cell are provided.