Cloning overexpression, and mutagenesis of the Sporobolomyces salmonicolor AKU4429 gene encoding a new aldehyde reductase, which catalyzes the stereoselective reduction of ethyl 4-chloro-3-oxobutanoate to ethyl (S)-4-chloro-3-hydroxybutanoate
Article Abstract:
The 1,032 bp-long yeast, Sporobolomyces salmonicolor AKU4429, gene that encodes a new aldehyde reductase is discussed. The NADPH-dependent reductase (ARII) catalyzes stereoselective reduction of ethyl 4-chloro-3-oxobutanoate to ethyl (S)-4-chloro-3-hydroxybutanoate. A cDNA clone of the gene has been cloned and analyzed to compare catalytic mechanisms of ARI and ARII and learn about the molecular basis of the stereospecific reduction of 4-COBE. The gene is interrupted by four introns and encodes a 37,315-Da polypeptide. The amino acid sequence has considerable similarity to sequences of members of the mammalian 3beta-hydroxysteroid dehydrogenase-plant dehydroflavonol 4-reductase superfamily.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1999
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Cloning of the aldehyde reductase gene from a red yeast, Sporobolomyces salmonicolor, and characterization of the gene and its product
Article Abstract:
The cDNA encoding aldehyde reductase (ALR) in the red yeast Sporobolomyces salmonicolor has been cloned using oligonucleotide probes. The ALR gene contains an open reading frame of 323 residues with two introns in the noncoding sequence and four introns in the coding sequence. The encoded polypeptide has a molecular mass of 35,232 Da and its amino acid sequence is similar to that of other aldo-keto reductases, especially in the N-terminal region. An Escherichia coli strain expressing the ALR gene produces an enzyme structurally and catalytically similar to the yeast ALR.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1996
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Properties of poly(3-hydroxybutyrate) depolymerase from a marine bacterium, Alcaligenes faecalis AE122
Article Abstract:
The enzyme poly(3-hydroxybutyrate)(PHB) depolymerase isolated from the bacteria Alcaligenes faecalis is probably a monomeric protein with a high molecular mass. The bacteria uses PHB as its only carbon source and the optimal conditions for PHB polymerase are a pH of 9.0 and a temperature of 55 degree temperature. The activity of this enzyme increases by the addition of salts such as NaCl, MgCl2 and CaCl2. The products of the PHB polymerase are biodegradable plastics.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1995
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