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Appl. Environ. Microbiol., Jul 1996, 2303-2310, Vol 62, No. 7
K Kita, K Matsuzaki, T Hashimoto, H Yanase, N Kato, MC Chung, M Kataoka and S Shimizu
An NADPH-dependent aldehyde reductase (ALR) isolated from a red yeast,
Sporobolomyces salmonicolor, catalyzes the reduction of a variety of
carbonyl compounds. To investigate its primary structure, we cloned and
sequenced the cDNA coding for ALR. The aldehyde reductase gene (ALR)
comprises 969 bp and encodes a polypeptide of 35,232 Da. The deduced amino
acid sequence showed a high degree of similarity to other members of the
aldo-keto reductase superfamily. Analysis of the genomic DNA sequence
indicated that the ALR gene was interrupted by six introns (two in the 5'
noncoding region and four in the coding region). Southern hybridization
analysis of the genomic DNA from S. salmonicolor indicated that there was
one copy of the gene. The ALR gene was expressed in Escherichia coli under
the control of the tac promoter. The enzyme expressed in E. coli was
purified to homogeneity and showed the same catalytic properties as did the
enzyme from S. salmonicolor.
Copyright © 1996, American Society for Microbiology
Cloning of the aldehyde reductase gene from a red yeast, Sporobolomyces salmonicolor, and characterization of the gene and its product
Department of Biotechnology, Tottori University, Japan. kita @bio.tottori-u.ac.jp
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