Molecular cloning and characterization of the alcohol dehydrogenase ADH1 gene of Candida utilis ATCC 9950.
The alcohol dehydrogenase gene (ADH1) of Candida utilis ATCC9950 was cloned and expressed in recombinant Escherichia coli. C. utilis ADH1 was obtained by PCR amplification of C. utilis genomic DNA using two degenerate primers. Amino acid sequence analysis of C. utilis ADH1 indicated that it contained a zinc-binding consensus region and a NAD(P)(+)-binding site, and lacked a mitochondrial targeting peptide. It has a 98 and 73% identity with ADH1s of C. albicans and Saccharomyces cerevisiae, respectively. Amino acid sequence analysis and enzyme characterization with various aliphatic and branched alcohols suggested that C. utilis ADH1 might be a primary alcohol dehydrogenase existing in the cytoplasm and requiring zinc ion and NAD(P)(+) for reaction.
Park
Yong-Cheol
YC
Department of Biochemistry and Cell Biology, Rice University, 6100 Main street, Houston, TX 77005, USA. gbennett@bioc.rice.edu
Yun
Na-Rae
NR
San
Ka-Yiu
KY
Bennett
George N
GN
D000426:Alcohol Dehydrogenase / Q000737:chemistry* / Q000235:genetics*; D000595:Amino Acid Sequence; D002175:Candida / Q000201:enzymology* / Q000235:genetics; D003001:Cloning, Molecular; D004926:Escherichia coli / Q000235:genetics; D005800:Genes, Fungal; D008969:Molecular Sequence Data; D009249:NADP / Q000737:chemistry; D017386:Sequence Homology, Amino Acid; D015032:Zinc / Q000737:chemistry
D009249:NADP; D000426:Alcohol Dehydrogenase; D015032:Zinc