Rosli Md.Illias
Department of Bioprocess Engineering, Faculty of Chemical Engineering and Natural Resources
Engineering, Universiti Teknologi Malaysia, 81300, Skudai, Johor Malaysia
Graem A. Reid
Institute of Cell and Molecular Biology, University of Edinburgh, Maryland Road,
Edinburgh EH9 3JR, Scotland, UK
Stephen K. Chapman
Department of Chemistry, University of Edinburgh, West Mains Road, Edinburgh EH9 3JJ, Scotland, UK
Charles A. Fewson
Institute of Medical and life Sciences, University of Glasgow, Glasgow G 12 8QQ
John S. Miles
Institute of Medical and life Sciences, University of Glasgow, Glasgow G 12 8QQ
ABSTRACT
The yeast Rhodotorula graminis can use D, L-mandelate as a source of carbon and energy. We have isolated the gene encoding D-mandelate dehydrogenase, one of the two enzymes that stereospecifically catalyze the first step in mandelate degradation. The sequences of the genomic DNA and a cDNA prepared by RT-PCR revealed the presence of three short introns within the coding region. The predicted amino acid sequence of D-mandelate dehydrogenase is 27-33% identical to other members of a large family of NAD+-dependent 2-hydroacid dehydrogenase from a broad spectrum of bacteria and eukaryotes and it has a wide range of substrate specificities.
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How to cite this article
Rosli Md.Illias, Graem A. Reid, Stephen K. Chapman, Charles A. Fewson and John S. Miles, 2002. Molecular Cloning and Sequencing of D-mandelate Dehydrogenase Gene from Rhodotorula graminis. Pakistan Journal of Biological Sciences, 5: 871-877.
DOI: 10.3923/pjbs.2002.871.877
URL: https://scialert.net/abstract/?doi=pjbs.2002.871.877
DOI: 10.3923/pjbs.2002.871.877
URL: https://scialert.net/abstract/?doi=pjbs.2002.871.877
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