Molecular Cloning and Sequencing of D-mandelate Dehydrogenase Gene from Rhodotorula graminis
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.
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.
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