Comparison Of The Amino Acid Sequence Of L-Mandelate Dehydrogenase From Rhodotorula Graminis With Other L-2-Hydroxyacid Dehydrogenase Enzyme And Its Primary Structure Prediction

• Main Authors: Md. Illias, Rosli, Reid, Graeme A., A. Wahab, Nadzarah
• Format: Article
• Language: English
• Published: Penerbit UTM Press 2001
• Subjects: TP Chemical technology
• Online Access: http://eprints.utm.my/id/eprint/878/1/JT34C4.pdf; http://eprints.utm.my/id/eprint/878/; http://www.penerbit.utm.my/onlinejournal/34/C/JT34C4.pdf

A comparison of the primary structure for L-mandelate dehydrogenase (L-MDH) from Rhodotorula graminis with other proteins from the protein databank suggests that there is similarity between this protein and L-2-hydroxyacid dehydrogenase enzymes. R. graminis LMDH exhibits 26–42% identity to L-lactate dehydrogenase from Saccharomyces cerevisiae, L-lactate dehydrogenase from Hansenula anomala, glycolate oxidase from spinach, L-lactate dehydrogenase from Escherichia coli, L-mandelate dehydrogenase from Pseudomonas putida and lactate-2-monooxygenase from Mycobacterium smegmatis. Structurally conserved amino acids are predicted from LMDH sequences corresponding to important regions of the cytochrome and FMN-binding domain defined from the known three-dimensional structure of the L-lactate dehydrogenase from Saccharomyces cerevisiae.