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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

Md. Illias, Rosli and Reid, Graeme A. and A. Wahab, Nadzarah (2001) 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. Jurnal Teknologi C (34C). pp. 25-34. ISSN 0127-9696

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Official URL: http://www.penerbit.utm.my/onlinejournal/34/C/JT34...

Abstract

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.

Item Type:Article
Uncontrolled Keywords:L-MDH, Rhodotorula graminis, L-mandelate dehydrogenase, amino acid, flavocytochrome b2
Subjects:T Technology > TP Chemical technology
Divisions:Chemical and Natural Resources Engineering (Formerly known)
ID Code:878
Deposited By: En Mohd. Nazir Md. Basri
Deposited On:22 Feb 2007 08:36
Last Modified:15 Oct 2010 04:33

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