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
|
PDF
505kB |
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 |
ID Code: | 878 |
Deposited By: | Mohd. Nazir Md. Basri |
Deposited On: | 22 Feb 2007 08:36 |
Last Modified: | 01 Nov 2017 04:17 |
Repository Staff Only: item control page