| Summary: | 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.
|
|---|