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Perbandingan struktur primer L(+)–mendalate dehydrogenase (L–MDH) daripada yis Rhodotorula graminis dengan protein lain di dalam bank data protein menunjukkan persamaan di antara protein ini dengan kumpulan enzim L–2–hidroksiasid dehidrogenase. LMDH daripada R. graminis mempamerkan kesamaan antara 26–42% kepada L–lactate dehidrogenase daripada Sacchomoryces cerevisiae, L–lactate dehidrogenase daripada Hansenula anomala, glikolat oksida daripada bayam, L–laktat dehidrogenase daripada Escherichia coli, LMDH daripada Psedomonas putida dan laktat–2 monooksigenase daripada Mycobakterium smegmatis. Asid amino yang penting secara strukturnya bagi LMDH diramalkan secara perbandingan dengan bahagian penting domain sitokram dan domain perlekatan FMN yang diperoleh daripada struktur tiga dimensi L–laktat dehidrogenase daripada Sacchoromyces cerevisiae. Kata kunci: L-MDH; Rhodotorula gramisis; L(+)-mandalate dehydrogenase; asid amino,flavocytochrome b2 A comparison of the primary structure or 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 dehyrogenase from Sacchoromyces cerevisiae. Key words: L-MDH; Rhodotorula graminis; L-mandelate dehydrogenase; amino acid;flavocytochrome b2