Several bacteria and fungi are capable of growing either D(-)-, L(+)- or DL-mandelate as the sole source of carbon and energy. Mandelate dehydrogenases catalyse the first step in this process, the stereospecific oxidation of D(-)- or L(+)- mandelate to phenylglyoxalate. In some bacteria the Mandelate Dehydrogenases (MANDH) are NAD(P)+-independent, integral membrane proteins and requiring flavin as their prosthetic group.
The yeast Rhodotorula graminis was the first organisms which have both a dye-linked L(+)-mandelate dehydrogenase and NAD+-dependent D(-)- mandelate dehydrogenase.
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