oxidation of lactate to pyruvate is similar to the reaction i ask about. However,it is still a possibility, i wonder if there are more certain answers or literatures to prove it.
It looks like the lactate dehydrogenases from 2 or more species ( P falciparum and Lactobacillus helveticus) can utilize the phenyl substituted substrate. One reference for the Lactobacillus case is attached. For future reference, you can always consult the BRENDA enzyme catalog (http://brenda-enzymes.info/index.php4) for information about substrate specificities or inhibition. There is a lot of information available on many systems, along with links to the primary literature. Cheers-Kevin
It really depends what LDHs are available to you. Even our own 3 (human) 'LDH' genes encode three enzymes of quite distinct ranges of specificity and kinetic properties. Of those three, it is the least well known one, LDH-X, which is confined to testis and sperm, that would give you the highest rates with a bigger substrate like phenyllactate. As Kevin Mccusker says, bacterial LDHs might be a more accessible source!