Threonine and serine dehydratase activity in the buffalo liver-fluke Fasciola indica.
Serine dehydratase was found to be five times more active than threonine dehydratase in the liver-fluke Fasciola indica. The latter was not affected by L-isoleucine. Optimum pH for both enzymes was found to be 9.0 in tris-universal buffer. Seven metallic ions tested did not accelerate the enzyme activity, but produced different effects on two enzymes. Two different enzymes probably exist for the two aminoacids, L-threonine and L-serine.
D000818:Animals; D005209:Fasciola / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D007532:Isoleucine / Q000494:pharmacology; D012695:L-Serine Dehydratase / Q000378:metabolism*; D008670:Metals / Q000494:pharmacology; D013913:Threonine Dehydratase / Q000378:metabolism*
D008670:Metals; D007532:Isoleucine; D012695:L-Serine Dehydratase; D013913:Threonine Dehydratase