S-Adenosylhomocysteine hydrolase activity in Trichomonas vaginalis and other trichomonads.

S-Adenosylhomocysteine hydrolase has been detected in crude homogenates of Trichomonas vaginalis, Tritrichomonas foetus and Trichomitus batrachorum at activities of 14, 1.2 and 3.3 nmol min-1 mg-1 protein, respectively. The enzyme from T. vaginalis was found to be soluble with pH optimum of 8.0 and apparent Km values for adenosine and homocysteine of 100 and 155 microM, respectively. Ara A was shown to inhibit the T. vaginalis enzyme but only at relatively high concentration (I50 100 microM), whereas sinefungin and 2'-deoxyadenosine had only small inhibitory effects. EDTA (I50 6 mM) and various divalent cations also inhibited the enzyme from T. vaginalis.