Trichomonas species: homocysteine desulphurase and serine sulphydrase activities |
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| Authors: | K W Thong G H Coombs |
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| Institution: | 1. Department of Food Hygiene of Animal Origin, Faculty of Veterinary Medicine, University of Life Sciences in Lublin, Akademicka 12, 20-033 Lublin, Poland;2. Department of Preclinical Sciences and Infectious Diseases, Faculty of Veterinary Medicine and Animal Science, Poznań University of Life Sciences, Wołyńska 35, 60-637 Poznań, Poland;3. The Witold Stefański Institute of Parasitology, Polish Academy of Sciences, Twarda 51/55, 00-818 Warszawa, Poland;3. Department of Pharmacology, Vanderbilt University, Nashville, Tennessee 37232;4. Division of Surgery, Department of Medicine, Vanderbilt University Medical Center, Nashville, Tennessee 37232;5. Vanderbilt Center for Neuroscience Drug Discovery, Vanderbilt University, Nashville, Tennessee 37232;6. Vanderbilt Institute of Chemical Biology, Vanderbilt University, Nashville, Tennessee 37232;1. Department of Organ transplantation, The First Hospital of China Medical University, Shenyang 110001, China;2. Department of General Surgery, The First Hospital of Liaoning Medical University, Jinzhou 121000, China |
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| Abstract: | Homocysteine desulphurase (EC 4.4.1.2) and serine sulphydrase (EC 4.2.1.22) activities in various lines of Trichomonas vaginalis, both metronidazole resistant and sensitive, and other trichomonad species were assessed. T. vaginalis contained the highest homocysteine desulphurase and serine sulphydrase activities of all the species. Although the levels of the enzyme activity in T. vaginalis isolates differed, no correlation between the activities and sensitivity to metronidazole was apparent. T. vaginalis homocysteine desulphurase catalysed both the hydrolysis of homocysteine to hydrogen sulphide, ammonia, and 2-oxoacid, and an exchange reaction between homocysteine and 2-mercaptoethanol. Homocysteine desulphurase was detected as a single enzyme band on isoelectric focusing, whereas several isoenzymes of serine sulphydrase were found. There were large differences in serine sulphydrase isoenzyme patterns between T. vaginalis lines and between species. Several isoenzymes were amplified in cells grown with 10(-5) M DL-propargylglycine for 24 hr. T. vaginalis homocysteine desulphurase and serine sulphydrase activities were inhibited by bithionol, hexachlorophene, and dichlorophene. These compounds also inhibited growth in vitro of T. vaginalis at concentrations similar to those that inhibited the enzymes. |
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