Serine hydroxymethyltransferase activity in Trypanosoma cruzi, Trypanosoma rangeli and American Leishmania spp.
Serine hydroxymethyltransferase (SHMT) was studied in several American trypanosomatids, Trypanosoma cruzi epimastigotes displaying, in contrast with T. rangeli, high enzymatic activity. Several Leishmania spp. members, including L. braziliensis, L. mexicana and L. garnhami promastigotes, under identical assay conditions, showed low enzymatic activity. The T. cruzi and leishmanial enzymes presented several different kinetic properties, and thus apparent Km for THF was 0.30 mM for the trypanosomal SHMT vs 0.60 mM for the leishmanial enzyme, while the apparent Km for serine was 0.40 mM for trypanosomal SHMT vs 0.15 mM for leishmanial enzyme. There were significant variations in the specific activity of SHMT between the several different trypanosomatids strains studied, but the meaning of these results is not clear because they showed no correlation either with taxonomy or infectivity.
D000818:Animals; D012696:Glycine Hydroxymethyltransferase / Q000378:metabolism*; D007700:Kinetics; D007891:Leishmania / Q000201:enzymology*; D013045:Species Specificity; D014166:Transferases / Q000378:metabolism*; D014345:Trypanosoma / Q000201:enzymology*; D014349:Trypanosoma cruzi / Q000201:enzymology*
D014166:Transferases; D012696:Glycine Hydroxymethyltransferase