The serine hydroxymethyltransferase of Plasmodium lophurae.
Plasmodium lophurae serine hydroxymethyltransferase (EC 2.1.2.1) was partially purified and characterized by (NH4)2SO4 fractionation and chromatography on Sephadex G-100. The enzyme, precipitated by 3.0.3.3 M (NH4)2SO4, had a molecular weight of 68,300 as estimated by exclusion chromatography on G-100. The pH optimum of the enzyme was 6.8-7.6 in sodium phosphate-citrate buffer. Citrate stabilized the enzyme during storage in phosphate buffer at 4 C. The Km was 4.3 X 10(-3) M for L-serine and 2.5 X 10(-4) M for tetrahydrofolate.
D000645:Ammonium Sulfate / Q000494:pharmacology; D000818:Animals; D002951:Citrates / Q000494:pharmacology; D004372:Ducks; D012696:Glycine Hydroxymethyltransferase / Q000302:isolation & purification*; D006863:Hydrogen-Ion Concentration; D008970:Molecular Weight; D010961:Plasmodium / Q000201:enzymology*; D014166:Transferases / Q000302:isolation & purification*
D002951:Citrates; D014166:Transferases; D012696:Glycine Hydroxymethyltransferase; D000645:Ammonium Sulfate