TAILIEUCHUNG - Báo cáo khoa học: Serine hydroxymethyltransferase from Plasmodium vivax is different in substrate specificity from its homologues

The putative gene ofPlasmodium vivaxserine hydroxymethyltransferase (PvSHMT; EC ) was cloned and expressed in Escherichia coli. The purified enzyme was shown to be a dimeric protein with a monomeric molecular mass of 49 kDa. PvSHMT has a maximum absorption peak at 422 nm with a molar absorption coefficient of 6370m )1 Æcm )1 . The Kd for binding of the enzyme and pyridoxal-5-phosphate was ± . | ỊFEBS Journal Serine hydroxymethyltransferase from Plasmodium vivax is different in substrate specificity from its homologues Kittipat Sopitthummakhun1 Somchart Maenpuen1 z Yongyuth Yuthavong2 Ubolsree Leartsakulpanich2 and Pimchai Chaiyen1 1 Department of Biochemistry and Center for Excellence in Protein Structure and Function Faculty of Science MahidolUniversity Bangkok Thailand 2 NationalCenter for Genetic Engineering and Biotechnology NationalScience and Technology Development Agency Pathumthani Thailand Keywords deoxythymidylate cycle folate metabolism Plasmodium vivax pyridoxal-5-phosphate serine hydroxymethyltransferase Correspondence P. Chaiyen Department of Biochemistry and Center for Excellence in Protein Structure and Function Faculty of Science Mahidol University Rama 6 Road Bangkok 10400 Thailand Fax 66 2354 7174 Tel 66 2201 5596 E-mail scpcy@ U. Leartsakulpanich National center for Genetic Engineering and Biotechnology National Science and Technology Development Agency 113 Paholyothin Road Pathumthani 12120 Thailand Fax 66 2564 6707 Tel 66 2564 6700 E-mail ubolsree@ Website http chaiyen_p These authors contributed equally to this work Received 9 February 2009 revised 17 April 2009 accepted 22 May 2009 doi The putative gene of Plasmodium vivax serine hydroxymethyltransferase PvSHMT EC was cloned and expressed in Escherichia coli. The purified enzyme was shown to be a dimeric protein with a monomeric molecular mass of 49 kDa. PvSHMT has a maximum absorption peak at 422 nm with a molar absorption coefficient of 6370 M-1-cm-1. The Kd for binding of the enzyme and pyridoxal-5-phosphate was M. An alternative assay for measuring the tetrahydrofolate-dependent SHMT activity based on the coupled reaction with 5 10-methylenetetrahydrofolate reductase EC from E. coli was developed. PvSHMT uses a ternary-complex mechanism with a kcat value of s-1 .

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