Somchart MaenpuenWatcharee AmornwatcharapongPasupat KrasatongJeerus SucharitakulBruce A. PalfeyYongyuth YuthavongPenchit ChitnumsubUbolsree LeartsakulpanichPimchai ChaiyenMahidol UniversityBurapha UniversityChulalongkorn UniversityUniversity of Michigan, Ann ArborThailand National Center for Genetic Engineering and Biotechnology2018-11-232018-11-232015-03-27Journal of Biological Chemistry. Vol.290, No.13 (2015), 8656-86651083351X002192582-s2.0-84925796253https://repository.li.mahidol.ac.th/handle/20.500.14594/35482© 2015 by The American Society for Biochemistry and Molecular Biology, Inc. Background: Plasmodium vivax serine hydroxymethyltransferase (PvSHMT) catalyzes formation of glycine from L-serine and tetrahydrofolate. Results: Results indicate that PvSHMT can bind to either substrate first. The rate constant of glycine formation is similar to kcat. Conclusion: PvSHMT reaction occurs via a random-order mechanism and glycine formation is the rate-limiting step. Significance: The data are useful for future investigation on inhibition of SHMT for antimalarial drug development.Mahidol UniversityBiochemistry, Genetics and Molecular BiologyArticleSCOPUS10.1074/jbc.M114.612275