Publication:
Kinetic mechanism and the rate-limiting step of Plasmodium vivax serine hydroxymethyltransferase

dc.contributor.authorSomchart Maenpuenen_US
dc.contributor.authorWatcharee Amornwatcharapongen_US
dc.contributor.authorPasupat Krasatongen_US
dc.contributor.authorJeerus Sucharitakulen_US
dc.contributor.authorBruce A. Palfeyen_US
dc.contributor.authorYongyuth Yuthavongen_US
dc.contributor.authorPenchit Chitnumsuben_US
dc.contributor.authorUbolsree Leartsakulpanichen_US
dc.contributor.authorPimchai Chaiyenen_US
dc.contributor.otherMahidol Universityen_US
dc.contributor.otherBurapha Universityen_US
dc.contributor.otherChulalongkorn Universityen_US
dc.contributor.otherUniversity of Michigan, Ann Arboren_US
dc.contributor.otherThailand National Center for Genetic Engineering and Biotechnologyen_US
dc.date.accessioned2018-11-23T09:44:44Z
dc.date.available2018-11-23T09:44:44Z
dc.date.issued2015-03-27en_US
dc.description.abstract© 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.en_US
dc.identifier.citationJournal of Biological Chemistry. Vol.290, No.13 (2015), 8656-8665en_US
dc.identifier.doi10.1074/jbc.M114.612275en_US
dc.identifier.issn1083351Xen_US
dc.identifier.issn00219258en_US
dc.identifier.other2-s2.0-84925796253en_US
dc.identifier.urihttps://repository.li.mahidol.ac.th/handle/20.500.14594/35482
dc.rightsMahidol Universityen_US
dc.rights.holderSCOPUSen_US
dc.source.urihttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=84925796253&origin=inwarden_US
dc.subjectBiochemistry, Genetics and Molecular Biologyen_US
dc.titleKinetic mechanism and the rate-limiting step of Plasmodium vivax serine hydroxymethyltransferaseen_US
dc.typeArticleen_US
dspace.entity.typePublication
mu.datasource.scopushttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=84925796253&origin=inwarden_US

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