Publication: Kinetic mechanism and the rate-limiting step of Plasmodium vivax serine hydroxymethyltransferase
1
Issued Date
2015-03-27
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ISSN
1083351X
00219258
00219258
Other identifier(s)
2-s2.0-84925796253
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Mahidol University
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SCOPUS
Bibliographic Citation
Journal of Biological Chemistry. Vol.290, No.13 (2015), 8656-8665
Suggested Citation
Somchart Maenpuen, Watcharee Amornwatcharapong, Pasupat Krasatong, Jeerus Sucharitakul, Bruce A. Palfey, Yongyuth Yuthavong, Penchit Chitnumsub, Ubolsree Leartsakulpanich, Pimchai Chaiyen Kinetic mechanism and the rate-limiting step of Plasmodium vivax serine hydroxymethyltransferase. Journal of Biological Chemistry. Vol.290, No.13 (2015), 8656-8665. doi:10.1074/jbc.M114.612275 Retrieved from: https://repository.li.mahidol.ac.th/handle/123456789/35482
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Title
Kinetic mechanism and the rate-limiting step of Plasmodium vivax serine hydroxymethyltransferase
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.