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Kinetic mechanism and the rate-limiting step of Plasmodium vivax serine hydroxymethyltransferase
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Metadata
Document Title
Kinetic mechanism and the rate-limiting step of Plasmodium vivax serine hydroxymethyltransferase
Author
Maenpuen S.,Amornwatcharapong W.,Krasatong P.,Sucharitakul J.,Palfey B.A.,Yuthavong Y.,Chitnumsub P.,Leartsakulpanich U.,Chaiyen P.
Name from Authors Collection
Affiliations
Department of Biochemistry and Center of Excellence in Protein Structure and Function, Faculty of Science, Mahidol University, Rama 6 Rd., Ratchatewi, Bangkok, 10400, Thailand; Department of Biochemistry, Faculty of Science, Burapha University, Chonburi, 20131, Thailand; Department of Biochemistry, Faculty of Dentistry, Chulalongkorn University, Bangkok, 10300, Thailand; Department of Biological Chemistry, University of Michigan, Ann Arbor, MI 48109, United States; National Center for Genetic Engineering and Biotechnology, National Science and Technology Development Agency, 113 Paholyothin Rd., Pathumthani, 12120, Thailand
Type
Article
Source Title
Journal of Biological Chemistry
ISSN
00219258
Year
2015
Volume
290
Issue
13
Open Access
All Open Access, Hybrid Gold, Green
Publisher
American Society for Biochemistry and Molecular Biology Inc.
DOI
10.1074/jbc.M114.612275
Abstract
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. © 2015 by The American Society for Biochemistry and Molecular Biology, Inc.
Industrial Classification
Knowledge Taxonomy Level 1
Knowledge Taxonomy Level 2
Knowledge Taxonomy Level 3
License
CC BY-NC-ND
Rights
Elsevier B.V.
Publication Source
Scopus