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• W1974133262 endingPage "9050" @default.
• W1974133262 startingPage "9040" @default.
• W1974133262 abstract "Folylpoly-gamma-glutamate synthetase (FPGS, EC 6.3.2.17) is an ATP-dependent ligase that catalyzes formation of poly-gamma-glutamate derivatives of reduced folates and antifolates such as methotrexate and 5,10-dideaza-5,6,7,8-tetrahydrofolate (DDAH 4PteGlu 1). While the chemical mechanism of the reaction catalyzed by FPGS is known, it is unknown whether single or multiple glutamate residues are added following each folate binding event. A very sensitive high-performance liquid chromatography method has been used to analyze the multiple ligation reactions onto radiolabeled DDAH 4PteGlu 1 catalyzed by FPGS to distinguish between distributive or processive mechanisms of catalysis. Reaction time courses, substrate trapping, and pulse-chase experiments were used to assess folate release during multiple glutamate additions. Together, the results of these experiments indicate that hFPGS can catalyze the processive addition of approximately four glutamate residues to DDAH 4PteGlu 1. The degree of processivity was determined to be dependent on the concentration of the folate substrate, thus suggesting a mechanism for the regulation of folate polyglutamate synthesis in cells." @default.
• W1974133262 created "2016-06-24" @default.
• W1974133262 creator A5032651935 @default.
• W1974133262 creator A5049873425 @default.
• W1974133262 creator A5085925780 @default.
• W1974133262 date "2008-08-01" @default.
• W1974133262 modified "2023-09-26" @default.
• W1974133262 title "Concentration-Dependent Processivity of Multiple Glutamate Ligations Catalyzed by Folylpoly-γ-glutamate Synthetase" @default.
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• W1974133262 doi "https://doi.org/10.1021/bi800406w" @default.
• W1974133262 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2805413" @default.
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• W1974133262 hasPublicationYear "2008" @default.
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