Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 400, Issue 4, Pages 758-762Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2010.09.001
Keywords
Isoprenoid; Prenyltransferase; Reaction mechanism; Sequential; Concerted
Categories
Funding
- National Science Council of Taiwan
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Undecaprenyl pyrophosphate synthase (UPPS) is a cis-type prenyltransferases which catalyzes condensation reactions of farnesyl diphosphate (FPP) with eight isopentenyl pyrophosphate (IPP) units to generate C-55 product. In this study, we used two analogues of FPP, 2-fluoro-FPP and [1,1-H-2(2)]FPP, to probe the reaction mechanism of Escherichia coli UPPS. The reaction rate of 2-fluoro-FPP with IPP under single-turnover condition is similar to that of FPP, consistent with the mechanism without forming a farnesyl carbocation intermediate. Moreover, the deuterium secondary KIE of 0.985 +/- 0.022 measured for UPPS reaction using [1,1-2H2]FPP supports the associative transition state. Unlike the sequential mechanism used by trans-prenyltransferases, our data demonstrate E. coli UPPS utilizes the concerted mechanism. (C) 2010 Elsevier Inc. All rights reserved.
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