Structures,mechanisms and inhibitors of undecaprenyl diphosphate synthase: A cis-prenyltransferase for bacterial peptidoglycan biosynthesis |
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| Institution: | 1. Department of Life Sciences, Ben Gurion University of the Negev, Beersheva 84105, Israel;2. Department of Biochemistry, Duke University Medical Center, Durham, NC 27710, USA;1. Laboratory of Food Chemistry, Wageningen University & Research, Bornse Weilanden 9, 6708 WG, Wageningen, Netherlands;2. Laboratory of Plant Physiology, Wageningen University & Research, Droevendaalsesteeg 1, 6708 PB, Wageningen, Netherlands;3. Wageningen Plant Research, Wageningen University & Research, Droevendaalsesteeg 1, 6708 PB, Wageningen, Netherlands |
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| Abstract: | Isoprenoids are an intensive group of compounds made from isopentenyl diphosphate (IPP), catalyzed by prenyltransferases such as farnesyl diphosphate (FPP) cyclases, squalene synthase, protein farnesyltransferases and geranylgeranyltransferases, aromatic prenyltransferases as well as a group of prenyltransferases (cis- and trans-types) catalyzing consecutive condensation reactions of FPP with specific numbers of IPP to generate linear products with designate chain lengths. These prenyltransferases play significant biological functions and some of them are drug targets. In this review, structures, mechanisms, and inhibitors of a cis-prenyltransferase, undecaprenyl diphosphate synthase (UPPS) that mediates bacterial peptidoglycan biosynthesis, are summarized for comparison with the most related trans-prenyltransferases and other prenyltransferases. |
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