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- W2488112774 abstract "We report the first structure of heptaprenyl diphosphate synthase from Staphylococcus aureus (SaHepPPS), together with an investigation of its mechanism of action and inhibition. The protein is involved in the formation of menaquinone, a key electron transporter in many bacteria, including pathogens. SaHepPPS consists of a catalytic subunit (SaHepPPS-2) having two DDXXD motifs and a regulatory subunit (SaHepPPS-1) that lacks these motifs. High concentrations of the substrates, isopentenyl diphosphate and farnesyl diphosphate, inhibit the enzyme, which is also potently inhibited by bisphosphonates. The most active inhibitors (Ki ∼200 nm) were N-alkyl analogues of zoledronate containing ∼C6 alkyl side chains. They were modestly active against S. aureus cell growth, and growth inhibition was partially rescued by the addition of menaquinone-7. Because SaHepPPS is essential for S. aureus cell growth, its structure is of interest in the context of the development of menaquinone biosynthesis inhibitors as potential antibiotic leads." @default.
- W2488112774 created "2016-08-23" @default.
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- W2488112774 date "2016-07-26" @default.
- W2488112774 modified "2023-10-16" @default.
- W2488112774 title "Structure, Function, and Inhibition of<i>Staphylococcus aureus</i>Heptaprenyl Diphosphate Synthase" @default.
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- W2488112774 doi "https://doi.org/10.1002/cmdc.201600311" @default.
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