Undecaprenyl pyrophosphate synthase

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== Function ==
== Function ==
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'''Undecaprenyl pyrophosphate synthase''' (UPP) catalyzes the consecutive condensation of farnesyl pyrophosphate (FPP) with 8 molecules of isopentenyl pyrophosphate (IPP) to produce undecaprenyl pyrophosphate. Undecaprenyl pyrophosphate serves as a lipid carrier for peptidoglycan synthesis of bacterial cell wall<ref>PMID:15788389</ref>. Bisphosphonate drugs are UPP inhibitors.
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'''Undecaprenyl pyrophosphate synthase''' (UPP) catalyzes the consecutive condensation of farnesyl pyrophosphate (FPP) with 8 molecules of isopentenyl pyrophosphate (IPP) to produce undecaprenyl pyrophosphate. Undecaprenyl pyrophosphate serves as a lipid carrier for peptidoglycan synthesis of bacterial cell wall. Bisphosphonate drugs are UPP inhibitors.
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== Disease ==
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== Relevance ==
== Relevance ==
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UPP inhibitors are investigated as potential antibacterials<ref>PMID:26718796</ref>.
== Structural highlights ==
== Structural highlights ==
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The active site of UPP contains an octahedrally coordinated Mg+2 ion bound to the pyrophosphate group of isopentenyl pyrophosphate<ref>PMID:15788389</ref>.
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Revision as of 11:05, 5 December 2016

Structure of E. coli UPP complex with isopentenyl pyrophosphate, phosphate and Mg+2 (green) (PDB code 1x07).

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3D structures of undecaprenyl pyrophosphate synthase

Updated on 05-December-2016

References

  1. Guo RT, Ko TP, Chen AP, Kuo CJ, Wang AH, Liang PH. Crystal structures of undecaprenyl pyrophosphate synthase in complex with magnesium, isopentenyl pyrophosphate, and farnesyl thiopyrophosphate: roles of the metal ion and conserved residues in catalysis. J Biol Chem. 2005 May 27;280(21):20762-74. Epub 2005 Mar 23. PMID:15788389 doi:10.1074/jbc.M502121200
  2. Jukic M, Rozman K, Gobec S. Recent Advances in the Development of Undecaprenyl Pyrophosphate Synthase Inhibitors as Potential Antibacterials. Curr Med Chem. 2016;23(5):464-82. PMID:26718796
  3. Guo RT, Ko TP, Chen AP, Kuo CJ, Wang AH, Liang PH. Crystal structures of undecaprenyl pyrophosphate synthase in complex with magnesium, isopentenyl pyrophosphate, and farnesyl thiopyrophosphate: roles of the metal ion and conserved residues in catalysis. J Biol Chem. 2005 May 27;280(21):20762-74. Epub 2005 Mar 23. PMID:15788389 doi:10.1074/jbc.M502121200

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