Undecaprenyl pyrophosphate synthase: Difference between revisions

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== Function ==
== Function ==
 
'''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.
'''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.
 
== Disease ==


== Relevance ==
== Relevance ==
UPP inhibitors are investigated as potential antibacterials<ref>PMID:26718796</ref>.


== Structural highlights ==
== Structural highlights ==
The active site of UPP contains an octahedrally coordinated Mg+2 ion bound to the pyrophosphate group of isopentenyl pyrophosphate<ref>PMID:15788389</ref>.
</StructureSection>
</StructureSection>



Revision as of 14:05, 5 December 2016


Function

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[1]. Bisphosphonate drugs are UPP inhibitors.

Relevance

UPP inhibitors are investigated as potential antibacterials[2].

Structural highlights

The active site of UPP contains an octahedrally coordinated Mg+2 ion bound to the pyrophosphate group of isopentenyl pyrophosphate[3].

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

Drag the structure with the mouse to rotate

3D structures of undecaprenyl pyrophosphate synthase3D structures of undecaprenyl pyrophosphate synthase

Updated on 05-December-2016

ReferencesReferences

  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

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky