Undecaprenyl pyrophosphate synthase: Difference between revisions

Revision as of 15:06, 10 October 2019

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 of UPP (water molecules are shown as red spheres) contains an ^[3].

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 synthase3D structures of undecaprenyl pyrophosphate synthase

Updated on 10-October-2019

ReferencesReferences

↑ 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
↑ 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
↑ 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

[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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 == Structural highlights ==
-The <scene name='59/591995/Cv/3'>active site</scene> of UPP contains an <scene name='59/591995/Cv/1'>octahedrally coordinated Mg+2 ion bound to the pyrophosphate group of isopentenyl pyrophosphate</scene><ref>PMID:15788389</ref>. Water molecules shown as red spheres.
+The <scene name='59/591995/Cv/5'>active site</scene> of UPP (water molecules are shown as red spheres) contains an <scene name='59/591995/Cv/6'>octahedrally coordinated Mg+2 ion bound to the pyrophosphate group of isopentenyl pyrophosphate</scene><ref>PMID:15788389</ref>.
 </StructureSection>