EC 2.5.1.31 - ditrans,polycis-undecaprenyl-diphosphate synthase [(2E,6E)-farnesyl-diphosphate specific]

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IntEnz Enzyme Nomenclature
EC 2.5.1.31

Names

Accepted name:
ditrans,polycis-undecaprenyl-diphosphate synthase [(2E,6E)-farnesyl-diphosphate specific]
Other names:
ditrans,polycis-undecaprenyl-diphosphate synthase
UPP synthetase
bactoprenyl-diphosphate synthase
undecaprenyl diphosphate synthetase
undecaprenyl pyrophosphate synthetase
undecaprenyl-diphosphate synthase
undecaprenyl pyrophosphate synthase
ditrans,polycis-undecaprenylcistransferase
Systematic name:
(2E,6E)-farnesyl-diphosphate:isopentenyl-diphosphate cistransferase (adding 8 isopentenyl units)

Reaction

Comments:

Undecaprenyl pyrophosphate synthase catalyses the consecutive condensation reactions of a farnesyl diphosphate with eight isopentenyl diphosphates, in which new cis-double bonds are formed, to generate undecaprenyl diphosphate that serves as a lipid carrier for peptidoglycan synthesis of bacterial cell wall [3].

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , DIAGRAM , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC00817
Structural data: CSA , EC2PDB
Gene Ontology: GO:0008834
CAS Registry Number: 52350-87-5
UniProtKB/Swiss-Prot: (43) [show] [UniProt]

References

  1. Muth, J.D. and Allen, C.M.
    Undecaprenyl pyrophosphate synthetase from Lactobacillus plantarum: a dimeric protein.
    Arch. Biochem. Biophys. 230: 49-60 (1984). [PMID: 6712246]
  2. Takahashi, I. and Ogura, K.
    Prenyltransferases of Bacillus subtilis: undecaprenyl pyrophosphate synthetase and geranylgeranyl pyrophosphate synthetase.
    J. Biochem. 92: 1527-1537 (1982). [PMID: 6818223]
  3. Guo, R. T., Ko, T. P., Chen, A. P., Kuo, C. J., Wang, A. H., Liang, P. H.
    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. 280: 20762-20774 (2005). [PMID: 15788389]
  4. Ko, T. P., Chen, Y. K., Robinson, H., Tsai, P. C., Gao, Y. G., Chen, A. P., Wang, A. H., Liang, P. H.
    Mechanism of product chain length determination and the role of a flexible loop in Escherichia coli undecaprenyl-pyrophosphate synthase catalysis.
    J. Biol. Chem. 276: 47474-47482 (2001). [PMID: 11581264]
  5. Fujikura, K., Zhang, Y. W., Fujihashi, M., Miki, K., Koyama, T.
    Mutational analysis of allylic substrate binding site of Micrococcus luteus B-P 26 undecaprenyl diphosphate synthase.
    Biochemistry 42: 4035-4041 (2003). [PMID: 12680756]
  6. Fujihashi, M., Zhang, Y. W., Higuchi, Y., Li, X. Y., Koyama, T., Miki, K.
    Crystal structure of cis-prenyl chain elongating enzyme, undecaprenyl diphosphate synthase.
    Proc. Natl. Acad. Sci. USA 98: 4337-4342 (2001). [PMID: 11287651]
  7. Pan, J. J., Chiou, S. T., Liang, P. H.
    Product distribution and pre-steady-state kinetic analysis of Escherichia coli undecaprenyl pyrophosphate synthase reaction.
    Biochemistry 39: 10936-10942 (2000). [PMID: 10978182]
  8. Kharel, Y., Zhang, Y. W., Fujihashi, M., Miki, K., Koyama, T., Khare, Y.
    Significance of highly conserved aromatic residues in Micrococcus luteus B-P 26 undecaprenyl diphosphate synthase.
    J. Biochem. 134: 819-826 (2003). [PMID: 14769870]

[EC 2.5.1.31 created 1984, modified 2010, modified 2011]