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In enzymology, an undecaprenyl-diphosphatase (EC 3.6.1.27) is an enzyme that catalyzes the chemical reaction

undecaprenyl diphosphate + H₂O ${\displaystyle \rightleftharpoons }$ undecaprenyl phosphate + phosphate

Thus, the two substrates of this enzyme are undecaprenyl diphosphate and H₂O, whereas its two products are undecaprenyl phosphate and phosphate. The enzymatic activity is enhanced by divalent cations, particularly Ca.

In many bacteria, this enzyme is a membrane protein that participates in peptidoglycan biosynthesis. The enzyme has been implicated in conferring resistance to the antibiotic bacitracin.

Nomenclature

This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides in phosphorus-containing anhydrides. The systematic name of this enzyme class is undecaprenyl-diphosphate phosphohydrolase. Other names in common use include Undecaprenyl-pyrophosphate phosphatase (Uppp), UPP phosphatase, BacA, C55-isoprenyl diphosphatase, C55-isoprenyl pyrophosphatase, and isoprenyl pyrophosphatase.

Note: The enzyme Uppp/BacA (EC 3.6.1.27) has occasionally been incorrectly termed an "undecaprenol kinase". However, that name should be reserved for a distinct enzyme (EC 2.7.1.66), which catalyses the addition of a phosphate group from ATP to undecaprenol (C55-isoprenyl alcohol).

Structure

X-ray crystal structures of the membrane-form of the enzyme from E. coli are available (PDB IDs: 5OON, 6CB2).

References

1. Chalker AF, Ingraham KA, Lunsford RD, Bryant AP, Bryant J, Wallis NG, Broskey JP, Pearson SC, Holmes DJ (July 2000). "The bacA gene, which determines bacitracin susceptibility in Streptococcus pneumoniae and Staphylococcus aureus, is also required for virulence". Microbiology. 146 (Pt 7): 1547–53. doi:10.1099/00221287-146-7-1547. PMID 10878119.
2. "undecaprenyl diphosphate (YMDB00637) - Yeast Metabolome Database". www.ymdb.ca. Retrieved 2023-09-07.
3. El Ghachi M, Bouhss A, Blanot D, Mengin-Lecreulx D (July 2004). "The bacA gene of Escherichia coli encodes an undecaprenyl pyrophosphate phosphatase activity". The Journal of Biological Chemistry. 279 (29): 30106–13. doi:10.1074/jbc.M401701200. PMID 15138271.
4. El Ghachi M, Howe N, Huang CY, Olieric V, Warshamanage R, Touzé T, Weichert D, Stansfeld PJ, Wang M, Kerff F, Caffrey M (March 2018). "Crystal structure of undecaprenyl-pyrophosphate phosphatase and its role in peptidoglycan biosynthesis". Nature Communications. 9 (1): 1078. doi:10.1038/s41467-018-03477-5. PMC 5852022. PMID 29540682.
5. Workman SD, Worrall LJ, Strynadka NC (March 2018). "Crystal structure of an intramembranal phosphatase central to bacterial cell-wall peptidoglycan biosynthesis and lipid recycling". Nature Communications. 9 (1): 1159. doi:10.1038/s41467-018-03547-8. PMC 5861054. PMID 29559664.
6. "5OON - Structure of Undecaprenyl-Pyrophosphate Phosphatase, BacA". RCSB Protein Data Bank.
7. "6CB2 - Crystal structure of Escherichia coli UppP". RCSB Protein Data Bank.

Further reading

• Goldman R, Strominger JL (August 1972). "Purification and properties of C 55 -isoprenylpyrophosphate phosphatase from Micrococcus lysodeikticus". The Journal of Biological Chemistry. 247 (16): 5116–22. PMID 4341539.

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