Undecaprenyl-diphosphatase explained
undecaprenyl-diphosphatase |
Ec Number: | 3.6.1.27 |
Cas Number: | 9077-80-9 |
Go Code: | 0050380 |
Bacitracin resistance protein |
Pfam: | PF02673 |
Interpro: | IPR003824 |
Opm Family: | 479 |
Opm Protein: | 5oon |
In enzymology, an undecaprenyl-diphosphatase is an enzyme that catalyzes the chemical reaction
undecaprenyl diphosphate + H2O
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 Ca2+.
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.[1]
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.[2]
Note: The enzyme Uppp/BacA (EC 3.6.1.27) has occasionally been incorrectly termed an "undecaprenol kinase".[3] 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[4] [5] are available (PDB IDs: 5OON,[6] 6CB2[7]).
Further reading
- Goldman R, Strominger JL . Purification and properties of C 55 -isoprenylpyrophosphate phosphatase from Micrococcus lysodeikticus . The Journal of Biological Chemistry . 247 . 16 . 5116–22 . August 1972 . 4341539 .
Notes and References
- Chalker AF, Ingraham KA, Lunsford RD, Bryant AP, Bryant J, Wallis NG, Broskey JP, Pearson SC, Holmes DJ . The bacA gene, which determines bacitracin susceptibility in Streptococcus pneumoniae and Staphylococcus aureus, is also required for virulence . Microbiology . 146 . Pt 7 . 1547–53 . July 2000 . 10878119 . 10.1099/00221287-146-7-1547 . free .
- Web site: undecaprenyl diphosphate (YMDB00637) - Yeast Metabolome Database . 2023-09-07 . www.ymdb.ca.
- El Ghachi M, Bouhss A, Blanot D, Mengin-Lecreulx D . The bacA gene of Escherichia coli encodes an undecaprenyl pyrophosphate phosphatase activity . The Journal of Biological Chemistry . 279 . 29 . 30106–13 . July 2004 . 15138271 . 10.1074/jbc.M401701200 . free .
- El Ghachi M, Howe N, Huang CY, Olieric V, Warshamanage R, Touzé T, Weichert D, Stansfeld PJ, Wang M, Kerff F, Caffrey M . Crystal structure of undecaprenyl-pyrophosphate phosphatase and its role in peptidoglycan biosynthesis . Nature Communications . 9 . 1 . 1078 . March 2018 . 29540682 . 5852022 . 10.1038/s41467-018-03477-5 .
- Workman SD, Worrall LJ, Strynadka NC . Crystal structure of an intramembranal phosphatase central to bacterial cell-wall peptidoglycan biosynthesis and lipid recycling . Nature Communications . 9 . 1 . 1159 . March 2018 . 29559664 . 5861054 . 10.1038/s41467-018-03547-8 .
- Web site: 5OON - Structure of Undecaprenyl-Pyrophosphate Phosphatase, BacA. RCSB Protein Data Bank.
- Web site: 6CB2 - Crystal structure of Escherichia coli UppP. RCSB Protein Data Bank..