“Undecaprenyl-diphosphatase”的意思、由来-开放百科全书

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

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.

Note: The enzyme Uppp/BacA (EC 3.6.1.27) has occasionally been incorrectly termed an "undecaprenol kinase".^[2] 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^[3]^[4] are available (PDB IDs: 5OON^[5], 6CB2^[6]).

References

1. ^{{cite journal | vauthors = Chalker AF, Ingraham KA, Lunsford RD, Bryant AP, Bryant J, Wallis NG, Broskey JP, Pearson SC, Holmes DJ | title = The bacA gene, which determines bacitracin susceptibility in Streptococcus pneumoniae and Staphylococcus aureus, is also required for virulence | journal = Microbiology | volume = 146 | issue = Pt 7 | pages = 1547–53 | date = July 2000 | pmid = 10878119 | doi = 10.1099/00221287-146-7-1547 }}
2. ^{{cite journal | vauthors = El Ghachi M, Bouhss A, Blanot D, Mengin-Lecreulx D | title = The bacA gene of Escherichia coli encodes an undecaprenyl pyrophosphate phosphatase activity | journal = The Journal of Biological Chemistry | volume = 279 | issue = 29 | pages = 30106–13 | date = July 2004 | pmid = 15138271 | doi = 10.1074/jbc.M401701200 }}
3. ^{{cite journal | vauthors = El Ghachi M, Howe N, Huang CY, Olieric V, Warshamanage R, Touzé T, Weichert D, Stansfeld PJ, Wang M, Kerff F, Caffrey M | title = Crystal structure of undecaprenyl-pyrophosphate phosphatase and its role in peptidoglycan biosynthesis | journal = Nature Communications | volume = 9 | issue = 1 | pages = 1078 | date = March 2018 | pmid = 29540682 | pmc = 5852022 | doi = 10.1038/s41467-018-03477-5 }}
4. ^{{cite journal | vauthors = Workman SD, Worrall LJ, Strynadka NC | title = Crystal structure of an intramembranal phosphatase central to bacterial cell-wall peptidoglycan biosynthesis and lipid recycling | journal = Nature Communications | volume = 9 | issue = 1 | pages = 1159 | date = March 2018 | pmid = 29559664 | pmc = 5861054 | doi = 10.1038/s41467-018-03547-8 }}
5. ^{{Cite web|url=http://www.rcsb.org/structure/5OON|title=5OON - Structure of Undecaprenyl-Pyrophosphate Phosphatase, BacA|last=|first=|date=|website=RCSB Protein Data Bank|archive-url=|archive-date=|dead-url=|access-date=}}
6. ^{{Cite web|url=https://www.rcsb.org/structure/6CB2|title=6CB2 - Crystal structure of Escherichia coli UppP|last=|first=|date=|website=RCSB Protein Data Bank.|archive-url=|archive-date=|dead-url=|access-date=}}

Nomenclature

Structure

References

Further reading