Biology:Undecaprenyl-diphosphatase
| undecaprenyl-diphosphatase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.6.1.27 | ||||||||
| CAS number | 9077-80-9 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
| Bacitracin resistance protein | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | ? | ||||||||
| Pfam | PF02673 | ||||||||
| InterPro | IPR003824 | ||||||||
| OPM superfamily | 479 | ||||||||
| OPM protein | 5oon | ||||||||
| |||||||||
In enzymology, an undecaprenyl-diphosphatase (EC 3.6.1.27) is an enzyme that catalyzes the chemical reaction
- undecaprenyl diphosphate + H2O [math]\displaystyle{ \rightleftharpoons }[/math] 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]).
References
- ↑ "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. doi:10.1099/00221287-146-7-1547. PMID 10878119.
- ↑ "undecaprenyl diphosphate (YMDB00637) - Yeast Metabolome Database". https://www.ymdb.ca/compounds/YMDB00637.
- ↑ "The bacA gene of Escherichia coli encodes an undecaprenyl pyrophosphate phosphatase activity". The Journal of Biological Chemistry 279 (29): 30106–13. July 2004. doi:10.1074/jbc.M401701200. PMID 15138271.
- ↑ "Crystal structure of undecaprenyl-pyrophosphate phosphatase and its role in peptidoglycan biosynthesis". Nature Communications 9 (1): 1078. March 2018. doi:10.1038/s41467-018-03477-5. PMID 29540682.
- ↑ "Crystal structure of an intramembranal phosphatase central to bacterial cell-wall peptidoglycan biosynthesis and lipid recycling". Nature Communications 9 (1): 1159. March 2018. doi:10.1038/s41467-018-03547-8. PMID 29559664.
- ↑ "5OON - Structure of Undecaprenyl-Pyrophosphate Phosphatase, BacA". http://www.rcsb.org/structure/5OON.
- ↑ "6CB2 - Crystal structure of Escherichia coli UppP". https://www.rcsb.org/structure/6CB2.
Further reading
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