Undecaprenyl-diphosphatase

Class of enzymes From Wikipedia, the free encyclopedia

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

undecaprenyl diphosphate + H2O undecaprenyl phosphate + phosphate
Quick facts Bacitracin resistance protein, Identifiers ...
Bacitracin resistance protein
Identifiers
Symbol?
PfamPF02673
InterProIPR003824
OPM superfamily479
OPM protein5oon
Available protein structures:
PDB  IPR003824 PF02673 (ECOD; PDBsum)  
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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

Further reading

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