Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.6.1.27 extracted from

  • Coker, O.; Palittapongarnpim, P.
    Current understanding of de novo synthesis of bacterial lipid carrier (undecaprenyl phosphate): More enzymes to be discovered (2011), Afr. J. Microbiol. Res., 5, 2555-2565.
No PubMed abstract available
Search for more literature for 3.6.1.27

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane inner cytoplasmic membrane Bacillus subtilis 16020
-
membrane inner cytoplasmic membrane Escherichia coli 16020
-

Organism

Organism UniProt Comment Textmining
Bacillus subtilis P94571
-
-
Escherichia coli P60932
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
undecaprenyl diphosphate + H2O
-
 Bacillus subtilis undecaprenyl phosphate + phosphate
-
 ?
undecaprenyl diphosphate + H2O
-
 Escherichia coli undecaprenyl phosphate + phosphate
-
 ?

Synonyms

Synonyms Comment Organism
bacA
-
 Escherichia coli
BcrC
-
 Bacillus subtilis
Und-pp phosphatase
-
 Bacillus subtilis
Und-pp phosphatase
-
 Escherichia coli
undecaprenyl pyrophosphate phosphatase
-
 Bacillus subtilis
undecaprenyl pyrophosphate phosphatase
-
 Escherichia coli
Upp-P
-
 Bacillus subtilis
Upp-P
-
 Escherichia coli

General Information

General Information Comment Organism
malfunction an undecaprenyl pyrophosphate phosphatase null mutant does not show any significant growth or morphological defect, neither is its sensitivity to bacitracin affected. However, the enzyme activity in the mutant is reduced by 75% Escherichia coli
physiological function the enzyme confers resistance to bacitracin Bacillus subtilis