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

BRENDA support

Literature summary extracted from

  • Brauer, L.; Brandt, W.; Wessjohann, L.A.
    Modeling the E. coli 4-hydroxybenzoic acid oligoprenyltransferase (ubiA transferase) and characterization of potential active sites. (2004), J. Mol. Model., 10, 317-327.
    View publication on PubMed

Organism

EC Number Organism UniProt Comment Textmining
2.5.1.39 Escherichia coli
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
2.5.1.39 a polyprenyl diphosphate + 4-hydroxybenzoate = diphosphate + a 4-hydroxy-3-polyprenylbenzoate a near SN1 mechanism for the cleavage of the diphosphate ion from the isoprenyl unit. The 4-hydroxybenzoic acid appears not to be activated as benzoate anion but rather as phenolate anion to allow attack of the isoprenyl cation to the phenolate, which appear to be the rate limiting step of the whole process according to our quantum chemical calculations Escherichia coli
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.5.1.39 geranyl diphosphate + 4-hydroxybenzoate
-
 Escherichia coli 3-geranyl-4-hydroxybenzoate + diphosphate
-
 ?
2.5.1.39 additional information one active site selected to be the most likely one for the docking of oligoprenyl diphosphate and 4-hydroxybenzoic acid is located near the N-terminus of the enzyme. An additional highly conserved region in the amino acid sequence of the ubiA enzyme is detected, which can be considered a putative active site Escherichia coli ?
-
 ?
2.5.1.39 octaprenyl diphosphate + 4-hydroxybenzoate
-
 Escherichia coli 4-hydroxy-3-octaprenylbenzoate + diphosphate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.5.1.39 ubiA
-
 Escherichia coli