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Literature summary for 2.5.1.39 extracted from

  • Bräuer, L.; Brandt, W.; Schulze, D.; Zakharova, S.; Wessjohann, L.
    A structural model of the membrane-bound aromatic prenyltransferase UbiA from E. coli (2008), Chembiochem, 9, 982-992.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli Escherichia coli

Protein Variants

Protein Variants Comment Organism
D191A mutant shows no 3-geranylgeranyl-4-hydroxybenzoate formation, mutant shows some residual hydrolysis activity Escherichia coli
D195A mutant shows no 3-geranylgeranyl-4-hydroxybenzoate formation, mutant shows some residual hydrolysis activity Escherichia coli
D71A mutant shows no 3-geranylgeranyl-4-hydroxybenzoate formation, mutant shows some residual hydrolysis activity Escherichia coli
D75A mutant shows no 3-geranylgeranyl-4-hydroxybenzoate formation, mutant shows some residual hydrolysis activity Escherichia coli
R137A mutant shows a strongly reduced formation of 3-geranylgeranyl-4-hydroxybenzoate, mutant shows some residual hydrolysis activity Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
Escherichia coli 16020
-

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
geranyl diphosphate + 4-hydroxybenzoate
-
Escherichia coli 3-geranyl-4-hydroxybenzoate + diphosphate
-
?
additional information in the presence of Mg2+ the enzyme is also able to hydrolyze geranyl diphosphate without forming geranylgeranyl-4-hydroxybenzoate Escherichia coli ?
-
?

Synonyms

Synonyms Comment Organism
4-hydroxybenzoic acid oligoprenyltransferase
-
Escherichia coli
ubiA
-
Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.8
-
assay at Escherichia coli