Literature summary for 2.5.1.39 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.

Search for more literature for 2.5.1.39

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
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)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
geranyl diphosphate + 4-hydroxybenzoate	-	Escherichia coli	3-geranyl-4-hydroxybenzoate + diphosphate	-	?
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	?	-	?
octaprenyl diphosphate + 4-hydroxybenzoate	-	Escherichia coli	4-hydroxy-3-octaprenylbenzoate + diphosphate	-	?

Synonyms

Synonyms	Comment	Organism
ubiA	-	Escherichia coli

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Release 2023.1 (January 2023)