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Information on EC 2.5.1.39 - 4-hydroxybenzoate polyprenyltransferase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P32378

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IUBMB Comments
This enzyme, involved in the biosynthesis of ubiquinone, attaches a polyprenyl side chain to a 4-hydroxybenzoate ring, producing the first ubiquinone intermediate that is membrane bound. The number of isoprenoid subunits in the side chain varies in different species. The enzyme does not have any specificity concerning the length of the polyprenyl tail, and accepts tails of various lengths with similar efficiency [2,4,5].
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Saccharomyces cerevisiae
UNIPROT: P32378
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The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
osppt1a, smppt, 4-hydroxybenzoate octaprenyltransferase, coq2p, 4-hydroxybenzoate polyprenyltransferase, nonaprenyl-4-hydroxybenzoate transferase, 4-hydroxybenzoate polyprenyl diphosphate transferase, 4-hydroxybenzoate:polyprenyl transferase, para-hydroxybenzoate-polyprenyl transferase, 4-hydroxybenzoate octaprenyl transferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4-hydroxybenzoate transferase
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dimethylallyltransferase, p-hydroxybenzoate poly-
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nonaprenyl-4-hydroxybenzoate transferase
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p-hydroxybenzoate dimethylallyltransferase
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p-hydroxybenzoate polyprenyltransferase
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p-hydroxybenzoic acid-polyprenyl transferase
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p-hydroxybenzoic-polyprenyl transferase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
alkenyl group transfer
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-
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PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
polyprenyl-diphosphate:4-hydroxybenzoate polyprenyltransferase
This enzyme, involved in the biosynthesis of ubiquinone, attaches a polyprenyl side chain to a 4-hydroxybenzoate ring, producing the first ubiquinone intermediate that is membrane bound. The number of isoprenoid subunits in the side chain varies in different species. The enzyme does not have any specificity concerning the length of the polyprenyl tail, and accepts tails of various lengths with similar efficiency [2,4,5].
CAS REGISTRY NUMBER
COMMENTARY hide
9030-77-7
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
decaprenyl diphosphate + 4-hydroxybenzoate
diphosphate + decaprenyl-4-hydroxybenzoate
show the reaction diagram
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-
-
-
?
solanesyl diphosphate + 4-hydroxybenzoate
diphosphate + nonaprenyl-4-hydroxybenzoate
show the reaction diagram
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-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
decaprenyl diphosphate + 4-hydroxybenzoate
diphosphate + decaprenyl-4-hydroxybenzoate
show the reaction diagram
-
-
-
-
?
solanesyl diphosphate + 4-hydroxybenzoate
diphosphate + nonaprenyl-4-hydroxybenzoate
show the reaction diagram
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-
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-
?
additional information
?
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the enzyme is required for biosynthesis of CoQ2, i.e. ubiquinone
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-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
in yeast extracts the specificity for the chain length of the isoprenyl diphosphate substrate is influenced by Mg2+
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
activity in recombinant yeast cells
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
enzyme contains a mitochondrion targeting sequence
Manually annotated by BRENDA team
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene COQ2, complementation of yeast Coq2 null mutant cells
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Forsgren, M.; Attersand, A.; Lake, S.; Gruenler, J.; Swiezewska, E.; Dallner, G.; Climent, I.
Isolation and functional expression of human COQ2, a gene encoding a polyprenyl transferase involved in the synthesis of CoQ
Biochem. J.
382
519-526
2004
Saccharomyces cerevisiae, Homo sapiens (Q96H96)
Manually annotated by BRENDA team
Lopez-Martin, J.M.; Salviati, L.; Trevisson, E.; Montini, G.; DiMauro, S.; Quinzii, C.; Hirano, M.; Rodriguez-Hernandez, A.; Cordero, M.D.; Sanchez-Alcazar, J.A.; Santos-Ocana, C.; Navas, P.
Missense mutation of the COQ2 gene causes defects of bioenergetics and de novo pyrimidine synthesis
Hum. Mol. Genet.
16
1091-1097
2007
Saccharomyces cerevisiae, Homo sapiens
Manually annotated by BRENDA team
Tran, U.C.; Clarke, C.F.
Endogenous synthesis of coenzyme Q in eukaryotes
Mitochondrion
7
62-71
2007
Arabidopsis thaliana, Oryza sativa, Saccharomyces cerevisiae (P32378), Schizosaccharomyces pombe (Q10252), Rattus norvegicus (Q499N4)
Manually annotated by BRENDA team