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Information on EC 2.1.1.114 - polyprenyldihydroxybenzoate methyltransferase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P27680

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EC Tree
IUBMB Comments
This enzyme is involved in ubiquinone biosynthesis. Ubiquinones from different organisms have a different number of prenyl units (for example, ubiquinone-6 in Saccharomyces, ubiquinone-9 in rat and ubiquinone-10 in human), and thus the natural substrate for the enzymes from different organisms has a different number of prenyl units. However, the enzyme usually shows a low degree of specificity regarding the number of prenyl units. For example, the human COQ3 enzyme can restore biosynthesis of ubiquinone-6 in coq3 deletion mutants of yeast . The enzymes from yeast and rat also catalyse the methylation of 3-demethylubiquinol-6 and 3-demethylubiquinol-9, respectively (this activity is classified as EC 2.1.1.64, 3-demethylubiquinol 3-O-methyltransferase).
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Saccharomyces cerevisiae
UNIPROT: P27680
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Word Map
  • 2.1.1.114
  • nonfermentable
  • multi-subunit
  • q-deficient
  • peripherally
  • co-migrate
  • elegans
  • worms
  • p-hydroxybenzoic
  • digitonin-solubilized
  • native-page
  • isoprenoid
  • medicine
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
coq3p, coq-3, coq3 o-methyltransferase, dhhb methyltransferase, dhhb-mtase, 3,4-dihydroxy-5-hexaprenylbenzoate methyltransferase, atcoq3, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3,4-dihydroxy-5-hexaprenylbenzoate methyltransferase
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DHHB methyltransferase
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3,4-dihydroxy-5-hexaprenylbenzoate methyltransferase
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dihydroxyhexaprenylbenzoate methyltransferase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
methyl group transfer
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-
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:3,4-dihydroxy-5-all-trans-polyprenylbenzoate 3-O-methyltransferase
This enzyme is involved in ubiquinone biosynthesis. Ubiquinones from different organisms have a different number of prenyl units (for example, ubiquinone-6 in Saccharomyces, ubiquinone-9 in rat and ubiquinone-10 in human), and thus the natural substrate for the enzymes from different organisms has a different number of prenyl units. However, the enzyme usually shows a low degree of specificity regarding the number of prenyl units. For example, the human COQ3 enzyme can restore biosynthesis of ubiquinone-6 in coq3 deletion mutants of yeast [3]. The enzymes from yeast and rat also catalyse the methylation of 3-demethylubiquinol-6 and 3-demethylubiquinol-9, respectively [2] (this activity is classified as EC 2.1.1.64, 3-demethylubiquinol 3-O-methyltransferase).
CAS REGISTRY NUMBER
COMMENTARY hide
139569-30-5
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139569-31-6
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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
S-adenosyl-L-methionine + 3,4-dihydroxy-5-(2E,6E)-farnesylbenzoate
S-adenosyl-L-homocysteine + 3-methoxy-4-hydroxy-5-farnesylbenzoate
show the reaction diagram
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-
-
?
S-adenosyl-L-methionine + 3,4-dihydroxy-5-all-trans-hexaprenylbenzoate
S-adenosyl-L-homocysteine + 5-all-trans-hexaprenyl-4-hydroxy-3-methoxybenzoate
show the reaction diagram
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-
-
?
S-adenosyl-L-methionine + 3,4-dihydroxy-5-hexaprenylbenzoate
S-adenosyl-L-homocysteine + 3-methoxy-4-hydroxy-5-hexaprenylbenzoate
show the reaction diagram
the enzyme catalyzes two methylation steps in the biosynthesis of ubiquinone-6, 1. the methylation of 3,4-dihydroxy-5-hexaprenylbenzoate and 2. the methylation of 3-demethylubiquinol-6 (this reaction is classified as EC 2.1.1.64)
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?
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
S-adenosyl-L-methionine + 3,4-dihydroxy-5-all-trans-hexaprenylbenzoate
S-adenosyl-L-homocysteine + 5-all-trans-hexaprenyl-4-hydroxy-3-methoxybenzoate
show the reaction diagram
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-
-
?
S-adenosyl-L-methionine + 3,4-dihydroxy-5-hexaprenylbenzoate
S-adenosyl-L-homocysteine + 3-methoxy-4-hydroxy-5-hexaprenylbenzoate
show the reaction diagram
the enzyme catalyzes two methylation steps in the biosynthesis of ubiquinone-6, 1. the methylation of 3,4-dihydroxy-5-hexaprenylbenzoate and 2. the methylation of 3-demethylubiquinol-6 (this reaction is classified as EC 2.1.1.64)
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?
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
the Coq3 polypeptide is peripherally associated with the matrix side of the inner membrane of yeast mitochondria
Manually annotated by BRENDA team
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Clarke, C.F.; Williams, W.; Teruya, J.H.
Ubiquinone biosynthesis in Saccharomyces cerevisae. Isolation and sequence of COQ3 the 3,4-dihydroxy-5-hexaprenylbenzoate methyltransferase gene
J. Biol. Chem.
266
16636-16644
1991
Saccharomyces cerevisiae (P27680), Saccharomyces cerevisiae
Manually annotated by BRENDA team
Poon, W.W.; Barkovich, R.J.; Hsu, A.Y.; Frankel, A.; Lee, P.T.; Sheperd, J.N.; Myles, D.C.; Clarke, C.F.
Yeast and rat Coq3 and Escherichia coli UbiG polypeptides catalyze both O-methyltransferase steps in coenzyme Q biosynthesis
J. Biol. Chem.
274
21665-21672
1999
Rattus norvegicus (Q63159), Saccharomyces cerevisiae (P27680), Saccharomyces cerevisiae
Manually annotated by BRENDA team
Marbois, B.; Gin, P.; Faull, K.F.; Poon, W.W.
Lee, P.T.; Strahan, J.; Shepherd, J.N., Clarke, C.F.: Coq3 and Coq4 define a polypeptide complex in yeast mitochondria for the biosynthesis of coenzyme Q
J. Biol. Chem.
280
20231-20238
2005
Saccharomyces cerevisiae (P27680), Saccharomyces cerevisiae
Manually annotated by BRENDA team