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Information on EC 2.1.1.64 - 3-demethylubiquinol 3-O-methyltransferase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P27680

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EC Tree
     2 Transferases
         2.1 Transferring one-carbon groups
             2.1.1 Methyltransferases
                2.1.1.64 3-demethylubiquinol 3-O-methyltransferase
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, Escherichia coli and rat also catalyse the methylation of 3,4-dihydroxy-5-all-trans-polyprenylbenzoate (a reaction that is classified as EC 2.1.1.114, polyprenyldihydroxybenzoate methyltransferase).
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Saccharomyces cerevisiae
UNIPROT: P27680
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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
5-demethylubiquinone-9-methyltransferase, 2-octaprenyl-3-methyl-5-hydroxy-6-methoxy-1,4-benzoquinone methyltransferase, ubig methyltransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2-octaprenyl-3-methyl-5-hydroxy-6-methoxy-1,4-benzoquinone methyltransferase
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5-demethylubiquinone-9 methyltransferase
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OMHMB-methyltransferase
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S-adenosyl-L-methionine:2-octaprenyl-3-methyl-5-hydroxy-6-methoxy-1,4-benzoquinone-O-methyltransferase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
methyl group transfer
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:3-hydroxy-2-methoxy-5-methyl-6-(all-trans-polyprenyl)-1,4-benzoquinol 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, Escherichia coli and rat also catalyse the methylation of 3,4-dihydroxy-5-all-trans-polyprenylbenzoate [3] (a reaction that is classified as EC 2.1.1.114, polyprenyldihydroxybenzoate methyltransferase).
CAS REGISTRY NUMBER
COMMENTARY hide
63774-48-1
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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-demethylubiquinol-3
S-adenosyl-L-homocysteine + ubiquinol-3
show the reaction diagram
i.e. 5-(2E,6E)-farnesyl-2-hydroxy-3-methoxy-6-methyl-1,4-benzoquinone
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S-adenosyl-L-methionine + 3-demethylubiquinol-6
S-adenosyl-L-homocysteine + ubiquinol-6
show the reaction diagram
the enzyme catalyzes two methylation steps in the biosynthesis of ubiquinone-6 in Saccharomyces cerevisiae, 1. the methylation of 3,4-dihydroxy-5-all-trans-hexaprenylbenzoate (this reaction is classified as EC 2.1.1.114) and 2. the methylation of 3-demethylubiquinol-6
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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-demethylubiquinol-6
S-adenosyl-L-homocysteine + ubiquinol-6
show the reaction diagram
the enzyme catalyzes two methylation steps in the biosynthesis of ubiquinone-6 in Saccharomyces cerevisiae, 1. the methylation of 3,4-dihydroxy-5-all-trans-hexaprenylbenzoate (this reaction is classified as EC 2.1.1.114) and 2. the methylation of 3-demethylubiquinol-6
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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
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
rat COQ3 gene restores O-methyltransferase activity in coq3 null mutant yeast
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
Coq3 and Coq4 are members of a ubiquinone-biosynthetic Coq polypeptide complex
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Escherichia coli, Rattus norvegicus (Q63159), Saccharomyces cerevisiae (P27680)
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)
Manually annotated by BRENDA team