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Information on EC 2.1.1.64 - 3-demethylubiquinol 3-O-methyltransferase and Organism(s) Rattus norvegicus and UniProt Accession Q63159

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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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Rattus norvegicus
UNIPROT: Q63159
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The taxonomic range for the selected organisms is: Rattus norvegicus
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
5-demethylubiquinone-9-methyltransferase
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2-octaprenyl-3-methyl-5-hydroxy-6-methoxy-1,4-benzoquinone methyltransferase
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-
-
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5-demethylubiquinone-9 methyltransferase
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-
-
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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
-
-
-
-
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, in vitro assay
-
-
?
S-adenosyl-L-methionine + 3-demethylubiquinol-9
S-adenosyl-L-homocysteine + ubiquinol-9
show the reaction diagram
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-9
S-adenosyl-L-homocysteine + ubiquinol-9
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
NADH stimualtes activity of mitochondrial fraction
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00006 - 0.00008
3-demethylubiquinol-9
pH 7.4, mitochondrial fraction
0.022
S-adenosyl-L-methionine
pH 7.4, mitochondrial fraction
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
COQ3_RAT
345
0
38708
Swiss-Prot
Mitochondrion (Reliability: 2)
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
rat COQ3 gene restores O-methyltransferase activity in coq3 null mutant yeast
the rescue of the yeast coq3 mutant by the rat homologue suggests that yeast and rat synthesize ubiquinone via the same early steps in this pathway
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
Houser, R.M.; Olson, E.
5-Demethylubiquinone-9-methyltransferase from rat liver mitochondria. Characterization, localization, and solubilization
J. Biol. Chem.
252
4017-4021
1977
Rattus norvegicus (Q63159)
Manually annotated by BRENDA team
Marbois, B.N.; Hsu, A.; Pillai, R.; Colicelli, J.; Clarke, C.F.
Cloning of a rat cDNA encoding dihydroxypolyprenylbenzoate methyltransferase by functional complementation of a Saccharomyces cerevisiae mutant deficient in ubiquinone biosynthesis
Gene
138
213-217
1994
Rattus norvegicus (Q63159)
Manually annotated by BRENDA team