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Information on EC 2.1.1.64 - 3-demethylubiquinol 3-O-methyltransferase and Organism(s) Homo sapiens

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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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Homo sapiens
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The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
5-demethylubiquinone-9-methyltransferase, ubig methyltransferase, 2-octaprenyl-3-methyl-5-hydroxy-6-methoxy-1,4-benzoquinone 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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Coq3 O-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-10
S-adenosyl-L-homocysteine + ubiquinol-10 + H+
show the reaction diagram
the enzyme catalyzes two methylation steps in the biosynthesis of ubiquinone-10, 1. the methylation of 3,4-dihydroxy-5-all-trans-decaprenylbenzoate (this reaction is classified as EC 2.1.1.114) and 2. the methylation of 3-demethylubiquinol-10
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?
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
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?
S-adenosyl-L-methionine + 3-demethylubiquinol-6
S-adenosyl-L-homocysteine + ubiquinol-6
show the reaction diagram
3-demethylubiquinol-6 is an intermediate in biosynthesis of ubiquinone-6 in Saccharomyces cerevisiae (methylated by the yeast enzyme COQ3 to ubiquinol-6). The human construct rescues the growth of a yeast coq3 null mutant on a nonfermentable carbon source and restores coenzyme Q biosynthesis, although at lower levels than that of wild type yeast
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additional information
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wide substrate specificity. The enzyme methylates both eukaryotic substrates 3,4-dihydroxy-5-farnesylbenzoic acid (this activity is classified as EC 2.1.1.114) and demethylubiquinol-3 and the distinct prokaryotic substrate 3-((2E,6E)-farnesyl)benzene-1,2-diol
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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-10
S-adenosyl-L-homocysteine + ubiquinol-10 + H+
show the reaction diagram
the enzyme catalyzes two methylation steps in the biosynthesis of ubiquinone-10, 1. the methylation of 3,4-dihydroxy-5-all-trans-decaprenylbenzoate (this reaction is classified as EC 2.1.1.114) and 2. the methylation of 3-demethylubiquinol-10
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?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
COQ3_HUMAN
369
0
41054
Swiss-Prot
Mitochondrion (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40998
x * 40998, calculated from sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 40998, calculated from sequence
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
when expressed in multicopy, the human construct rescues the growth of a yeast coq3 null mutant on a nonfermentable carbon source and restores coenzyme Q biosynthesis, although at lower levels than that of wild type yeast
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Jonassen, T.; Clarke, C.F.
Isolation and functional expression of human COQ3, a gene encoding a methyltransferase required for ubiquinone biosynthesis
J. Biol. Chem.
275
12381-12387
2000
Homo sapiens (Q9NZJ6)
Manually annotated by BRENDA team