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Information on EC 2.1.1.114 - polyprenyldihydroxybenzoate methyltransferase and Organism(s) Rattus norvegicus and UniProt Accession Q63159

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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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Rattus norvegicus
UNIPROT: Q63159
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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: Rattus norvegicus
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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ubiquinone biosynthesis O-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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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)-farnesyl)benzoate
S-adenosyl-L-homocysteine + 5-((2E,6E)-farnesyl)-4-hydroxy-3-methoxybenzoate
show the reaction diagram
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-
-
?
S-adenosyl-L-methionine + 3,4-dihydroxy-5-octaprenylbenzoate
S-adenosyl-L-homocysteine + 4-hydroxy-3-methoxy-5-octaprenylbenzoate
show the reaction diagram
the enzyme catalyzes two methylation steps in the biosynthesis of ubiquinone-8, 1. the methylation of 3,4-dihydroxy-5-octaprenylbenzoate and 2. the methylation of 3-demethylubiquinol-8 (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-octaprenylbenzoate
S-adenosyl-L-homocysteine + 4-hydroxy-3-methoxy-5-octaprenylbenzoate
show the reaction diagram
the enzyme catalyzes two methylation steps in the biosynthesis of ubiquinone-8, 1. the methylation of 3,4-dihydroxy-5-octaprenylbenzoate and 2. the methylation of 3-demethylubiquinol-8 (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
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
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
the levels of SAM-dependent methyltransferases Coq3 and Coq5 are decreased in the myocardial infarction groups. In addition, short-chain (C3) and medium-chain (C4-C12) acylcarnitine levels gradually decrease, whereas long-chain acylcarnitine (C14-18) levels increase in myocardial infarction
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
Rattus norvegicus (Q63159), Saccharomyces cerevisiae (P27680), Saccharomyces cerevisiae
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
Nam, M.; Jung, Y.; Ryu, D.; Hwang, G.
A metabolomics-driven approach reveals metabolic responses and mechanisms in the rat heart following myocardial infarction
Int. J. Cardiol.
227
239-246
2017
Rattus norvegicus (Q63159)
Manually annotated by BRENDA team