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Information on EC 2.1.1.114 - polyprenyldihydroxybenzoate methyltransferase and Organism(s) Homo sapiens and UniProt Accession Q9NZJ6

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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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Homo sapiens
UNIPROT: Q9NZJ6
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Word Map
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  • 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: Homo sapiens
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
Coq3 O-methyltransferase
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3,4-dihydroxy-5-hexaprenylbenzoate methyltransferase
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-
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COQ3
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dihydroxyhexaprenylbenzoate methyltransferase
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-
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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 + 5-(2E,6E)-farnesyl-4-hydroxy-3-methoxybenzoate
show the reaction diagram
in vitro assay
-
-
?
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
3,4-dihydroxy-5-all-trans-hexaprenylbenzoate is an intermediate in biosynthesis of ubiquinone-6 in Saccharomyces cerevisiae (that is methylated by the yeast enzyme CoQ3 to 4-hydroxy-3-methoxy-5-hexaprenylbenzoate). 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
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-
?
S-adenosyl-L-methionine + 5-all-trans-decaprenyl-3,4-dihydroxybenzoate
S-adenosyl-L-homocysteine + 5-all-trans-decaprenyl-4-hydroxy-3-methoxybenzoate
show the reaction diagram
the enzyme catalyzes two methylation steps in the biosynthesis of ubiquinone-10, 1. the methylation of 5-all-trans-decaprenyl-3,4-dihydroxybenzoate and 2. the methylation of 3-demethylubiquinol-10 (this reaction is classified as EC 2.1.1.64)
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-
?
S-adenosyl-L-methionine + 3,4-dihydroxy-5-all-trans-polyprenylbenzoate
S-adenosyl-L-homocysteine + 3-methoxy-4-hydroxy-5-all-trans-polyprenylbenzoate
show the reaction diagram
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?
additional information
?
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wide substrate specificity. The enzyme methylates both eukaryotic substrates demethylubiquinol-3 (this activity is classified as EC 2.1.1.64) and 3,4-dihydroxy-5-farnesylbenzoic acid 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 + 5-all-trans-decaprenyl-3,4-dihydroxybenzoate
S-adenosyl-L-homocysteine + 5-all-trans-decaprenyl-4-hydroxy-3-methoxybenzoate
show the reaction diagram
the enzyme catalyzes two methylation steps in the biosynthesis of ubiquinone-10, 1. the methylation of 5-all-trans-decaprenyl-3,4-dihydroxybenzoate and 2. the methylation of 3-demethylubiquinol-10 (this reaction is classified as EC 2.1.1.64)
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-
?
S-adenosyl-L-methionine + 3,4-dihydroxy-5-all-trans-polyprenylbenzoate
S-adenosyl-L-homocysteine + 3-methoxy-4-hydroxy-5-all-trans-polyprenylbenzoate
show the reaction diagram
-
-
-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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the primary role of the enzyme is to serve as an electron carrier in the respiratory electron transport chain in the mitochondrial inner membrane
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography and Superdex 200 gel filtration
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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
expressed in Escherichia coli BL21(DE3) cells
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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
Zhu, Y.; Wu, B.; Zhang, X.; Fan, X.; Niu, L.; Li, X.; Wang, J.; Teng, M.
Structural and biochemical studies reveal UbiG/Coq3 as a class of novel membrane-binding proteins
Biochem. J.
470
105-114
2015
Homo sapiens, Escherichia coli (P17993)
Manually annotated by BRENDA team