Information on EC 2.1.1.114 - polyprenyldihydroxybenzoate methyltransferase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
2.1.1.114
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RECOMMENDED NAME
GeneOntology No.
polyprenyldihydroxybenzoate methyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
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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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
methyl group transfer
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
superpathway of ubiquinol-6 biosynthesis (eukaryotic)
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ubiquinol-10 biosynthesis (eukaryotic)
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ubiquinol-6 biosynthesis from 4-hydroxybenzoate (eukaryotic)
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ubiquinol-6 bypass biosynthesis (eukaryotic)
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ubiquinol-7 biosynthesis (eukaryotic)
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ubiquinol-8 biosynthesis (eukaryotic)
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ubiquinol-9 biosynthesis (eukaryotic)
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Ubiquinone and other terpenoid-quinone biosynthesis
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Metabolic pathways
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Biosynthesis of secondary metabolites
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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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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
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-(2E,6E)-farnesylbenzoate
S-adenosyl-L-homocysteine + 3-methoxy-4-hydroxy-5-farnesylbenzoate
show the reaction diagram
-
-
-
-
?
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
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?
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
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
S-adenosyl-L-methionine + 3,4-dihydroxy-5-hexaprenylbenzoate
S-adenosyl-L-homocysteine + 3-methoxy-4-hydroxy-5-hexaprenylbenzoate
show the reaction diagram
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the enzyme catalyzes two methylation steps in the biosynthesis of ubiquinone-6, 1. the methylation of 3,4-dihydroxy-5-hexaprenylbenzoate and 2. the methylation of 3-demethylubiquinol-6 (this reaction is classified as EC 2.1.1.64)
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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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?
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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?
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 SUBSTRATES
NATURAL PRODUCTS
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-all-trans-hexaprenylbenzoate
S-adenosyl-L-homocysteine + 5-all-trans-hexaprenyl-4-hydroxy-3-methoxybenzoate
show the reaction diagram
P27680
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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
S-adenosyl-L-methionine + 3,4-dihydroxy-5-hexaprenylbenzoate
S-adenosyl-L-homocysteine + 3-methoxy-4-hydroxy-5-hexaprenylbenzoate
show the reaction diagram
-
the enzyme catalyzes two methylation steps in the biosynthesis of ubiquinone-6, 1. the methylation of 3,4-dihydroxy-5-hexaprenylbenzoate and 2. the methylation of 3-demethylubiquinol-6 (this reaction is classified as EC 2.1.1.64)
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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
Q63159
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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?
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
Q9NZJ6
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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?
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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the Coq3 polypeptide is peripherally associated with the matrix side of the inner membrane of yeast mitochondria
Manually annotated by BRENDA team
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 40998, calculated from sequence
monomer
x-ray crystallography
additional information
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Coq3 and Coq4 are members of a ubiquinone-biosynthetic Coq polypeptide complex
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography and Superdex 200 gel filtration
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
AtCOQ3 is able to restore the respiration ability and ubiquinone synthesis of the coq3 deletion mutant of Saccharomyces cerevisiae
expressed in an Escherichia coli ubiG mutant
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expressed in Escherichia coli BL21(DE3) cells
rat COQ3 gene restores O-methyltransferase activity in coq3 null mutant yeast
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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
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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