Information on EC 2.1.1.64 - 3-demethylubiquinol 3-O-methyltransferase

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

EC NUMBER
COMMENTARY hide
2.1.1.64
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RECOMMENDED NAME
GeneOntology No.
3-demethylubiquinol 3-O-methyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + 3-demethylubiquinol-n = S-adenosyl-L-homocysteine + ubiquinol-n
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
Biosynthesis of secondary metabolites
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Metabolic pathways
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ubiquinol-10 biosynthesis (eukaryotic)
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ubiquinol-10 biosynthesis (prokaryotic)
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ubiquinol-6 biosynthesis from 4-aminobenzoate (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-7 biosynthesis (prokaryotic)
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ubiquinol-8 biosynthesis (eukaryotic)
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ubiquinol-8 biosynthesis (prokaryotic)
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ubiquinol-9 biosynthesis (eukaryotic)
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ubiquinol-9 biosynthesis (prokaryotic)
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Ubiquinone and other terpenoid-quinone biosynthesis
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non-pathway related
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ubiquinone biosynthesis
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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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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
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
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the ubiG gene product is essential for growth on glycerol minimal medium
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
S-adenosyl-L-methionine + 3-demethylubiquinol-6
S-adenosyl-L-homocysteine + ubiquinol-6
show the reaction diagram
S-adenosyl-L-methionine + 3-demethylubiquinol-8
S-adenosyl-L-homocysteine + ubiquinol-8
show the reaction diagram
S-adenosyl-L-methionine + 3-demethylubiquinol-9
S-adenosyl-L-homocysteine + ubiquinol-9
show the reaction diagram
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 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-demethylubiquinol-10
S-adenosyl-L-homocysteine + ubiquinol-10 + H+
show the reaction diagram
Q9NZJ6
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-6
S-adenosyl-L-homocysteine + ubiquinol-6
show the reaction diagram
P27680
the enzyme catalyzes two methylation steps in the biosynthesis of ubiquinone-6 in Saccharomyces cerevisiae, 1. the methylation of 3,4-dihydroxy-5-all-trans-hexaprenylbenzoate (this reaction is classified as EC 2.1.1.114) and 2. the methylation of 3-demethylubiquinol-6
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?
S-adenosyl-L-methionine + 3-demethylubiquinol-8
S-adenosyl-L-homocysteine + ubiquinol-8
show the reaction diagram
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
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NADH stimualtes activity of mitochondrial fraction
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cd2+
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absolute requirement for a divalent metal ion. 1 mM Cd2+ stimulates 14fold
Co2+
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absolute requirement for a divalent metal ion. 1 mM Co2+ stimulates 67fold
Cu2+
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absolute requirement for a divalent metal ion. 1 mM Cu2+ stimulates 21fold
Fe2+
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absolute requirement for a divalent metal ion. 1 mM Fe2+ stimulates 63fold
Mg2+
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absolute requirement for a divalent metal ion. 1 mM Mg2+ stimulates about 3fold
Mn2+
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absolute requirement for a divalent metal ion. 1 mM Mn2+ stimulates 11fold
Ni2+
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absolute requirement for a divalent metal ion. 1 mM Ni2+ stimulates 24fold
Zn2+
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absolute requirement for a divalent metal ion. Zn2+ is most effective. 1 mM Zn2+ stimulates over 100fold
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
dithiothreitol
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the optimum ratio of dithiothreitol to divalent metal ion is about 10:1. The maximal methyltransferase activity is achieved at 10 mM dithiothreitol and 1 mM Zn2+
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00006 - 0.00008
3-demethylubiquinol-9
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pH 7.4, mitochondrial fraction
0.022
S-adenosyl-L-methionine
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pH 7.4, mitochondrial fraction
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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associated. In vivo, the methyltransferase reaction probably occurs at the internal surface of the cytoplasmic membrane
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
26600
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x * 26600, SDS-PAGE
40998
x * 40998, calculated from sequence
50000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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Coq3 and Coq4 are members of a ubiquinone-biosynthetic Coq polypeptide complex
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using either 0.1 M HEPES pH 7.5 and 20% polyethylene glycol 10000 or 10% (v/v) 2-methyl-2,4-pentanediol and 0.1 M HEPES pH 7.0
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography, DEAE column chromatography, and Superdex 200 gel filtration
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
AtCOQ3 is able to restore the respiration ability and ubiquinone synthesis of the coq3 deletion mutant of Saccharomyces cerevisiae
His6-tagged enzyme is expressed in Escherichia coli BL21(DE3) cells
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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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the ubiG gene is able to restore respiration in the yeast coq3 mutant, provided ubiG is modified to contain a mitochondrial leader sequence
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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
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