Information on EC 2.1.1.222 - 2-polyprenyl-6-hydroxyphenol methylase

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

EC NUMBER
COMMENTARY hide
2.1.1.222
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RECOMMENDED NAME
GeneOntology No.
2-polyprenyl-6-hydroxyphenol methylase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + 3-(all-trans-polyprenyl)benzene-1,2-diol = S-adenosyl-L-homocysteine + 2-methoxy-6-(all-trans-polyprenyl)phenol
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
ubiquinol-10 biosynthesis (prokaryotic)
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ubiquinol-7 biosynthesis (prokaryotic)
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ubiquinol-8 biosynthesis (prokaryotic)
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ubiquinol-9 biosynthesis (prokaryotic)
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ubiquinone biosynthesis
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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-(all-trans-polyprenyl)benzene-1,2-diol 2-O-methyltransferase
UbiG catalyses both methylation steps in ubiquinone biosynthesis in Escherichia coli. The second methylation is classified as EC 2.1.1.64 (3-demethylubiquinol 3-O-methyltransferase) [2]. In eukaryotes Coq3 catalyses the two methylation steps in ubiquinone biosynthesis. However, while the second methylation is common to both enzymes, the first methylation by Coq3 occurs at a different position within the pathway, and thus involves a different substrate and is classified as EC 2.1.1.114 (polyprenyldihydroxybenzoate methyltransferase). The substrate of the eukaryotic enzyme (3,4-dihydroxy-5-all-trans-polyprenylbenzoate) differs by an additional carboxylate moiety.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
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after 1 h of H2O2 treatment, the viability of the strain defective in ubiG is reduced 28fold compared to the corresponding wild-type. When treated with CuSO4, the viability of the the strain defective in ubiG (HW271), is reduced 4.4fold after 30 min compared to its isogenic wild-type
metabolism
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 + 2-(all-trans-decaprenyl)-5-hydroxy-6-methoxy-3-methylcyclohexa-2,5-diene-1,4-dione
S-adenosyl-L-homocysteine + 2-(all-trans-decaprenyl)-5,6-dimethoxy-3-methylcyclohexa-2,5-diene-1,4-dione
show the reaction diagram
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?
S-adenosyl-L-methionine + 3-((2E,6E)-farnesyl)benzene-1,2-diol
S-adenosyl-L-homocysteine + 2-methoxy-6-((2E,6E)-farnesyl)phenol
show the reaction diagram
S-adenosyl-L-methionine + 3-((2E,6E)-farnesyl)benzene-1,2-diol
S-adenosyl-L-homocysteine + 2-methoxy-6-(farnesyl)phenol
show the reaction diagram
i.e. 3-[(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-yl]benzene-1,2-diol. The substrate is an artificial farnesylated analog of the Escherichia coli substrate 2-octaprenyl-6-hydroxyphenol, an intermediate in the biosynthesis of ubiquinone-8 in Escherichia coli
i.e. 2-methoxy-6-((2E,6E)-3,7,11-trimethyldodeca-2,6,10-trienyl)phenol
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?
S-adenosyl-L-methionine + 3-(all-trans-decaprenyl)-benzene-1,2-diol
S-adenosyl-L-homocysteine + 3-(all-trans-decaprenyl)-1-methoxybenzene-2-ol
show the reaction diagram
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?
S-adenosyl-L-methionine + 3-(all-trans-octaprenyl)benzene-1,2-diol
S-adenosyl-L-homocysteine + 2-methoxy-6-(all-trans-octaprenyl)phenol
show the reaction diagram
additional information
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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-(all-trans-octaprenyl)benzene-1,2-diol
S-adenosyl-L-homocysteine + 2-methoxy-6-(all-trans-octaprenyl)phenol
show the reaction diagram
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the enzyme catalyzes two methylation steps in the biosynthesis of ubiquinone-8 in Escherichia coli, 1. the methylation of 3-(all-trans-octaprenyl)benzene-1,2-diol and 2. the methylation of 3-demethylubiquinol-8 (this reaction is classified as EC 2.1.1.64)
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additional information
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
S-adenosyl-L-methionine
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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
monomer
x-ray crystallography
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 0.1 M HEPES pH 7.5 and 20% (w/v) 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
His6-UbiG fusion protein
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Ni-NTA column chromatography, HiTrap column chromatography, and Superdex 200 gel filtration
Ni-NTA column chromatography, Superdex 200 gel filtration, and DEAE anion-exchange chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
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
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of the ubiG gene is higher under aerobic conditions than under anaerobic growth conditions. Addition of cAMP increases the expression of the ubiG gene in both cya and wild-type strains but not in a crp mutant. The cAMP receptor protein-cyclic AMP complex positively modulates ubiG gene transcription
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expression of the ubiG gene is higher under aerobic conditions than under anaerobic growth conditions. The presence of glucose in the culture medium decreases the transcription of the ubiG gene. cya and cip mutants exhibit lower levels of ubiG gene expression than the wild-type strain
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H186A
the mutation completely destroys the interaction of the enzyme with liposomes
I177A
the mutation sharply reduces the interaction of the enzyme with liposomes
K183A
the mutation nearly completely destroys the interaction of the enzyme with liposomes
L132Q
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the mutation results in ubiquinone deficiency in Escherichia coli leading to a high sensitivity to thiols and a failure to grow on succinate
L178A
the mutation nearly completely destroys the interaction of the enzyme with liposomes
L178E
the mutation nearly completely destroys the interaction of the enzyme with liposomes
R179A
the mutation sharply reduces the interaction of the enzyme with liposomes
V181A
the mutation nearly completely destroys the interaction of the enzyme with liposomes
V181A/P182A/K183A/G184A/T185A/H186A
the mutations nearly completely destroy the interaction of the enzyme with liposomes
additional information
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