Information on EC 2.1.1.201 - 2-methoxy-6-polyprenyl-1,4-benzoquinol methylase

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

EC NUMBER
COMMENTARY hide
2.1.1.201
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RECOMMENDED NAME
GeneOntology No.
2-methoxy-6-polyprenyl-1,4-benzoquinol methylase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + 2-methoxy-6-all-trans-polyprenyl-1,4-benzoquinol = S-adenosyl-L-homocysteine + 6-methoxy-3-methyl-2-all-trans-polyprenyl-1,4-benzoquinol
show the reaction diagram
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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ubiquinone biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:2-methoxy-6-all-trans-polyprenyl-1,4-benzoquinol 5-C-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, when the COQ5 gene from Saccharomyces cerevisiae is introduced into Escherichia coli, it complements the respiratory deficiency of an ubiE mutant [3]. The bifunctional enzyme from Escherichia coli also catalyses the methylation of demethylmenaquinol-8 (this activity is classified as EC 2.1.1.163) [1].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
physiological function
additional information
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-methoxy-6-(all-trans-hexaprenyl)-1,4-benzoquinol
S-adenosyl-L-homocysteine + 6-methoxy-5-methyl-2-(all-trans)-hexaprenyl-1,4-benzoquinol
show the reaction diagram
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-
-
-
?
S-adenosyl-L-methionine + 2-methoxy-6-all-trans-polyprenyl-1,4-benzoquinol
S-adenosyl-L-homocysteine + 6-methoxy-3-methyl-2-all-trans-polyprenyl-1,4-benzoquinol
show the reaction diagram
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-
-
?
S-adenosyl-L-methionine + 2-methoxy-6-octaprenyl-1,4-benzoquinol
S-adenosyl-L-homocysteine + 6-methoxy-5-methyl-2-octaprenyl-1,4-benzoquinol
show the reaction diagram
S-adenosyl-L-methionine + 2-methoxy-6-polyprenyl-1,4-benzoquinol
S-adenosyl-L-homocysteine + 6-methoxy-5-methyl-2-polyprenyl-1,4-benzoquinol
show the reaction diagram
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-
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-
?
S-adenosyl-L-methionine + 6-((2-trans,6-trans)-farnesyl)-2-methoxy-1,4-benzoquinone
S-adenosyl-L-homocysteine + 6-((2-trans,6-trans)-farnesyl)-5-methyl-2-methoxy-1,4-benzoquinone
show the reaction diagram
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product determined by reverse-phase HPLC
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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 + 2-methoxy-6-(all-trans-hexaprenyl)-1,4-benzoquinol
S-adenosyl-L-homocysteine + 6-methoxy-5-methyl-2-(all-trans)-hexaprenyl-1,4-benzoquinol
show the reaction diagram
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-
-
-
?
S-adenosyl-L-methionine + 2-methoxy-6-all-trans-polyprenyl-1,4-benzoquinol
S-adenosyl-L-homocysteine + 6-methoxy-3-methyl-2-all-trans-polyprenyl-1,4-benzoquinol
show the reaction diagram
P49017
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?
S-adenosyl-L-methionine + 2-methoxy-6-octaprenyl-1,4-benzoquinol
S-adenosyl-L-homocysteine + 6-methoxy-5-methyl-2-octaprenyl-1,4-benzoquinol
show the reaction diagram
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADH
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NAFH is required form optimal activity in in vitro assay with mitochondrial lysate. It is likely that the function of NADH is the reduction of the oxidized 2-methoxy-6-polyprenyl-1,4-benzoquinone substrate to the hydroquinone form (2-methoxy-6-polyprenyl-1,4-benzoquinol), which presumably acts as the methyl acceptor
S-adenosyl-L-methionine
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
highly expressed
Manually annotated by BRENDA team
relatively low expressed
Manually annotated by BRENDA team
highly expressed in young leaves, relatively low expressed in mature leaves
Manually annotated by BRENDA team
relatively low expressed
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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peripherally associated with the inner mitochondrial membrane on the matrix side
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
32200
x * 32200, calculated from sequence
34685
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x * 34685, calculated from sequence
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified enzyme in apoform and in complex with S-adenosyl-L-methionine, hanging drop vapour diffusion method, mixing of 0.003 ml of 5 mg/ml protein and 5 mM DTT with 0.001 ml reservoir solution containing 20% w/v 2-propanol, 20% w/v PEG 4000, 0.1 M sodium citrate tribasic, pH 5.6, for the apoenzyme, and 20% w/v PEG 3350, 0.2 M ammonium citrate tribasic, pH 7.0, for the enzyme complex, equilibration against 0.1 ml reservoir solution, 1-7 days, X-ray diffraction structure determination and analysis at 2.2-2.4 A resolution, single-wavelength anomalous dispersion phasing method
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant expression of N-terminally His-tagged truncated enzyme Coq5-DELTAN26 in Escherichia coli BL21(DE3) by nickel affinity chromatography and gel filtration
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
BoCOQ5-2 partially complements the yeast coq5 mutant. Escherichia coli cells expressing BoCOQ5-2 exhibit a greater than 3fold increase in total ubiquinone content in comparison with the vector-only control
expression in Escherichia coli
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gene COQ5 or YML110C, recombinant expression of N-terminally His-tagged truncated enzyme Coq5-DELTAN26 in Escherichia coli BL21(DE3), selenomethionine-labelled Coq5 protein is overexpressed in Escherichia coli strain B834 (DE3)
the COQ5 gene, when introduced into Escherichia coli, complements the respiratory deficiency of an ubiE mutant that maps near o251, suggesting that it is the yeast homolog of the ubiE gene product
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the gene encoding human COQ5 spans to 26 kb on chromosome 12q24.31 and is comprised of seven exons, HEK-293 cells are co-transfected with the pCOQ5-myc and pCOQ4-V5, expression of a COQ5-GFP construct in HeLa cells, construction of a hybrid yeast-human COQ5 (yhCOQ5) gene by amplifying a 5' segment of yCOQ5, corresponding to the mitochondrial targeting region (encoding aa 1-54) and the 3' of human COQ5
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
COQ5 gene expression is differentially upregulated by glycerol and oleate. The oleate response is controlled by the Rtg family of transcription factors
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the regulation of COQ5 gene expression by carbon source is multifactorial and involves the interaction of various transcription factors. Hap2p modulated the response to oleic acid
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transcription factor Mig1p represses COQ5 expression on dextrose
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transcription factor Rtg1p/Rtg3p heterodimer up-regulates COQ5 expression on oleic acid
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D142G
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Escherichia coli strains containing either the disruption of open reading frame in this region o251 or the point mutation in ubiE accumulated 2-octaprenyl-6-methoxy-1,4-benzoquinone and demethylmenaquinone as predominant intermediates
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
environmental protection
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BoCOQ5-2 methyltransferase is a facilitator of selenium volatilization, biologically based selenium volatilization is a particular area of interest for its potential in making detoxification of selenium pollution highly effective
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