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Information on EC 2.1.1.201 - 2-methoxy-6-polyprenyl-1,4-benzoquinol methylase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P49017

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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, when the COQ5 gene from Saccharomyces cerevisiae is introduced into Escherichia coli, it complements the respiratory deficiency of an ubiE mutant . The bifunctional enzyme from Escherichia coli also catalyses the methylation of demethylmenaquinol-8 (this activity is classified as EC 2.1.1.163) .
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Saccharomyces cerevisiae
UNIPROT: P49017
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The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
bocoq5-2, bocoq5-2 methyltransferase, coq5 methyltransferase, 2-hexaprenyl-6-methoxy-1,4-benzoquinone methyltransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2-hexaprenyl-6-methoxy-1,4-benzoquinone methyltransferase
-
C-methyltransferase Coq5
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Coq5 C-methyltransferase
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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
a putative catalytic mechanism of Coq5 is proposed in which Arg201 acts as a general base to initiate catalysis with the help of a water molecule, Arg201 abstracts a proton from the water molecule
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].
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
?
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 + 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
-
-
-
?
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
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADH
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
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
peripherally associated with the inner mitochondrial membrane on the matrix side
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
deletion of the chromosomal COQ5 gene results in a respiration deficiency and reduced levels of respiratory protein components
metabolism
Coq5 is an S-adenosyl methionine-dependent methyltransferase (SAM-MTase) that catalyzes the only C-methylation step in the coenzyme Q (CoQ) biosynthesis pathway, in which 2-methoxy-6-polyprenyl-1,4-benzoquinone (DDMQH2) is converted to 2-methoxy-5-methyl-6-polyprenyl-1,4-benzoquinone
physiological function
Coq5p catalyzes a step in ubiquinone biosynthesis and is essential for the stability and activity of other Coq polypeptides involved in Q biosynthesis (Coq3 and Coq4)
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
34685
x * 34685, calculated from sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 34685, calculated from sequence
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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
expression in Escherichia coli
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
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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hagerman, R.A.; Willis, R.A.
The yeast gene COQ5 is differentially regulated by Mig1p, Rtg3p and Hap2p
Biochim. Biophys. Acta
1578
51-58
2002
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Hagerman, R.A.; Trotter, P.J.; Willis, R.A.
The regulation of COQ5 gene expression by energy source
Free Radic. Res.
36
485-490
2002
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Dibrov, E.; Robinson, K.M.; Lemire, B.D.
The COQ5 gene encodes a yeast mitochondrial protein necessary for ubiquinone biosynthesis and the assembly of the respiratory chain
J. Biol. Chem.
272
9175-9181
1997
Saccharomyces cerevisiae (P49017), Saccharomyces cerevisiae
Manually annotated by BRENDA team
Barkovich, R.J.; Shtanko, A.; Shepherd, J.A.; Lee, P.T.; Myles, D.C.; Tzagoloff, A.; Clarke, C.F.
Characterization of the COQ5 gene from Saccharomyces cerevisiae. Evidence for a C-methyltransferase in ubiquinone biosynthesis
J. Biol. Chem.
272
9182-918
1997
Saccharomyces cerevisiae (P49017)
Manually annotated by BRENDA team
Baba, S.W.; Belogrudov, G.I.; Lee, J.C.; Lee, P.T.; Strahan, J.; Shepherd, J.N.; Clarke, C.F.
Yeast Coq5 C-methyltransferase is required for stability of other polypeptides involved in coenzyme Q biosynthesis
J. Biol. Chem.
279
10052-10059
2004
Saccharomyces cerevisiae (P49017), Saccharomyces cerevisiae
Manually annotated by BRENDA team
Dai, Y.N.; Zhou, K.; Cao, D.D.; Jiang, Y.L.; Meng, F.; Chi, C.B.; Ren, Y.M.; Chen, Y.; Zhou, C.Z.
Crystal structures and catalytic mechanism of the C-methyltransferase Coq5 provide insights into a key step of the yeast coenzyme Q synthesis pathway
Acta Crystallogr. Sect. D
70
2085-2092
2014
Saccharomyces cerevisiae (P49017), Saccharomyces cerevisiae
Manually annotated by BRENDA team