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Literature summary for 2.1.1.201 extracted from

  • 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 (2014), Acta Crystallogr. Sect. D, 70, 2085-2092.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
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) Saccharomyces cerevisiae

Crystallization (Commentary)

Crystallization (Comment) Organism
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 Saccharomyces cerevisiae

Protein Variants

Protein Variants Comment Organism
additional information construction of an N-terminally His-tagged truncated enzyme lacking the signal peptide Met1-Ala26, termed Coq5-DELTAN26 Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
S-adenosyl-L-methionine + 2-methoxy-6-all-trans-polyprenyl-1,4-benzoquinol Saccharomyces cerevisiae
-
S-adenosyl-L-homocysteine + 6-methoxy-3-methyl-2-all-trans-polyprenyl-1,4-benzoquinol
-
?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae P49017 gene COQ5 or YML110C
-

Purification (Commentary)

Purification (Comment) Organism
recombinant expression of N-terminally His-tagged truncated enzyme Coq5-DELTAN26 in Escherichia coli BL21(DE3) by nickel affinity chromatography and gel filtration Saccharomyces cerevisiae

Reaction

Reaction Comment Organism Reaction ID
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 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 Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-adenosyl-L-methionine + 2-methoxy-6-all-trans-polyprenyl-1,4-benzoquinol
-
Saccharomyces cerevisiae S-adenosyl-L-homocysteine + 6-methoxy-3-methyl-2-all-trans-polyprenyl-1,4-benzoquinol
-
?

Subunits

Subunits Comment Organism
dimer
-
Saccharomyces cerevisiae

Synonyms

Synonyms Comment Organism
C-methyltransferase Coq5
-
Saccharomyces cerevisiae
COQ5
-
Saccharomyces cerevisiae

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Saccharomyces cerevisiae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
assay at Saccharomyces cerevisiae

Cofactor

Cofactor Comment Organism Structure
S-adenosyl-L-methionine
-
Saccharomyces cerevisiae

General Information

General Information Comment Organism
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 Saccharomyces cerevisiae
additional information Coq5 displays a typical class I SAM-MTase structure with two minor variations beyond the core domain, both of which are considered to participate in dimerization and/or substrate recognition. Slight conformational changes at the active-site pocket are observed upon binding of SAM. Remodelling of the substrate-binding site, structure-based computational simulation, overview Saccharomyces cerevisiae