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 (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 | 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 | 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 | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | P49017 | gene COQ5 or YML110C | - |
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 | 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 | 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 | Comment | Organism |
---|---|---|
dimer | - |
Saccharomyces cerevisiae |
Synonyms | Comment | Organism |
---|---|---|
C-methyltransferase Coq5 | - |
Saccharomyces cerevisiae |
COQ5 | - |
Saccharomyces cerevisiae |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Saccharomyces cerevisiae |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
assay at | Saccharomyces cerevisiae |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
S-adenosyl-L-methionine | - |
Saccharomyces cerevisiae |
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 |