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show all sequences of 2.1.1.201

Crystal structures and catalytic mechanism of the C-methyltransferase Coq5 provide insights into a key step of the yeast coenzyme Q synthesis pathway

Dai, Y.N.; Zhou, K.; Cao, D.D.; Jiang, Y.L.; Meng, F.; Chi, C.B.; Ren, Y.M.; Chen, Y.; Zhou, C.Z.; Acta Crystallogr. Sect. D 70, 2085-2092 (2014)

Data extracted from this reference:

Cloned(Commentary)
Commentary
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
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
Engineering
Amino acid exchange
Commentary
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
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
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
Primary Accession No. (UniProt)
Commentary
Textmining
Saccharomyces cerevisiae
P49017
gene COQ5 or YML110C
-
Purification (Commentary)
Commentary
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
Commentary
Organism
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
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
S-adenosyl-L-methionine + 2-methoxy-6-all-trans-polyprenyl-1,4-benzoquinol
-
735364
Saccharomyces cerevisiae
S-adenosyl-L-homocysteine + 6-methoxy-3-methyl-2-all-trans-polyprenyl-1,4-benzoquinol
-
-
-
?
Subunits
Subunits
Commentary
Organism
dimer
-
Saccharomyces cerevisiae
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
assay at
Saccharomyces cerevisiae
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
assay at
Saccharomyces cerevisiae
Cofactor
Cofactor
Commentary
Organism
Structure
S-adenosyl-L-methionine
-
Saccharomyces cerevisiae
Cloned(Commentary) (protein specific)
Commentary
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
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
S-adenosyl-L-methionine
-
Saccharomyces cerevisiae
Crystallization (Commentary) (protein specific)
Crystallization
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
Engineering (protein specific)
Amino acid exchange
Commentary
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) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
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
-
-
?
Purification (Commentary) (protein specific)
Commentary
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
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
S-adenosyl-L-methionine + 2-methoxy-6-all-trans-polyprenyl-1,4-benzoquinol
-
735364
Saccharomyces cerevisiae
S-adenosyl-L-homocysteine + 6-methoxy-3-methyl-2-all-trans-polyprenyl-1,4-benzoquinol
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
dimer
-
Saccharomyces cerevisiae
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
assay at
Saccharomyces cerevisiae
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
assay at
Saccharomyces cerevisiae
General Information
General Information
Commentary
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
General Information (protein specific)
General Information
Commentary
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
Other publictions for EC 2.1.1.201
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
735364
Dai
Crystal structures and catalyt ...
Saccharomyces cerevisiae
Acta Crystallogr. Sect. D
70
2085-2092
2014
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735704
Nguyen
Molecular characterization of ...
Homo sapiens
Biochim. Biophys. Acta
1841
1628-1638
2014
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720768
Zhou
Think outside the box: seleniu ...
Brassica oleracea
Plant Signal. Behav.
5
76-77
2010
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3
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706320
Zhou
Involvement of a broccoli COQ5 ...
Brassica oleracea
Plant Physiol.
151
528-540
2009
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704408
Baba
Yeast Coq5 C-methyltransferase ...
Saccharomyces cerevisiae
J. Biol. Chem.
279
10052-10059
2004
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702398
Hagerman
The yeast gene COQ5 is differe ...
Saccharomyces cerevisiae
Biochim. Biophys. Acta
1578
51-58
2002
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3
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3
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703812
Hagerman
The regulation of COQ5 gene ex ...
Saccharomyces cerevisiae
Free Radic. Res.
36
485-490
2002
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698549
Lee
A C-methyltransferase involved ...
Escherichia coli
J. Bacteriol.
179
1748-1754
1997
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704387
Dibrov
The COQ5 gene encodes a yeast ...
Saccharomyces cerevisiae
J. Biol. Chem.
272
9175-9181
1997
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704388
Barkovich
Characterization of the COQ5 g ...
Saccharomyces cerevisiae
J. Biol. Chem.
272
9182-918
1997
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704239
Young
Characterization and genetic a ...
Escherichia coli K-12
J. Bacteriol.
105
769-778
1971
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