BRENDA - Enzyme Database show
show all sequences of 2.1.1.114

Isolation and functional expression of human COQ3, a gene encoding a methyltransferase required for ubiquinone biosynthesis

Jonassen, T.; Clarke, C.F.; J. Biol. Chem. 275, 12381-12387 (2000)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
when expressed in multicopy, the human construct rescues the growth of a yeast coq3 null mutant on a nonfermentable carbon source and restores coenzyme Q biosynthesis, although at lower levels than that of wild type yeast
Homo sapiens
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
40998
-
x * 40998, calculated from sequence
Homo sapiens
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
S-adenosyl-L-methionine + 5-all-trans-decaprenyl-3,4-dihydroxybenzoate
Homo sapiens
the enzyme catalyzes two methylation steps in the biosynthesis of ubiquinone-10, 1. the methylation of 5-all-trans-decaprenyl-3,4-dihydroxybenzoate and 2. the methylation of 3-demethylubiquinol-10 (this reaction is classified as EC 2.1.1.64)
S-adenosyl-L-homocysteine + 5-all-trans-decaprenyl-4-hydroxy-3-methoxybenzoate
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Homo sapiens
Q9NZJ6
-
-
Source Tissue
Source Tissue
Commentary
Organism
Textmining
heart
-
Homo sapiens
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
wide substrate specificity. The enzyme methylates both eukaryotic substrates demethylubiquinol-3 (this activity is classified as EC 2.1.1.64) and 3,4-dihydroxy-5-farnesylbenzoic acid and the distinct prokaryotic substrate 3-((2E,6E)-farnesyl)benzene-1,2-diol
485141
Homo sapiens
?
-
-
-
-
S-adenosyl-L-methionine + 3,4-dihydroxy-5-(2E,6E)-farnesylbenzoate
in vitro assay
485141
Homo sapiens
S-adenosyl-L-homocysteine + 5-(2E,6E)-farnesyl-4-hydroxy-3-methoxybenzoate
-
-
-
?
S-adenosyl-L-methionine + 3,4-dihydroxy-5-all-trans-hexaprenylbenzoate
3,4-dihydroxy-5-all-trans-hexaprenylbenzoate is an intermediate in biosynthesis of ubiquinone-6 in Saccharomyces cerevisiae (that is methylated by the yeast enzyme CoQ3 to 4-hydroxy-3-methoxy-5-hexaprenylbenzoate). When expressed in multicopy, the human construct rescues the growth of a yeast coq3 null mutant on a nonfermentable carbon source and restores coenzyme Q biosynthesis, although at lower levels than that of wild type yeast
485141
Homo sapiens
S-adenosyl-L-homocysteine + 5-all-trans-hexaprenyl-4-hydroxy-3-methoxybenzoate
-
-
-
?
S-adenosyl-L-methionine + 5-all-trans-decaprenyl-3,4-dihydroxybenzoate
the enzyme catalyzes two methylation steps in the biosynthesis of ubiquinone-10, 1. the methylation of 5-all-trans-decaprenyl-3,4-dihydroxybenzoate and 2. the methylation of 3-demethylubiquinol-10 (this reaction is classified as EC 2.1.1.64)
485141
Homo sapiens
S-adenosyl-L-homocysteine + 5-all-trans-decaprenyl-4-hydroxy-3-methoxybenzoate
-
-
-
?
Subunits
Subunits
Commentary
Organism
?
x * 40998, calculated from sequence
Homo sapiens
Cloned(Commentary) (protein specific)
Commentary
Organism
when expressed in multicopy, the human construct rescues the growth of a yeast coq3 null mutant on a nonfermentable carbon source and restores coenzyme Q biosynthesis, although at lower levels than that of wild type yeast
Homo sapiens
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
40998
-
x * 40998, calculated from sequence
Homo sapiens
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 + 5-all-trans-decaprenyl-3,4-dihydroxybenzoate
Homo sapiens
the enzyme catalyzes two methylation steps in the biosynthesis of ubiquinone-10, 1. the methylation of 5-all-trans-decaprenyl-3,4-dihydroxybenzoate and 2. the methylation of 3-demethylubiquinol-10 (this reaction is classified as EC 2.1.1.64)
S-adenosyl-L-homocysteine + 5-all-trans-decaprenyl-4-hydroxy-3-methoxybenzoate
-
-
?
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
heart
-
Homo sapiens
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
wide substrate specificity. The enzyme methylates both eukaryotic substrates demethylubiquinol-3 (this activity is classified as EC 2.1.1.64) and 3,4-dihydroxy-5-farnesylbenzoic acid and the distinct prokaryotic substrate 3-((2E,6E)-farnesyl)benzene-1,2-diol
485141
Homo sapiens
?
-
-
-
-
S-adenosyl-L-methionine + 3,4-dihydroxy-5-(2E,6E)-farnesylbenzoate
in vitro assay
485141
Homo sapiens
S-adenosyl-L-homocysteine + 5-(2E,6E)-farnesyl-4-hydroxy-3-methoxybenzoate
-
-
-
?
S-adenosyl-L-methionine + 3,4-dihydroxy-5-all-trans-hexaprenylbenzoate
3,4-dihydroxy-5-all-trans-hexaprenylbenzoate is an intermediate in biosynthesis of ubiquinone-6 in Saccharomyces cerevisiae (that is methylated by the yeast enzyme CoQ3 to 4-hydroxy-3-methoxy-5-hexaprenylbenzoate). When expressed in multicopy, the human construct rescues the growth of a yeast coq3 null mutant on a nonfermentable carbon source and restores coenzyme Q biosynthesis, although at lower levels than that of wild type yeast
485141
Homo sapiens
S-adenosyl-L-homocysteine + 5-all-trans-hexaprenyl-4-hydroxy-3-methoxybenzoate
-
-
-
?
S-adenosyl-L-methionine + 5-all-trans-decaprenyl-3,4-dihydroxybenzoate
the enzyme catalyzes two methylation steps in the biosynthesis of ubiquinone-10, 1. the methylation of 5-all-trans-decaprenyl-3,4-dihydroxybenzoate and 2. the methylation of 3-demethylubiquinol-10 (this reaction is classified as EC 2.1.1.64)
485141
Homo sapiens
S-adenosyl-L-homocysteine + 5-all-trans-decaprenyl-4-hydroxy-3-methoxybenzoate
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 40998, calculated from sequence
Homo sapiens
Other publictions for EC 2.1.1.114
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)
733306
Zhu
Structural and biochemical stu ...
Escherichia coli, Homo sapiens
Biochem. J.
470
105-114
2015
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2
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2
1
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2
2
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733930
Gomez
Restoring de novo coenzyme Q b ...
Caenorhabditis elegans, Caenorhabditis elegans N2
Gene
506
106-116
2012
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18
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1
1
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704413
Marbois
Lee, P.T.; Strahan, J.; Shephe ...
Saccharomyces cerevisiae
J. Biol. Chem.
280
20231-20238
2005
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3
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485141
Jonassen
Isolation and functional expre ...
Homo sapiens
J. Biol. Chem.
275
12381-12387
2000
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-
1
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-
1
1
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1
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1
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4
1
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1
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1
1
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1
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4
1
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485140
Poon
Yeast and rat Coq3 and Escheri ...
Rattus norvegicus, Saccharomyces cerevisiae
J. Biol. Chem.
274
21665-21672
1999
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1
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1
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2
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8
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4
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2
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1
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4
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2
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485139
Avelange-Macheral
Cloning and functional express ...
Arabidopsis thaliana
Plant J.
14
203-213
1998
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703840
Marbois
Cloning of a rat cDNA encoding ...
Rattus norvegicus
Gene
138
213-217
1994
-
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1
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4
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485138
Clarke
Ubiquinone biosynthesis in Sac ...
Saccharomyces cerevisiae
J. Biol. Chem.
266
16636-16644
1991
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1
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1
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4
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1
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1
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