BRENDA - Enzyme Database show
show all sequences of 2.1.1.114

Yeast and rat Coq3 and Escherichia coli UbiG polypeptides catalyze both O-methyltransferase steps in coenzyme Q biosynthesis

Poon, W.W.; Barkovich, R.J.; Hsu, A.Y.; Frankel, A.; Lee, P.T.; Sheperd, J.N.; Myles, D.C.; Clarke, C.F.; J. Biol. Chem. 274, 21665-21672 (1999)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
rat COQ3 gene restores O-methyltransferase activity in coq3 null mutant yeast
Rattus norvegicus
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
mitochondrion
the Coq3 polypeptide is peripherally associated with the matrix side of the inner membrane of yeast mitochondria
Saccharomyces cerevisiae
5739
-
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
S-adenosyl-L-methionine + 3,4-dihydroxy-5-hexaprenylbenzoate
Saccharomyces cerevisiae
the enzyme catalyzes two methylation steps in the biosynthesis of ubiquinone-6, 1. the methylation of 3,4-dihydroxy-5-hexaprenylbenzoate and 2. the methylation of 3-demethylubiquinol-6 (this reaction is classified as EC 2.1.1.64)
S-adenosyl-L-homocysteine + 3-methoxy-4-hydroxy-5-hexaprenylbenzoate
-
-
?
S-adenosyl-L-methionine + 3,4-dihydroxy-5-octaprenylbenzoate
Rattus norvegicus
the enzyme catalyzes two methylation steps in the biosynthesis of ubiquinone-8, 1. the methylation of 3,4-dihydroxy-5-octaprenylbenzoate and 2. the methylation of 3-demethylubiquinol-8 (this reaction is classified as EC 2.1.1.64)
S-adenosyl-L-homocysteine + 4-hydroxy-3-methoxy-5-octaprenylbenzoate
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Rattus norvegicus
Q63159
-
-
Saccharomyces cerevisiae
P27680
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
S-adenosyl-L-methionine + 3,4-dihydroxy-5-((2E,6E)-farnesyl)benzoate
-
485140
Rattus norvegicus
S-adenosyl-L-homocysteine + 5-((2E,6E)-farnesyl)-4-hydroxy-3-methoxybenzoate
-
-
-
?
S-adenosyl-L-methionine + 3,4-dihydroxy-5-(2E,6E)-farnesylbenzoate
-
485140
Saccharomyces cerevisiae
S-adenosyl-L-homocysteine + 3-methoxy-4-hydroxy-5-farnesylbenzoate
-
-
-
?
S-adenosyl-L-methionine + 3,4-dihydroxy-5-hexaprenylbenzoate
the enzyme catalyzes two methylation steps in the biosynthesis of ubiquinone-6, 1. the methylation of 3,4-dihydroxy-5-hexaprenylbenzoate and 2. the methylation of 3-demethylubiquinol-6 (this reaction is classified as EC 2.1.1.64)
485140
Saccharomyces cerevisiae
S-adenosyl-L-homocysteine + 3-methoxy-4-hydroxy-5-hexaprenylbenzoate
-
-
-
?
S-adenosyl-L-methionine + 3,4-dihydroxy-5-octaprenylbenzoate
the enzyme catalyzes two methylation steps in the biosynthesis of ubiquinone-8, 1. the methylation of 3,4-dihydroxy-5-octaprenylbenzoate and 2. the methylation of 3-demethylubiquinol-8 (this reaction is classified as EC 2.1.1.64)
485140
Rattus norvegicus
S-adenosyl-L-homocysteine + 4-hydroxy-3-methoxy-5-octaprenylbenzoate
-
-
-
?
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
assay at
Rattus norvegicus
7
-
assay at
Saccharomyces cerevisiae
Cloned(Commentary) (protein specific)
Commentary
Organism
rat COQ3 gene restores O-methyltransferase activity in coq3 null mutant yeast
Rattus norvegicus
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
mitochondrion
the Coq3 polypeptide is peripherally associated with the matrix side of the inner membrane of yeast mitochondria
Saccharomyces cerevisiae
5739
-
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 + 3,4-dihydroxy-5-hexaprenylbenzoate
Saccharomyces cerevisiae
the enzyme catalyzes two methylation steps in the biosynthesis of ubiquinone-6, 1. the methylation of 3,4-dihydroxy-5-hexaprenylbenzoate and 2. the methylation of 3-demethylubiquinol-6 (this reaction is classified as EC 2.1.1.64)
S-adenosyl-L-homocysteine + 3-methoxy-4-hydroxy-5-hexaprenylbenzoate
-
-
?
S-adenosyl-L-methionine + 3,4-dihydroxy-5-octaprenylbenzoate
Rattus norvegicus
the enzyme catalyzes two methylation steps in the biosynthesis of ubiquinone-8, 1. the methylation of 3,4-dihydroxy-5-octaprenylbenzoate and 2. the methylation of 3-demethylubiquinol-8 (this reaction is classified as EC 2.1.1.64)
S-adenosyl-L-homocysteine + 4-hydroxy-3-methoxy-5-octaprenylbenzoate
-
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
S-adenosyl-L-methionine + 3,4-dihydroxy-5-((2E,6E)-farnesyl)benzoate
-
485140
Rattus norvegicus
S-adenosyl-L-homocysteine + 5-((2E,6E)-farnesyl)-4-hydroxy-3-methoxybenzoate
-
-
-
?
S-adenosyl-L-methionine + 3,4-dihydroxy-5-(2E,6E)-farnesylbenzoate
-
485140
Saccharomyces cerevisiae
S-adenosyl-L-homocysteine + 3-methoxy-4-hydroxy-5-farnesylbenzoate
-
-
-
?
S-adenosyl-L-methionine + 3,4-dihydroxy-5-hexaprenylbenzoate
the enzyme catalyzes two methylation steps in the biosynthesis of ubiquinone-6, 1. the methylation of 3,4-dihydroxy-5-hexaprenylbenzoate and 2. the methylation of 3-demethylubiquinol-6 (this reaction is classified as EC 2.1.1.64)
485140
Saccharomyces cerevisiae
S-adenosyl-L-homocysteine + 3-methoxy-4-hydroxy-5-hexaprenylbenzoate
-
-
-
?
S-adenosyl-L-methionine + 3,4-dihydroxy-5-octaprenylbenzoate
the enzyme catalyzes two methylation steps in the biosynthesis of ubiquinone-8, 1. the methylation of 3,4-dihydroxy-5-octaprenylbenzoate and 2. the methylation of 3-demethylubiquinol-8 (this reaction is classified as EC 2.1.1.64)
485140
Rattus norvegicus
S-adenosyl-L-homocysteine + 4-hydroxy-3-methoxy-5-octaprenylbenzoate
-
-
-
?
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
assay at
Rattus norvegicus
7
-
assay at
Saccharomyces cerevisiae
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
1
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2
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2
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2
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2
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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
-
-
1
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-
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2
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18
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2
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2
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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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-
-
-
-
-
-
-
-
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-
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3
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1
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1
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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
-
-
1
-
-
-
-
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1
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2
-
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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1
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3
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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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