EC number:2.1.1.114

Enzyme

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     2. Transferases
        2.1 Transferring one-carbon groups
            2.1.1 Methyltransferases
ID:2.1.1.114
Description:Polyprenyldihydroxybenzoate methyltransferase.
Alternative Name: Dihydroxyhexaprenylbenzoate methyltransferase.
DHHB-Mt.
DHHB O-methyltransferase.
DHHB methyltransferase.
3,4-dihydroxy-5-hexaprenylbenzoate methyltransferase.
Cath: 3.40.50.150;

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 2.1.1.114
BRENDA Enzyme Link: BRENDA 2.1.1.114
KEGG Enzyme Link: KEGG2.1.1.114
BioCyc Enzyme Link: BioCyc 2.1.1.114
ExPASy Enzyme Link: ExPASy2.1.1.114
EC2PDB Enzyme Link: EC2PDB 2.1.1.114
ExplorEnz Enzyme Link: ExplorEnz 2.1.1.114
PRIAM enzyme-specific profiles Link: PRIAM 2.1.1.114
IntEnz Enzyme Link: IntEnz 2.1.1.114
MEDLINE Enzyme Link: MEDLINE 2.1.1.114

EC number:2.1.1.114

MSA:

2.1.1.114;
Phylogenetic Tree:

2.1.1.114;
Uniprot:
M-CSA:
RHEA:14121 3,4-dihydroxy-5-all-trans-hexaprenylbenzoate + S-adenosyl-L-methionine = 3-methoxy-4-hydroxy-5-all-trans-hexaprenylbenzoate + H(+) + S-adenosyl-L-homocysteine
RULE(radius=1) [*:1]-[OH;+0:2].[*:3]-[S+;H0:4](-[*:5])-[CH3;+0:6]>>[*:1]-[O;H0;+0:2]-[CH3;+0:6].[*:3]-[S;H0;+0:4]-[*:5]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction
RHEA:44452 3,4-dihydroxy-5-all-trans-polyprenylbenzoate + S-adenosyl-L-methionine = 3-methoxy,4-hydroxy-5-all-trans-polyprenylbenzoate + H(+) + S-adenosyl-L-homocysteine
RULE(radius=1) [*:1]-[OH;+0:2].[*:3]-[S+;H0:4](-[*:5])-[CH3;+0:6]>>[*:1]-[O;H0;+0:2]-[CH3;+0:6].[*:3]-[S;H0;+0:4]-[*:5]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Isolation and functional expression of human COQ3, a gene encoding a methyltransferase required for ubiquinone biosynthesis.Jonassen T, Clarke CF2000 Apr 2810777520
Yeast and rat Coq3 and Escherichia coli UbiG polypeptides catalyze both O-methyltransferase steps in coenzyme Q biosynthesis.Poon WW, Barkovich RJ, Hsu AY, Frankel A, Lee PT, Shepherd JN, Myles DC, Clarke CF1999 Jul 3010419476
RHEA:44480 3,4-dihydroxy-5-all-trans-heptaprenylbenzoate + S-adenosyl-L-methionine = 3-methoxy-4-hydroxy-5-all-trans-heptaprenylbenzoate + H(+) + S-adenosyl-L-homocysteine
RULE(radius=1) [*:1]-[OH;+0:2].[*:3]-[S+;H0:4](-[*:5])-[CH3;+0:6]>>[*:1]-[O;H0;+0:2]-[CH3;+0:6].[*:3]-[S;H0;+0:4]-[*:5]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction
RHEA:44484 3,4-dihydroxy-5-all-trans-octaprenylbenzoate + S-adenosyl-L-methionine = 3-methoxy-4-hydroxy-5-all-trans-octaprenylbenzoate + H(+) + S-adenosyl-L-homocysteine
RULE(radius=1) [*:1]-[OH;+0:2].[*:3]-[S+;H0:4](-[*:5])-[CH3;+0:6]>>[*:1]-[O;H0;+0:2]-[CH3;+0:6].[*:3]-[S;H0;+0:4]-[*:5]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction
RHEA:44488 3,4-dihydroxy-5-all-trans-nonaprenylbenzoate + S-adenosyl-L-methionine = 3-methoxy-4-hydroxy-5-all-trans-nonaprenylbenzoate + H(+) + S-adenosyl-L-homocysteine
RULE(radius=1) [*:1]-[OH;+0:2].[*:3]-[S+;H0:4](-[*:5])-[CH3;+0:6]>>[*:1]-[O;H0;+0:2]-[CH3;+0:6].[*:3]-[S;H0;+0:4]-[*:5]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Yeast and rat Coq3 and Escherichia coli UbiG polypeptides catalyze both O-methyltransferase steps in coenzyme Q biosynthesis.Poon WW, Barkovich RJ, Hsu AY, Frankel A, Lee PT, Shepherd JN, Myles DC, Clarke CF1999 Jul 3010419476
RHEA:44492 3,4-dihydroxy-5-all-trans-decaprenylbenzoate + S-adenosyl-L-methionine = 3-methoxy-4-hydroxy-5-all-trans-decaprenylbenzoate + H(+) + S-adenosyl-L-homocysteine
RULE(radius=1) [*:1]-[OH;+0:2].[*:3]-[S+;H0:4](-[*:5])-[CH3;+0:6]>>[*:1]-[O;H0;+0:2]-[CH3;+0:6].[*:3]-[S;H0;+0:4]-[*:5]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Isolation and functional expression of human COQ3, a gene encoding a methyltransferase required for ubiquinone biosynthesis.Jonassen T, Clarke CF2000 Apr 2810777520