EC number:2.1.1.145

Enzyme

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     2. Transferases
        2.1 Transferring one-carbon groups
            2.1.1 Methyltransferases
ID:2.1.1.145
Description:Trans-aconitate 3-methyltransferase.
Cath: 1.10.150.290; 3.40.50.150;

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 2.1.1.145
BRENDA Enzyme Link: BRENDA 2.1.1.145
KEGG Enzyme Link: KEGG2.1.1.145
BioCyc Enzyme Link: BioCyc 2.1.1.145
ExPASy Enzyme Link: ExPASy2.1.1.145
EC2PDB Enzyme Link: EC2PDB 2.1.1.145
ExplorEnz Enzyme Link: ExplorEnz 2.1.1.145
PRIAM enzyme-specific profiles Link: PRIAM 2.1.1.145
IntEnz Enzyme Link: IntEnz 2.1.1.145
MEDLINE Enzyme Link: MEDLINE 2.1.1.145

EC number:2.1.1.145

MSA:

2.1.1.145;
Phylogenetic Tree:

2.1.1.145;
Uniprot:
M-CSA:
RHEA:22200 S-adenosyl-L-methionine + trans-aconitate = (E)-2-(methoxycarbonylmethyl)but-2-enedioate + 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
3-Isopropylmalate is the major endogenous substrate of the Saccharomyces cerevisiae trans-aconitate methyltransferase.Katz JE, Dumlao DS, Wasserman JI, Lansdown MG, Jung ME, Faull KF, Clarke S2004 May 2515147181
Identification of the gene and characterization of the activity of the trans-aconitate methyltransferase from Saccharomyces cerevisiae.Cai H, Dumlao D, Katz JE, Clarke S2001 Nov 1311695919
Distinct reactions catalyzed by bacterial and yeast trans-aconitate methyltransferases.Cai H, Strouse J, Dumlao D, Jung ME, Clarke S2001 Feb 2011329290
A novel methyltransferase catalyzes the methyl esterification of trans-aconitate in Escherichia coli.Cai H, Clarke S1999 May 710224113