Enzyme

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     2. Transferases
        2.1 Transferring one-carbon groups
            2.1.1 Methyltransferases
ID:2.1.1.9
Description:Thiol S-methyltransferase.
Cath: 3.40.50.150;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 2.1.1.9
BRENDA Enzyme Link: BRENDA 2.1.1.9
KEGG Enzyme Link: KEGG2.1.1.9
BioCyc Enzyme Link: BioCyc 2.1.1.9
ExPASy Enzyme Link: ExPASy2.1.1.9
EC2PDB Enzyme Link: EC2PDB 2.1.1.9
ExplorEnz Enzyme Link: ExplorEnz 2.1.1.9
PRIAM enzyme-specific profiles Link: PRIAM 2.1.1.9
IntEnz Enzyme Link: IntEnz 2.1.1.9
MEDLINE Enzyme Link: MEDLINE 2.1.1.9
MSA:

2.1.1.9;

Phylogenetic Tree:

2.1.1.9;

Uniprot:
M-CSA:
RHEA:18277 a thiol + S-adenosyl-L-methionine = a methyl thioether + H(+) + S-adenosyl-L-homocysteine
RULE(radius=1) [*:1]-[S+;H0:2](-[*:3])-[CH3;+0:4].[*:5]-[SH;+0:6]>>[*:1]-[S;H0;+0:2]-[*:3].[*:5]-[S;H0;+0:6]-[CH3;+0:4]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Purification and characterization of rat liver microsomal thiol methyltransferase.Borchardt RT, Cheng CF1978 Feb 10623768
Thiol S-methyltransferase from rat liver.Weisiger RA, Jakoby WB1979 Sep485170
Arabidopsis HARMLESS TO OZONE LAYER protein methylates a glucosinolate breakdown product and functions in resistance to Pseudomonas syringae pv. maculicola.Nagatoshi Y, Nakamura T2009 Jul 1719419967