EC number:2.1.1.265

Enzyme

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EC Tree
     2. Transferases
        2.1 Transferring one-carbon groups
            2.1.1 Methyltransferases
ID:2.1.1.265
Description:Tellurite methyltransferase.
Cath: 3.40.50.150;

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 2.1.1.265
BRENDA Enzyme Link: BRENDA 2.1.1.265
KEGG Enzyme Link: KEGG2.1.1.265
BioCyc Enzyme Link: BioCyc 2.1.1.265
ExPASy Enzyme Link: ExPASy2.1.1.265
EC2PDB Enzyme Link: EC2PDB 2.1.1.265
ExplorEnz Enzyme Link: ExplorEnz 2.1.1.265
PRIAM enzyme-specific profiles Link: PRIAM 2.1.1.265
IntEnz Enzyme Link: IntEnz 2.1.1.265
MEDLINE Enzyme Link: MEDLINE 2.1.1.265

EC number:2.1.1.265

MSA:

2.1.1.265;
Phylogenetic Tree:

2.1.1.265;
Uniprot:
M-CSA:
RHEA:34539 S-adenosyl-L-methionine + tellurite = methanetellurite + S-adenosyl-L-homocysteine
RULE(radius=1) [*:1]-[S+;H0:2](-[*:3])-[CH3;+0:4].[*:5]=[Te+2;H0:6](-[*:7])-[OH;+0:8]>>[*:1]-[S;H0;+0:2]-[*:3].[*:5]=[Te+4;H0:6](-[*:7])(-[CH3;+0:4])=[O;H0;+0:8]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Structure and mechanism of the chalcogen-detoxifying protein TehB from Escherichia coli.Choudhury HG, Cameron AD, Iwata S, Beis K2011 Apr 121244361