EC number:2.1.1.280

Enzyme

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     2. Transferases
        2.1 Transferring one-carbon groups
            2.1.1 Methyltransferases
ID:2.1.1.280
Description:Selenocysteine Se-methyltransferase.

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 2.1.1.280
BRENDA Enzyme Link: BRENDA 2.1.1.280
KEGG Enzyme Link: KEGG2.1.1.280
BioCyc Enzyme Link: BioCyc 2.1.1.280
ExPASy Enzyme Link: ExPASy2.1.1.280
EC2PDB Enzyme Link: EC2PDB 2.1.1.280
ExplorEnz Enzyme Link: ExplorEnz 2.1.1.280
PRIAM enzyme-specific profiles Link: PRIAM 2.1.1.280
IntEnz Enzyme Link: IntEnz 2.1.1.280
MEDLINE Enzyme Link: MEDLINE 2.1.1.280

EC number:2.1.1.280

MSA:

2.1.1.280;
Phylogenetic Tree:

2.1.1.280;
Uniprot:
M-CSA:
RHEA:26341 L-selenocysteine + S-methyl-L-methionine = H(+) + L-methionine + Se-methyl-L-selenocysteine
RULE(radius=1) [*:1]-[S+;H0:2](-[*:3])-[CH3;+0:4].[*:5]-[SeH;+0:6]>>[*:1]-[S;H0;+0:2]-[*:3].[*:5]-[Se;H0;+0:6]-[CH3;+0:4]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
On the mechanism of selenium tolerance in selenium-accumulating plants. Purification and characterization of a specific selenocysteine methyltransferase from cultured cells of Astragalus bisculatus.Neuhierl B, Böck A1996 Jul 18706715
Biochemical and molecular characterization of the homocysteine S-methyltransferase from broccoli (Brassica oleracea var. italica).Lyi SM, Zhou X, Kochian LV, Li L2007 Apr17391716
Molecular and biochemical characterization of the selenocysteine Se-methyltransferase gene and Se-methylselenocysteine synthesis in broccoli.Lyi SM, Heller LI, Rutzke M, Welch RM, Kochian LV, Li L2005 May15863700