ExplorEnz: EC 2.1.1.280

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2.1.1.280

Accepted name:

selenocysteine Se-methyltransferase

Reaction:

S-methyl-L-methionine + L-selenocysteine = L-methionine + Se-methyl-L-selenocysteine

Other name(s):

SMT

Systematic name:

S-methyl-L-methionine:L-selenocysteine Se-methyltransferase

Comments:

The enzyme uses S-adenosyl-L-methionine as methyl donor less actively than S-methyl-L-methionine. The enzyme from broccoli (Brassica oleracea var. italica) also has the activity of EC 2.1.1.10, homocysteine S-methyltransferase [4].

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Neuhierl, B. and Bock, A. On the mechanism of selenium tolerance in selenium-accumulating plants. Purification and characterization of a specific selenocysteine methyltransferase from cultured cells of Astragalus bisculatus. Eur. J. Biochem. 239 (1996) 235–238. [DOI] [PMID: 8706715]
2.	Neuhierl, B., Thanbichler, M., Lottspeich, F. and Bock, A. A family of S-methylmethionine-dependent thiol/selenol methyltransferases. Role in selenium tolerance and evolutionary relation. J. Biol. Chem. 274 (1999) 5407–5414. [DOI] [PMID: 10026151]
3.	Lyi, S.M., Heller, L.I., Rutzke, M., Welch, R.M., Kochian, L.V. and Li, L. Molecular and biochemical characterization of the selenocysteine Se-methyltransferase gene and Se-methylselenocysteine synthesis in broccoli. Plant Physiol. 138 (2005) 409–420. [DOI] [PMID: 15863700]
4.	Lyi, S.M., Zhou, X., Kochian, L.V. and Li, L. Biochemical and molecular characterization of the homocysteine S-methyltransferase from broccoli (Brassica oleracea var. italica). Phytochemistry 68 (2007) 1112–1119. [DOI] [PMID: 17391716]

[EC 2.1.1.280 created 2013]