Biology:Homocysteine S-methyltransferase
| Homocysteine S-methyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 2.1.1.10 | ||||||||
| CAS number | 9012-40-2 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
Homocysteine S-methyltransferase (EC 2.1.1.10) is an enzyme that catalyzes the chemical reaction
- REDIRECT Template:Chemical reaction
A methyl group is transferred from S-methyl-L-methioninate to L-homocysteine, forming two molecules of the amino acid, L-methionine.[1][2][3] The methyl group can also be transferred from S-adenosyl methionine but in plants this is less preferred than from S-methyl-L-methioninate.[4][5]
Alternative names
The systematic name of this enzyme class is S-adenosyl-L-methionine:L-homocysteine S-methyltransferase. Other names in use include S-adenosylmethionine homocysteine transmethylase, S-methylmethionine homocysteine transmethylase, adenosylmethionine transmethylase, methylmethionine:homocysteine methyltransferase, adenosylmethionine:homocysteine methyltransferase, homocysteine methylase, homocysteine methyltransferase, homocysteine transmethylase, L-homocysteine S-methyltransferase, S-adenosyl-L-methionine:L-homocysteine methyltransferase, S-adenosylmethionine-homocysteine transmethylase, and S-adenosylmethionine:homocysteine methyltransferase.[6]
References
- ↑ "Methionine biosynthesis in Escherichia coli: induction and repression of methylmethionine(or adenosylmethionine):homocysteine methyltransferase". Arch. Biochem. Biophys. 119 (1): 62–8. 1967. doi:10.1016/0003-9861(67)90429-8. PMID 4861151.
- ↑ Shapiro SK (1958). "Adenosylmethionine-homocysteine transmethylase". Biochim. Biophys. Acta 29 (2): 405–409. doi:10.1016/0006-3002(58)90199-9. PMID 13572358.
- ↑ Shapiro SK; Yphantis DA (1959). "Assay of S-methylmethionine and S-adenosylmethionine homocysteine transmethylases". Biochim. Biophys. Acta 36: 241–244. doi:10.1016/0006-3002(59)90089-7. PMID 14445542.
- ↑ Ranocha, Philippe; McNeil, Scott D.; Ziemak, Michael J.; Li, Changjiang; Tarczynski, Mitchell C.; Hanson, Andrew D. (2001). "The S -methylmethionine cycle in angiosperms: Ubiquity, antiquity and activity". The Plant Journal 25 (5): 575–584. doi:10.1046/j.1365-313x.2001.00988.x. PMID 11309147.
- ↑ Ranocha, Philippe; Bourgis, Fabienne; Ziemak, Michael J.; Rhodes, David; Gage, Douglas A.; Hanson, Andrew D. (2000). "Characterization and Functional Expression of cDNAs Encoding Methionine-sensitive and -insensitive Homocysteine S-Methyltransferases from Arabidopsis". Journal of Biological Chemistry 275 (21): 15962–15968. doi:10.1074/jbc.M001116200. PMID 10747987.
- ↑ Enzyme 2.1.1.10 at KEGG Pathway Database.
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