Homocysteine S-methyltransferase
| homocysteine S-methyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.1.1.10 | ||||||||
| CAS no. | 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 | ||||||||
| |||||||||
In enzymology, a homocysteine S-methyltransferase (EC 2.1.1.10) is an enzyme that catalyzes the chemical reaction
- S-methylmethionine + L-homocysteine 2 L-methionine
Thus, the two substrates of this enzyme are S-methylmethionine and L-homocysteine, and it produces 2 molecules of L-methionine.
This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:L-homocysteine S-methyltransferase. This enzyme participates in methionine metabolism.
Alternative names
[edit]Other names of this enzyme in common 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.
References
[edit]- Balish E, Shapiro SK (1967). "Methionine biosynthesis in Escherichia coli: induction and repression of methylmethionine(or adenosylmethionine):homocysteine methyltransferase". Arch. Biochem. Biophys. 119 (1): 62–8. 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.
