Sterol 24-C-methyltransferase
| sterol 24-C-methyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.1.1.41 | ||||||||
| CAS no. | 37257-07-1 | ||||||||
| 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 | ||||||||
| |||||||||
 | This article includes a list of general references, but it lacks sufficient corresponding inline citations. (October 2021) |
In enzymology, a sterol 24-C-methyltransferase (EC 2.1.1.41) is an enzyme that catalyzes the chemical reaction
- S-adenosyl-L-methionine + 5alpha-cholesta-8,24-dien-3beta-ol S-adenosyl-L-homocysteine + 24-methylene-5alpha-cholest-8-en-3beta-ol
Thus, the two substrates of this enzyme are S-adenosyl methionine and 5alpha-cholesta-8,24-dien-3beta-ol, whereas its two products are S-adenosylhomocysteine and 24-methylene-5alpha-cholest-8-en-3beta-ol.
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:zymosterol 24-C-methyltransferase. Other names in common use include Delta24-methyltransferase, Delta24-sterol methyltransferase, zymosterol-24-methyltransferase, S-adenosyl-4-methionine:sterol Delta24-methyltransferase, SMT1, 24-sterol C-methyltransferase, S-adenosyl-L-methionine:Delta24(23)-sterol methyltransferase, and phytosterol methyltransferase. This enzyme participates in biosynthesis of steroids. It employs one cofactor, glutathione.
References
[edit]- Moore JT, Gaylor JL (1969). "Isolation and purification of an S-adenosylmethionine: delta 24-sterol methyltransferase from yeast". J. Biol. Chem. 244 (23): 6334–40. PMID 5354959.
- Venkatramesh M, Guo DA, Jia Z, Nes WD (1996). "Mechanism and structural requirements for transformation of substrates by the (S)-adenosyl-L-methionine:delta 24(25)-sterol methyl transferase from Saccharomyces cerevisiae". Biochim. Biophys. Acta. 1299 (3): 313–24. doi:10.1016/0005-2760(95)00218-9. PMID 8597586.
- MD, Zhou W, Lopez M, Nes WD (1997). ", Stereochemical features of C-methylation on the path to Delta24(28)-methylene and Delta24(28)-ethylidene sterols: studies on the recombinant phytosterol methyl transferase from Arabidopsis thaliana". Tetrahedron Lett. 38 (35): 6115–6118. doi:10.1016/S0040-4039(97)01386-5.
- Bouvier-Nave P, Husselstein T, Benveniste P (1998). "Two families of sterol methyltransferases are involved in the first and the second methylation steps of plant sterol biosynthesis". Eur. J. Biochem. 256 (1): 88–96. doi:10.1046/j.1432-1327.1998.2560088.x. PMID 9746350.
- Nes WD, McCourt BS, Zhou WX, Ma J, Marshall JA, Peek LA, Brennan M (1998). "Overexpression, purification, and stereochemical studies of the recombinant (S)-adenosyl-L-methionine: delta 24(25)- to delta 24(28)-sterol methyl transferase enzyme from Saccharomyces cerevisiae". Arch. Biochem. Biophys. 353 (2): 297–311. doi:10.1006/abbi.1998.0665. PMID 9606964.
