sterol 24-C-methyltransferase

{{infobox enzyme

| Name = sterol 24-C-methyltransferase

| EC_number = 2.1.1.41

| CAS_number = 37257-07-1

| GO_code = 0003838

| image =

| width =

| caption =

}}

In enzymology, a sterol 24-C-methyltransferase ({{EC number|2.1.1.41}}) is an enzyme that catalyzes the chemical reaction

:S-adenosyl-L-methionine + 5alpha-cholesta-8,24-dien-3beta-ol $\rightleftharpoons$ 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

{{cite journal | vauthors = Moore JT, Gaylor JL | date = 1969 | title = Isolation and purification of an S-adenosylmethionine: delta 24-sterol methyltransferase from yeast | journal = J. Biol. Chem. | volume = 244 | pages = 6334–40 | pmid = 5354959 | issue = 23 }}
{{cite journal | vauthors = Venkatramesh M, Guo DA, Jia Z, Nes WD | date = 1996 | title = Mechanism and structural requirements for transformation of substrates by the (S)-adenosyl-L-methionine:delta 24(25)-sterol methyl transferase from Saccharomyces cerevisiae | journal = Biochim. Biophys. Acta | volume = 1299 | pages = 313–24 | pmid = 8597586 | issue = 3 | doi = 10.1016/0005-2760(95)00218-9 }}
{{cite journal | vauthors = MD, Zhou W, Lopez M, Nes WD | date = 1997 | title = , 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 | journal = Tetrahedron Lett. | volume = 38 | pages = 6115–6118 | doi = 10.1016/S0040-4039(97)01386-5 | issue = 35 }}
{{cite journal | vauthors = Bouvier-Nave P, Husselstein T, Benveniste P | date = 1998 | title = Two families of sterol methyltransferases are involved in the first and the second methylation steps of plant sterol biosynthesis | journal = Eur. J. Biochem. | volume = 256 | pages = 88–96 | pmid = 9746350 | doi = 10.1046/j.1432-1327.1998.2560088.x | issue = 1 }}
{{cite journal | vauthors = Nes WD, McCourt BS, Zhou WX, Ma J, Marshall JA, Peek LA, Brennan M | date = 1998 | title = 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 | journal = Arch. Biochem. Biophys. | volume = 353 | pages = 297–311 | pmid = 9606964 | doi = 10.1006/abbi.1998.0665 | issue = 2 }}

Category:EC 2.1.1

Category:Enzymes of unknown structure