5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase

From Wikipedia, the free encyclopedia

In enzymology, a 5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase (EC 2.1.1.14) is an enzyme that catalyzes the chemical reaction

5-methyltetrahydropteroyltri-L-glutamate + L-homocysteine $\rightleftharpoons$ tetrahydropteroyltri-L-glutamate + L-methionine

Thus, the two substrates of this enzyme are 5-methyltetrahydropteroyltri-L-glutamatic acid and L-homocysteine, whereas its two products are tetrahydropteroyltri-L-glutamatic acid and 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 5-methyltetrahydropteroyltri-L-glutamate:L-homocysteine S-methyltransferase. Other names in common use include tetrahydropteroyltriglutamate methyltransferase, homocysteine methylase, methyltransferase, tetrahydropteroylglutamate-homocysteine transmethylase, methyltetrahydropteroylpolyglutamate:homocysteine methyltransferase, cobalamin-independent methionine synthase, methionine synthase (cobalamin-independent), and MetE. This enzyme participates in methionine metabolism. It has 2 cofactors: orthophosphate, and zinc.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] Structural studies

As of late 2007, 9 structures have been solved for this class of enzymes, with PDB accession codes 1T7L, 1U1H, 1U1J, 1U1U, 1U22, 1XDJ, 1XPG, 1XR2, and 2NQ5.

[edit] References

IUBMB entry for 2.1.1.14
BRENDA references for 2.1.1.14 (Recommended.)
PubMed references for 2.1.1.14
PubMed Central references for 2.1.1.14
Google Scholar references for 2.1.1.14
Guest JR, Friedman S, Foster MA, Tejerina G, Woods DD (1964). "Transfer of the methyl group from N5-methyltetrahydrofolates to homocysteine in Escherichia coli". Biochem. J. 92: 497–504. PMID 5319972.
Whitfield CD, Steers EJ Jr, Weisbach H (1970). "Purification and properties of 5-methyltetrahydropteroyltriglutamate-homocysteine transmethylase". J. Biol. Chem. 245: 390–401. PMID 4904482.
Eichel J, Gonzalez JC, Hotze M, Matthews RG, Schroder J (1995). "Vitamin-B12-independent methionine synthase from a higher plant (Catharanthus roseus). Molecular characterization, regulation, heterologous expression, and enzyme properties". Eur. J. Biochem. 230: 1053–8. doi:10.1111/j.1432-1033.1995.tb20655.x. PMID 7601135.
Gonzalez JC, Peariso K, Penner-Hahn JE, Matthews RG (1996). "Cobalamin-independent methionine synthase from Escherichia coli: a zinc metalloenzyme". Biochemistry. 35: 12228–34. doi:10.1021/bi9615452. PMID 8823155.
Penner-Hahn JE (1998). "Characterization of the zinc binding site in methionine synthase enzymes of Escherichia coli: The role of zinc in the methylation of homocysteine". J. Am. Chem. Soc. 120: 8410–8416. doi:10.1021/ja980581g.