Cobalamin-dependent and cobamide-dependent methyltransferases

Autor:	Rowena G. Matthews, Supratim Datta, Markos Koutmos
Rok vydání:	2008
Předmět:	Methyltransferase Methionine Homocysteine biology Stereochemistry Lability Cobalamin Cofactor chemistry.chemical_compound Biochemistry chemistry Catalytic cycle Structural Biology biology.protein sense organs Molecular Biology Histidine
Zdroj:	Current Opinion in Structural Biology. 18:658-666
ISSN:	0959-440X
DOI:	10.1016/j.sbi.2008.11.005
Popis:	Methyltransferases that employ cobalamin cofactors, or their analogs the cobamides, as intermediates in catalysis of methyl transfer play vital roles in energy generation in anaerobic unicellular organisms. In a broader range of organisms they are involved in the conversion of homocysteine to methionine. Although the individual methyl transfer reactions catalyzed are simple S N 2 displacements, the required change in coordination at the cobalt of the cobalamin or cobamide cofactors and the lability of the reduced Co +1 intermediates introduces the necessity for complex conformational changes during the catalytic cycle. Recent spectroscopic and structural studies on several of these methyltransferases have helped to reveal the strategies by which these conformational changes are facilitated and controlled.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::4977f8b0362ad8665128fad723223a5e https://doi.org/10.1016/j.sbi.2008.11.005 Zobrazit plný text záznamu Full Text from ScienceDirect