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Structure-function relationships in methionine adenosyltransferases

AutorMarkham, George D.; Pajares, María A.
Palabras claveMethionine adenosyltransferase
S-adenosylmethionine synthetase
Crystal structure
Reaction mechanism
Fecha de publicación2009
CitaciónCellular and Molecular Life Sciences 66(4): 636-648 (2009)
ResumenMethionine adenosyltransferases (MAT) are the family of enzymes that synthesize the main biological methyl donor, S-adenosylmethionine. The high sequence conservation among catalytic subunits from bacteria and Eukarya preserves key residues that control activity and oligomerization, which is reflected in the protein structure. However, structural differences among complexes with substrates and products have led to proposals of several reaction mechanisms. In parallel, folding studies are starting to explain how the three intertwined domains of the catalytic subunit are produced, and the importance of certain intermediates in attaining the active final conformation. This review analyzes the available structural data and proposes a consensus interpretation that facilitates an understanding of the pathological problems derived from impairment of MAT function. In addition, new research opportunities directed toward clarification of aspects that remain obscure are also identified.
DescripciónEl pdf del artículo es la versión post-print.
Versión del editorhttp://dx.doi.org/10.1007/s00018-008-8516-1
ReferenciasPMID: 18953685
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