期刊
CELLULAR AND MOLECULAR LIFE SCIENCES
卷 66, 期 4, 页码 636-648出版社
SPRINGER BASEL AG
DOI: 10.1007/s00018-008-8516-1
关键词
Methionine adenosyltransferase; S-adenosylmethionine synthetase; crystal structure; reaction mechanism; folding; mutants; hepatic disease
资金
- Ministerio de Educacion y Ciencia [BMC2002-00243, BFU2005-00050]
- Fondo de Investigacion Sanitaria del Instituto de Salud Carlos III [RCMN C03/08]
- National Institutes of Health [GM31186, CA06927]
Methionine adenosyltransferases (MATs) 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 begin to explain how the three intertwined domains of the catalytic subunit are produced, and to highlight 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.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据