4.5 Review

Diversification and evolution of L-myo-inositol 1-phosphate synthas

期刊

FEBS LETTERS
卷 553, 期 1-2, 页码 3-10

出版社

WILEY
DOI: 10.1016/S0014-5793(03)00974-8

关键词

myo-inositol; L-myo-inositol 1-phosphate synthase; NAD binding; oxidoreductase; core structure; protein evolution

向作者/读者索取更多资源

L-myo-Inositol 1-phosphate synthase (MIPS, EC 5.5.1.4), the key enzyme in the inositol and phosphoinositide biosymbetic pathway, is present throughout evolutionarily diverse organisms and is considered an ancient protein/gene. Analysis by multiple sequence alignment, phylogenetic tree generation and comparison of newly determined crystal structures provides new insight into the origin and evolutionary relationships among the various MIPS proteins/genes. The evolution of the MIPS protein/gene among the prokaryotes seems more diverse and complex than amongst the eukaryotes. However, conservation of a 'core catalytic structure' among the MIPS proteins implies an essential function of the enzyme in cellular metabolism throughout the biological kingdom. (C) 2003 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.

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。

评论

主要评分

4.5
评分不足

次要评分

新颖性
-
重要性
-
科学严谨性
-
评价这篇论文

推荐

暂无数据
暂无数据