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

被引:98
|
作者
Majumder, AL [1 ]
Chatterjee, A [1 ]
Dastidar, KG [1 ]
Majee, M [1 ]
机构
[1] Bose Inst, Kolkata 700054, W Bengal, India
来源
FEBS LETTERS | 2003年 / 553卷 / 1-2期
关键词
myo-inositol; L-myo-inositol 1-phosphate synthase; NAD binding; oxidoreductase; core structure; protein evolution;
D O I
10.1016/S0014-5793(03)00974-8
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:3 / 10
页数:8
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