Diversification and evolution of L‐myo‐inositol 1‐phosphate synthase

FEBS Letters

Ghosh Dastidar, Krishnarup¹  Majee, Manoj¹  Majumder, Arun Lahiri¹  Chatterjee, Anirban¹ 

[1] Plant Molecular and Cellular Genetics, Bose Institute (Centenary Building), P-1/12 CIT Scheme VII M, Kolkata 700054, India

关键词: myo-Inositol;    L-myo-Inositol 1-phosphate synthase;    NAD binding;    Oxidoreductase;    Core structure;    Protein evolution;   

DOI  :  10.1016/S0014-5793(03)00974-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

L-myo-Inositol 1-phosphate synthase (MIPS, EC 5.5.1.4), the key enzyme in the inositol and phosphoinositide biosynthetic 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.

【 授权许可】

Unknown