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Diversification and evolution of L ‐ myo ‐inositol 1‐phosphate synthase 1
Author(s) -
Majumder Arun Lahiri,
Chatterjee Anirban,
Ghosh Dastidar Krishnarup,
Majee Manoj
Publication year - 2003
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(03)00974-8
Subject(s) - gene , atp synthase , phylogenetic tree , enzyme , biology , inositol , biochemistry , phylogenetics , function (biology) , conserved sequence , genetics , computational biology , peptide sequence , receptor
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.