Diversification and evolution of L-myo-inositol 1-phosphate synthase.
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.
Majumder
Arun Lahiri
AL
Plant Molecular and Cellular Genetics, Bose Institute (Centenary Building), Kolkata, India. lahiri@bic.boseinst.ernet.in
Chatterjee
Anirban
A
Ghosh Dastidar
Krishnarup
K
Majee
Manoj
M
D000595:Amino Acid Sequence; D000818:Animals; D017124:Conserved Sequence; D018360:Crystallography, X-Ray; D019143:Evolution, Molecular; D006801:Humans; D008969:Molecular Sequence Data; D007296:Myo-Inositol-1-Phosphate Synthase / Q000737:chemistry* / Q000235:genetics* / Q000378:metabolism; D010802:Phylogeny; D013329:Structure-Activity Relationship
D007296:Myo-Inositol-1-Phosphate Synthase