Diversification and evolution of L‐myo‐inositol 1‐phosphate synthase¹

Abstract

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. ß

Myo-inositol content in pteridophytes and the isolation and characterization of L-myo-inositol-1-phosphate synthase from Diplopterygium glaucum

“…Like all other eukaryotes, the D. glaucum MIPS requires NH 4 + for optimal activity in contrast to the divalent cationrequiring MIPS of prokaryotes (Majumder et al, 2003). This indicates that the pteridophytic MIPS is a type-III aldolase.…”

“…Free myoinositol content was detected in relatively large quantities in the reproductive pinnules of Lycopodium cernuum and Diplopterygium glaucum. Different inositol derivatives are known to be essential for all life forms (Majumder et al, 2003). Hence, the detection of free myo-inositol in these pteridophytes is not surprising.…”

A Novel Salt-tolerant l-myo-Inositol-1-phosphate Synthase from Porteresia coarctata (Roxb.) Tateoka, a Halophytic Wild Rice

“…Subsequently, the complete nucleotide sequence of the full-length INO1 gene from S. cerevisiae was reported by Johnson and Henry (8). Until now, over 60 genes homologous to INO1 have been cloned and characterized from a wide variety of prokaryotic, archaeal, and eukaryotic sources (9 -12), and the conservation of a probable "core catalytic structure" among all has been proposed (12). The crystal structures of MIPS(s) from Saccharomyces and Mycobacterium have been worked out, providing evidence for the structural insight for the proposed reaction mechanism (13)(14)(15)(16)(17).…”

Comparative Expression and Cellular Localization of Myo-inositol Phosphate Synthase (MIPS) in the Wild Type and in an EMS Mutant During Common Bean (Phaseolus vulgaris L.) Seed Development

“…The amino acid sequence of Pv_BAT93 MIPS shows a high degree of similarity and is strongly clustered in a subgroup belonging to Fabales species. These data indicate that the genes encoding MIPS reveal remarkable evolutionary conservation of the primary structure (Majumder et al 2003).…”

“…MIPS coding sequences have been isolated (Hegman et al 2001) and characterized by a temporally and spatially distinct expression pattern from a number of plant species, such as G. max (Nunes et al 2006), S. indicum (Chun et al 2003) and A. thaliana (Chiera and Grabau 2007). In some cases, two or three MIPS genes have been isolated from each species (Majumder et al 2003).…”