L-myo-inositol-1-phosphate synthase (MIPS)

L-myo-inositol-1-phosphate synthase (MIPS) is a cytosolic NAD+-dependent enzyme that catalyzes the conversion of D-glucose 6-phosphate to L-myo-inositol 1-phosphate, the first and rate-limiting step in the biosynthesis of all inositol-containing compounds, such as phosphoinositides and certain phospholipids. It is highly conserved across eukaryotes and some prokaryotes and is structurally characterized as a multimeric enzyme with key sequence motifs responsible for catalysis and cofactor binding. MIPS plays an essential role in a variety of fundamental cellular processes, including membrane biogenesis, cell signaling, and responses to oxidative stress. It is essential in plants, fungi, and certain bacteria, where it may serve as a therapeutic target, especially for antimicrobial drug discovery. In higher organisms, regulation of MIPS is tied closely to metabolic state and development.

Other names

Myo-inositol-1-phosphate synthaseInositol-3-phosphate synthaseMyo-inositol-1-phosphate synthetaseD-glucose 6-phosphate cycloaldolaseInositol 1-phosphate synthaseGlucose-6-phosphate inositol monophosphate cycloaldolaseGlucocycloaldolaseINO1 (gene name in yeast and plants)Ino-1 (used in some bacteria)

Enzyme inhibitors block the conversion of glucose 6-phosphate to inositol 1-phosphate, interrupting inositol and phosphoinositide metabolism, with potential for antifungal or antibacterial effects. Mechanistically, targets the active/catalytic site; several substrate analogs and small molecule inhibitors have been described in biochemical research.