1L-myo-Inositol-1-phosphate synthase catalyzes the conversion of D-glu
cose 6-phosphate to 1L-myo-inositol-1-phosphate, the first committed s
tep in the production of all inositol-containing compounds, including
phospholipids, either directly or by salvage. The enzyme exists in a c
ytoplasmic form in a wide range of plants, animals, and fungi. It has
also been detected in several bacteria and a chloroplast form is obser
ved in alga and higher plants. The enzyme has been purified from a wid
e range of organisms and its active form is a multimer of identical su
bunits ranging in molecular weight from 58 000 to 67 000. The activity
of the synthase is stimulated by NH4Cl and inhibited by glucitol 6-ph
osphate and 2-deoxyglucose 6-phosphate. Structural genes (INO1) encodi
ng the 1L-myo-inositol-1-phosphate synthase subunit have been isolated
from several eukaryotic microorganisms and higher plants. In baker's
yeast, Saccharomyces cerevisiae, the transcriptional regulation of the
INO1 gene has been studied in detail and its expression is sensitive
to the availability of phospholipid precursors as well as growth phase
. The regulation of the structural gene encoding 1L-myo-inositol-1-pho
sphate synthase has also been analyzed at the transcriptional level in
the aquatic angiosperm, Spirodela polyrrhiza and the halophyte, Mesem
bryanthemum crystallinum. (C) 1997 Elsevier Science B.V.