Stereochemistry of the myo-inositol-1-phosphate synthase reaction.

Experiments with D-glucose-6-P stereospecifically tritiated at C-6 showed that the myo-inositol-1 P synthase reaction catalyzed by both the enzyme from beef testis and from pollen of Lilium longiflorum proceeds with stereospecific loss of the pro-6R and incorporation of the pro-6S hydrogen into the product. The ring closure thus occurs in a retention mode at C-6 of the substrate, a finding at variance with an earlier report, but in agreement with the stereochemistry recently determined for the reaction in Streptomyces flavopersicus and with the general stereochemical mode of operation of aldolases.