title: Studies on the biosynthesis of cyclitols, XXXV. On the mechanism of action of myo-inositol-1-phosphate synthase from rat testicles.
abstract: The animal myo-inositol-1-phosphate synthase is competitively inhibited by pyridoxal phosphate and trinitrobenzensulphonate, both compounds known to prevent Schiff's base formation. When incubated with labelled substrate and then treated with NaBH4, label can be recovered in the enzyme protein. In analogous experiments with tritiated NaBH4 the enzyme protein also becomes labelled; after hydrolysis of such protein only one labelled compound, derived from lysine and D-glucose 6-phosphate, could be isolated. Its exact structure is not yet known. From these results it can be concluded that during its action myo-inositol-1-phosphate synthase forms a Schiff's base with its substrate, in analogy to the class I aldolases.
mesh_terms: D000818:Animals; D001894:Borohydrides / Q000494:pharmacology; D002238:Carbohydrate Epimerases / Q000378:metabolism*; D005033:Ethylmaleimide / Q000494:pharmacology; D005958:Glucosephosphates / Q000378:metabolism; D066298:In Vitro Techniques; D007700:Kinetics; D008297:Male; D007296:Myo-Inositol-1-Phosphate Synthase / Q000037:antagonists & inhibitors / Q000378:metabolism*; D011732:Pyridoxal Phosphate / Q000494:pharmacology; D051381:Rats; D012545:Schiff Bases / Q000378:metabolism; D013737:Testis / Q000201:enzymology*; D014302:Trinitrobenzenesulfonic Acid / Q000494:pharmacology
chemical_list: D001894:Borohydrides; D005958:Glucosephosphates; D012545:Schiff Bases; D011732:Pyridoxal Phosphate; D014302:Trinitrobenzenesulfonic Acid; D002238:Carbohydrate Epimerases; D007296:Myo-Inositol-1-Phosphate Synthase; D005033:Ethylmaleimide