Abstract
The formation of a Shiff''s base by myo-inositol-1-phosphate synthase [EC 5.5.1.4] of rat testicles occurs by binding the aldehyde group of the open form of its substrate, D-glucose 6-phosphate, to a lysyl residue of 1 or both smaller subunits of the enzyme. The participation of the Shiff''s base formation in the catalytic process is supported by the observations that no Shiff''s base is formed if NAD+ is removed from the enzyme and that in the presence of NAD+, the dehydrogenation step involved in the catalytic mechanism apparently takes place rapidly after the formation of the Shiff''s base.