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JBC, Vol. 252, Issue 20, 7221-7223, Oct, 1977
M. W. Loewus
myo-Inositol-1-phosphate synthase (EC 5.5.1.4) from rat testis, Acer
pseudoplatanus L. cell culture and Oryza sativa L. cell culture, converted
D-[5-3H]glucose 6-phosphate to myo-[2-3H]inositol 1-phosphate at rates
ranging from 0.21 to 0.48 that of unlabeled substrate. D-[3-3H]- and
D-[4-3H]glucose 6-phosphate were converted at approximately the same rate
as that of unlabeled substrate. In the case of testis enzyme, storage as a
frozen solution further lowered the rate with D-[5-3H]glucose 6-phosphate
as substrate. When the reaction was run in [3H]water, no 3H appeared in
myo-inositol 1-phosphate but a small amount was recovered in substrate
isolated from the final reaction mixture. These data support the
involvement of carbon 5 of D-glucose 6-phosphate in the mechanism proposed
for this conversion.
Hydrogen isotope effects in the cyclization of D-glucose 6-phosphate by myo-inositol-1-phosphate synthase
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