Loewus M W
J Biol Chem. 1977 Oct 25;252(20):7221-3.
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.
来自大鼠睾丸、悬铃木细胞培养物和水稻细胞培养物的肌醇-1-磷酸合酶(EC 5.5.1.4)将D-[5-³H]葡萄糖6-磷酸转化为肌醇-[2-³H]磷酸的速率为未标记底物的0.21至0.48。D-[3-³H]-和D-[4-³H]葡萄糖6-磷酸的转化速率与未标记底物的速率大致相同。对于睾丸酶,以冷冻溶液形式储存会进一步降低以D-[5-³H]葡萄糖6-磷酸为底物时的反应速率。当反应在[³H]水中进行时,肌醇1-磷酸中未出现³H,但从最终反应混合物中分离出的底物中回收了少量³H。这些数据支持了D-葡萄糖6-磷酸的碳5参与了该转化所提出的机制。