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- W1597786032 abstract "L-myo-Inositol-1-phosphate synthase has been found to have at least a 5-fold preference for the beta-anomer of its natural substrate D-Glc-6-P. The alpha-anomer appears to be an inhibitor of the reaction and may be converted to product as well. As well as showing an enzymatic preference for the equatorial C-1 hydroxyl of D-Glc-6-P, our results suggest that it is the pyranose form of D-Glc-6-P that binds to the enzyme and that ring-opening is an enzymatic step. We have also found D-2-dGlc-6-P, D-2-F-2-dGlc-6-P, and D-Man-6-P each to be both competitive inhibitors and substrates that are converted to inositol phosphates by the synthase. D-Allose-6-P is a weak inhibitor of the enzyme, but not a substrate. D-Gal-6-P is neither substrate nor inhibitor. Thus the specificity of the synthase with respect to single position epimers of D-Glc-6-P increases in the order C1 less than C2 much less than C3 less than C4." @default.
- W1597786032 created "2016-06-24" @default.
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- W1597786032 date "1985-09-01" @default.
- W1597786032 modified "2023-09-28" @default.
- W1597786032 title "Anomeric and other substrate specificity studies with myo-inositol-1-P synthase." @default.
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- W1597786032 doi "https://doi.org/10.1016/s0021-9258(17)39151-2" @default.
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