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- W2347454673 abstract "Comparison of the inhibition of 5′-AMP and its analogs on snake muscle fructose1,6-bisphosphatase showed that both the 6-amino group of the purine ring and the5′-phosphate group of the ribose of 5′-AMP were critically essential,whereas theimidazole part of the purine ring in 5′-AMP did not significantly contribute tothe binding of 5′-AMP on the enzyme.The inhibition pattern of 5′-dAMP on snake muscle fructose 1,6-bisphophstasewas unique.The inhibition constant cal-culated from 50% inhibition was 3μM,almostthe same as the inhibition constant of 5′-AMP.The maximum inhibition of thisinhibitor,however,was only 60%.The binding of 2′-dAMP and 5′-AMP may resultin different conformational changes on fructose 1,6-bisphosphatase and the interactionof 2′-OH of 5′-AMP with a certain group at the allosteric site of the enzyme wouldconduct the transmission of the message from the allosteric site to the catalytic site.The enzyme modified with water soluble carbodiimide gave rise to 40% of 5′-AMPinhibition.The results tentatively suggest that the carboxyl group and the groupthat interacted with 2′-OH of 5′-AMP together responded to the whole message tran-smission from the allosteric site to the catalytic site." @default.
- W2347454673 created "2016-06-24" @default.
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- W2347454673 date "1984-01-01" @default.
- W2347454673 modified "2023-09-24" @default.
- W2347454673 title "ALLOSTERIC SITE OF SNAKE MUSCLE FRUCTOSE 1,6-BISPHOSPHATASE" @default.
- W2347454673 hasPublicationYear "1984" @default.
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