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- W2022285763 abstract "S→N acyl migration, taking place concomitantly with the hydrolysis of p-nitro-phenyl acetate catalyzed by glyceraldehyde-3-phosphate dehydrogenase (D-glycer-aldehyde-3-phosphate:NAD oxidoreductase (phosphorylating), EC 1.2.1.12), is inhibited by coenzyme and by AMP. The coenzyme appears to bind in the same way to both the native enzyme and its N-acetyl derivative. The inhibition of acyl migration does not, therefore, support the existence of an interaction between the nucleotides and the acyl acceptor amino group. This is presumably the result of changes in the structure of the protein induced by the binding of the nucleotides. Both nucleotides protect the enzyme against spontaneous denaturation, influence its susceptibility to trypsin (EC 3.4.4.4) and facilitate its crystallization." @default.
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- W2022285763 date "1966-01-01" @default.
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- W2022285763 title "The effect of coenzyme on the S→N acyl migration in glyceraldehyde-3-phosphate dehydrogenase" @default.
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- W2022285763 doi "https://doi.org/10.1016/s0926-6593(66)80036-x" @default.
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