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- W1986137771 abstract "When the dehydrogenase activity of muscle glyceraldehyde-3-phosphate dehydrogenase is reversibly inactivated with o-iodosobenzoate or under certain conditions with iodine monochloride, the enzyme is converted to an acetyl phosphatase. Inactivation of the dehydrogenase activity with tetrathionate, iodoacetate, and iodoacetamide does not convert the enzyme to an acetyl phosphatase. When the dehydrogenase activity is reversibly inactivated with o-iodosobenzoate at 0 ° and then incubated at 37 °, the dehydrogenase activity is irreversibly inactivated and the acetyl phosphatase activity disappears at a comparable rate. When CN−, SO3=, S2O3=, thiourea, 6-propyl thiouracil, and phenyl arsene oxide are added to the enzyme at pH 5.9 after its oxidation with o-iodosobenzoate, the acetyl phosphatase activity is inactivated. Evidence which has been presented previously (14) suggests that the catalytically active sulfhydryl group of glyceraldehyde-3-phosphate dehydrogenase is converted to a stabilized sulfenic acid residue during its reversible inactivation with o-iodosobenzoate. To reconcile the activation and inactivation of the acetyl phosphatase activity by the various reagents used in this study, it is suggested that the stabilized sulfenic acid derivative of the catalytically active sulfhydryl group of glyceraldehyde-3-phosphate dehydrogenase participates directly in acetyl phosphatase hydrolysis. A mechanism which postulates a sulfenyl carboxylate intermediate has been proposed for the hydrolytic reaction." @default.
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- W1986137771 title "The activation and inactivation of the acyl phosphatase activity of glyceraldehyde-3-phosphate dehydrogenase" @default.
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- W1986137771 doi "https://doi.org/10.1016/0003-9861(70)90209-2" @default.
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