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- W2895784712 abstract "A histidine residue has been shown to be essential for the association of glutamate dehydrogenase. After photooxidation of one histidine residue per polypeptide chain with pyridoxal 5′-phosphate as photosensitizer the enzyme sediments with sedimentation coefficients significantly lower than the 25 S of the native enzyme. These preparations retain about 70% of their activity. A further histidine residue has been shown to be essential for the activity of glutamate dehydrogenase. After photooxidation of a second histidine residue per polypeptide chain the enzyme is inactive. These results have been confirmed by modification experiments with diethylpyrocarbonate. The inactive enzyme has lost its ability to bind NADH. The photooxidation of the first histidine residue is accompanied by a change in the regulatory properties of the enzyme. GTP no longer inhibits the activity while the effect of ADP is unchanged. A novel reaction of pyridoxal-P with the enzyme has been investigated. During irradiation of the enzyme · pyridoxal-P complex pyridoxal-P becomes slowly irreversibly incorporated. At the point of about 80% inactivation the glutamate dehydrogenase contains 0.43 molecules pyridoxal-P per polypeptide chain as indicated by the incorporation of radioactivity from [4-3H]pyridoxal-P. The reaction is accompanied by the appearance of a new absorption maximum at 325 nm. The effect is interpreted as a photoactivated addition of an imidazole group to the double bond of a Schiff base formed between pyridoxal-P and an ɛ-NH2 group of a lysine residue. There is evidence that the position 97 identified by Smith et al. in 1970 (Proc. Nat. Acad. Sci. U.S.A. 67, 724) is not involved in this reaction. The reaction may be important for the determination of the relative position in the tertiary structure of the two functional groups involved." @default.
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- W2895784712 date "1973-01-01" @default.
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- W2895784712 title "Studies of Glutamate Dehydrogenase. Characterization of Histidine Residues Involved in the Activity and Association Photoactivated Labelling with Pyridoxal 5'-Phosphate" @default.
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- W2895784712 doi "https://doi.org/10.1111/j.1432-1033.1973.tb02580.x" @default.
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