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• W1643915825 abstract "The inhibition kinetic patterns obtained when ATP and pyridoxal analogues are used as inhibitors of the reaction catalyzed by pyridoxal kinase are consistent with a rapid equilibrium random Bi Bi, in which binary complexes, i.e. enzyme . ATP and enzyme . pyridoxal, are formed in kinetically significant amounts. Protein fluorescence quenching was used to determine the dissociation constant (Kd = 25 microM) of ATP . Zn bound to the nucleotide site of the kinase. The binding of ATP to the kinase induces a conformational change which is transmitted to other areas of the macromolecule. Pyridoxaloxime, a competitive inhibitor of pyridoxal, was used as a probe of the pyridoxal-binding site. It binds to the kinase with Ki = 2 microM and displays a fluorescent decay time of 7.8 ns. Time emission anisotropy measurements yield a rotational correlation time for bound pyridoxaloxime of approximately 2 ns, which is considerably shorter than the rotational correlation time of the protein (phi = 38 ns). The fast rotation of pyridoxaloxime remains unaffected by the binding of ATP." @default.
• W1643915825 created "2016-06-24" @default.
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• W1643915825 date "1981-01-01" @default.
• W1643915825 modified "2023-09-26" @default.
• W1643915825 title "Brain pyridoxal kinase. Mechanism of substrate addition, binding of ATP, and rotational mobility of the inhibitor pyridoxaloxime." @default.
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• W1643915825 doi "https://doi.org/10.1016/s0021-9258(19)70044-1" @default.
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