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KMID : 0380219940270030266
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Journal of Biochemistry and Molecular Biology
1994 Volume.27 No. 3 p.266 ~ p.270
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Importance of the Hydroxyl Group of Ser65 for Glutathione Binding of Human Glutathione S-Transferase P1-1
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Abstract
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Abstract:
@EN The mutational replacement of Ser65 with alanine decreased the binding affinity of the enzyme for S-hexyl-GSH-Sepharose and GSH-agarose, and increased the KmGSH value and I50 inhibitory effect for S-hexyl-GSH, but did not significantly affect
the
kcat value for glutathione conjugation with 1-chloro-2,4-dinitrobenzene. The pKa value of the thiol groups of GSH bound in S65A was shifted approximately 0.6pK units higher than the pKa value in the wild type. Therefore, Ser65 seems to contribute
to the
binding of GSH.
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KEYWORD
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