Abstract:
:Human class Alpha glutathione transferase (GST) A1-1 has been subjected to site-directed mutagenesis of a Tyr residue conserved in all classes of cytosolic GSTs. The change of Tyr8----Phe lowers the specific activities with three substrates to 2-8% of the values for the wild-type enzyme. The changes in the kinetic parameters kcat/KM, Vmax and S0.5 show that the decreased activities are partly due to a reduced affinity for glutathione. The effect is reflected in lowered kcat values, suggesting that the hydroxyl group of Tyr8 is involved in the activation of glutathione. The proposal of such a role for the Tyr residue has support from the 3D structure of a pig lung class Pi GST [Reinemer et al. (1991) EMBO J. 10, 1997-2005]. Thus, Tyr8 appears to be the first active site residue established as participating in the chemical mechanism of a GST.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Stenberg G,Board PG,Mannervik Bdoi
10.1016/0014-5793(91)81174-7subject
Has Abstractpub_date
1991-11-18 00:00:00pages
153-5issue
1-2eissn
0014-5793issn
1873-3468pii
0014-5793(91)81174-7journal_volume
293pub_type
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