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Microsomal glutathione transferase 1 exhibits one-third-of-the-sites-reactivity towards glutathione
Vise andre og tillknytning
2009 (engelsk)Inngår i: Archives of Biochemistry and Biophysics, ISSN 0003-9861, E-ISSN 1096-0384, Vol. 487, nr 1, s. 42-48Artikkel i tidsskrift (Fagfellevurdert) Published
Abstract [en]

The trimeric membrane protein microsomal glutathione transferase 1 (MGST1) possesses glutathione transferase and peroxidase activity. Previous data indicated one active site/trimer whereas structural data suggests three GSH-binding sites. Here we have determined ligand interactions of MGST1 by several techniques. Nanoelectrospray mass spectrometry of native MGST1 revealed binding of three GSH molecules/trimer and equilibrium dialysis showed three product molecules/trimer (K(d) = 320 +/- 50 mu M). All three product molecules Could be competed out with GSH. Reinvestigation of GSH-binding showed one high affinity site per trimer, consistent with earlier data. Using single turnover stopped flow kinetic measurements, Kd could be determined for a low affinity GSH-binding site (2.5 +/- 0.5 mu M). Thus we can reconcile previous observations and show here that MGST1 contains three active sites with different affinities for GSH and that only the high affinity site is catalytically competent.

sted, utgiver, år, opplag, sider
2009. Vol. 487, nr 1, s. 42-48
Emneord [en]
GSH, MGST1, MAPEG, Alternating sites, Cooperativity, Glutathione transferase
HSV kategori
Identifikatorer
URN: urn:nbn:se:kth:diva-82938DOI: 10.1016/j.abb.2009.04.009ISI: 000267407800006OAI: oai:DiVA.org:kth-82938DiVA, id: diva2:498606
Merknad
QC 20120214Tilgjengelig fra: 2012-02-12 Laget: 2012-02-12 Sist oppdatert: 2017-12-07bibliografisk kontrollert

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