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  • 1. Eriksson, Sandra
    et al.
    Gutierrez Arenas, Omar
    Department of Biochemistry and Organic Chemistry, Uppsala University.
    Bjerling, Pernilla
    Tomkinson, Birgitta
    Development, evaluation and application of tripeptidyl-peptidase II sequence signatures2009Ingår i: Archives of Biochemistry and Biophysics, ISSN 0003-9861, E-ISSN 1096-0384, Vol. 484, nr 1, s. 39-45Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    Tripeptidyl-peptidase II (TPP II) is a cytosolic peptidase that has been implicated in fat formation and cancer, apparently independent of the enzymatic activity. In search for alternative functional regions, conserved motifs were identified and eleven signatures were constructed. Seven of the signatures covered previously investigated residues, whereas the functional importance of the other motifs is unknown. This provides directions for future investigations of alternative activities of TPP II. The obtained signatures provide an efficient bioinformatic tool for the identification of TPP II homologues. Hence, a TPP II sequence homologue from fission yeast, Schizosaccharomyces pombe, was identified and demonstrated to encode the TPP II-like protein previously reported as multicorn. Furthermore, an homologous protein was found in the prokaryote Blastopirellula marina, albeit the TPP II function was apparently not conserved. This gene is probably the result of a rare gene transfer from eukaryote to prokaryote.

  • 2. Ålander, J.
    et al.
    Lengqvist, J.
    Holm, P.J.
    Svensson, R.
    Gerbaux, P.
    van der Heuvel, R.H.H.
    Hebert, Hans
    Department of Biosciences, Karolinska Institutet.
    Griffiths, W.J.
    Armstrong, R.N.
    Morgenstern, R.
    Microsomal glutathione transferase 1 exhibits one-third-of-the-sites-reactivity towards glutathione2009Ingår i: Archives of Biochemistry and Biophysics, ISSN 0003-9861, E-ISSN 1096-0384, Vol. 487, nr 1, s. 42-48Artikel i tidskrift (Refereegranskat)
    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.

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