title: Effects of hydrostatic pressure on the quaternary structure and enzymatic activity of a large peptidase complex from Pyrococcus horikoshii.
abstract: While molecular adaptation to high temperature has been extensively studied, the effect of hydrostatic pressure on protein structure and enzymatic activity is still poorly understood. We have studied the influence of pressure on both the quaternary structure and enzymatic activity of the dodecameric TET3 peptidase from Pyrococcus horikoshii. Small angle X-ray scattering (SAXS) revealed a high robustness of the oligomer under high pressure of up to 300 MPa at 25°C as well as at 90°C. The enzymatic activity of TET3 was enhanced by pressure up to 180 MPa. From the pressure behavior of the different rate-constants we have determined the volume changes associated with substrate binding and catalysis. Based on these results we propose that a change in the rate-limiting step occurs around 180 MPa.
authors: Group Extremophiles and Large Molecular Assemblies (ELMA), CEA, Institut de Biologie Structurale, Grenoble, France.
authors: Eva
authors: E
authors: Rosenbaum
authors: Frank
authors: F
authors: Gabel
authors: M Asunción
authors: MA
authors: Durá
authors: Stéphanie
authors: S
authors: Finet
authors: Cécile
authors: C
authors: Cléry-Barraud
authors: Patrick
authors: P
authors: Masson
authors: Bruno
authors: B
authors: Franzetti
mesh_terms: D019843:Archaeal Proteins / Q000737:chemistry* / Q000378:metabolism*; D004795:Enzyme Stability; D006874:Hydrostatic Pressure; D007700:Kinetics; D010447:Peptide Hydrolases / Q000737:chemistry* / Q000378:metabolism*; D020836:Protein Structure, Quaternary; D043902:Pyrococcus horikoshii / Q000201:enzymology*; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D053838:Scattering, Small Angle; D013696:Temperature; D014961:X-Ray Diffraction
chemical_list: D019843:Archaeal Proteins; D011994:Recombinant Proteins; D010447:Peptide Hydrolases