Structural Basis for Par-4 Recognition by the SPRY Domain- and SOCS Box-Containing Proteins SPSB1, SPSB2, and SPSB4

Autor: Zhihe Kuang, Panagis Filippakopoulos, Raymond S. Norton, Alex N. Bullock, J. Uppenberg, Pavel Savitsky, Timothy Sharpe, Shenggen Yao, Andrew Low, Sandra E. Nicholson, Rowena S. Lewis

Publikováno v: Journal of Molecular Biology

The mammalian SPRY domain- and SOCS box-containing proteins, SPSB1 to SPSB4, belong to the SOCS box family of E3 ubiquitin ligases. Substrate recognition sites for the SPRY domain are identified only for human Par-4 (ELNNNL) and for the Drosophila or

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::576b5bd8bf1b5dd009c1ee2d663f2c06
http://europepmc.org/articles/PMC2923778

Xylose Acetals - a New Class of Sustainable Solvents and Their Application in Enzymatic Polycondensation.

Autor: Komarova AO; Laboratory of Sustainable and Catalytic Processing, Institute of Chemical Sciences and Engineering, École Polytechnique Fédérale de Lausanne (EPFL), Station 6, 1015, Lausanne, Switzerland., Warne CM; acib GmbH, Konrad-Lorenz-Strasse 20, 3430, Tulln an der Donau, Austria.; Institute of Environmental Biotechnology, Department of Agrobiotechnology, IFA-Tulln, University of Natural Resources and Life Sciences Vienna, Konrad-Lorenz-Strasse 20, 3430, Tulln an der Donau, Austria., Pétremand H; Laboratory of Sustainable and Catalytic Processing, Institute of Chemical Sciences and Engineering, École Polytechnique Fédérale de Lausanne (EPFL), Station 6, 1015, Lausanne, Switzerland., König-Mattern L; Max Planck Institute for Dynamics of Complex Technical Systems, Process Systems Engineering (PSE), Sandtorstraße 1, D-39106, Magdeburg, Germany., Stöckelmaier J; Institute of Molecular Modeling and Simulation (MMS), University of Natural Resources and Life Sciences Vienna, Muthgasse 18, 1190, Vienna, Austria., Oostenbrink C; Institute of Molecular Modeling and Simulation (MMS), University of Natural Resources and Life Sciences Vienna, Muthgasse 18, 1190, Vienna, Austria., Guebitz GM; acib GmbH, Konrad-Lorenz-Strasse 20, 3430, Tulln an der Donau, Austria.; Institute of Environmental Biotechnology, Department of Agrobiotechnology, IFA-Tulln, University of Natural Resources and Life Sciences Vienna, Konrad-Lorenz-Strasse 20, 3430, Tulln an der Donau, Austria., Luterbacher J; Laboratory of Sustainable and Catalytic Processing, Institute of Chemical Sciences and Engineering, École Polytechnique Fédérale de Lausanne (EPFL), Station 6, 1015, Lausanne, Switzerland., Pellis A; Universitá di Genova, Dipartimento di Chimica e Chimica Industriale, via Dodecaneso 31, 16146, Genova (GE), Italy.

Publikováno v: ChemSusChem [ChemSusChem] 2024 Oct 31, pp. e202401877. Date of Electronic Publication: 2024 Oct 31.

Crystallographic and molecular-modeling studies of lipase B from Candida antarctica reveal a stereospecificity pocket for secondary alcohols

Autor: M Norin, N Ohrner, T.A. Jones, Karl Hult, Shamkant Anant Patkar, Gerard J. Kleywegt, T Anthonsen, Waagen, J. Uppenberg

Publikováno v: Biochemistry. 34:16838-16851

Many lipases are potent catalysts of stereoselective reactions and are therefore of interest for use in chemical synthesis. The crystal structures of lipases show a large variation in the shapes of their active site environments that may explain the

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2ccb0cbf464afb8cd097c9400bc435c0
https://doi.org/10.1021/bi00051a035

Crystallization and Preliminary X-ray Studies of Lipase B from Candida antarctica

Autor: J. Uppenberg, T.A. Jones, Terese Bergfors, S. Patkar

Publikováno v: Journal of Molecular Biology. 235:790-792

Lipase B from Candida antarctica has been crystallized in five different crystal forms. The space groups and cell dimensions have been determined by X-ray diffraction methods. Four of the crystal forms have been judged to be of good quality for furth

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::88eab3de464939f22c08e6fce08de3ad
https://doi.org/10.1006/jmbi.1994.1035

Crystal structure of a mammalian purple acid phosphatase

Autor: J, Uppenberg, F, Lindqvist, C, Svensson, B, Ek-Rylander, G, Andersson

Publikováno v: Journal of molecular biology. 290(1)

Tartrate-resistant acid phosphatase (TRAP) is a mammalian di-iron- containing enzyme that belongs to the family of purple acid phosphatases (PAP). It is highly expressed in a limited number of tissues, predominantly in bone-resorbing osteoclasts and

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::a543743573bddce358701b94a3286829
https://pubmed.ncbi.nlm.nih.gov/10388567