Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Vanina Rea"'
Autor:
Maarten Honing, Wilfried M. A. Niessen, Jeroen Kool, Jan N. M. Commandeur, Frans J. J. de Kanter, Nico P. E. Vermeulen, David Falck, Vanina Rea
Publikováno v:
Rea, V, Falck, D, Kool, J, de Kanter, F J J, Commandeur, J N M, Vermeulen, N P E, Niessen, W M A & Honing, M 2013, ' Combination of biotransformation by P450 BM3 mutants with
post-column bioaffinity and mass spectrometric profiling as a novel strategy to diversify and characterize p38α kinase inhibitors. ', MedChemComm, vol. 4, pp. 371-377 . https://doi.org/10.1039/c2md20283b
MedChemComm, 4, 371-377. Royal Society of Chemistry
post-column bioaffinity and mass spectrometric profiling as a novel strategy to diversify and characterize p38α kinase inhibitors. ', MedChemComm, vol. 4, pp. 371-377 . https://doi.org/10.1039/c2md20283b
MedChemComm, 4, 371-377. Royal Society of Chemistry
Mutants of bacterial cytochrome P450 BM3 from Bacillus megaterium have gained increasing interest to support drug metabolism studies by producing human relevant biotransformation products and/or to support drug discovery by producing libraries of new
Autor:
Harini Venkataraman, Jan N. M. Commandeur, Stephanie B.A. de Beer, Karlijn Keijzer, Vanina Rea, Daan P. Geerke, Laura A. H. van Bergen, Nico P. E. Vermeulen, F. Matthias Bickelhaupt, Célia Fonseca Guerra
Publikováno v:
Current Drug Metabolism, 13(2), 155-166. Bentham Science Publishers B.V.
de Beer, S B A, van Bergen, L A H, Keijzer, K, Rea, V, Venkataraman, H, Fonseca Guerra, C, Bickelhaupt, F M, Vermeulen, N P E, Commandeur, J N M & Geerke, D P 2012, ' The role of protein plasticity in computational rationalization studies on regioselectivity in testosterone hydroxylation by Cytochrome P450 BM3 mutants ', Current Drug Metabolism, vol. 13, no. 2, pp. 155-166 . https://doi.org/10.2174/138920012798918471
de Beer, S B A, van Bergen, L A H, Keijzer, K, Rea, V, Venkataraman, H, Fonseca Guerra, C, Bickelhaupt, F M, Vermeulen, N P E, Commandeur, J N M & Geerke, D P 2012, ' The role of protein plasticity in computational rationalization studies on regioselectivity in testosterone hydroxylation by Cytochrome P450 BM3 mutants ', Current Drug Metabolism, vol. 13, no. 2, pp. 155-166 . https://doi.org/10.2174/138920012798918471
Recently, it was found that mutations in the binding cavity of drug-metabolizing Cytochrome P450 BM3 mutants can result in major changes in regioselectivity in testosterone (TES) hydroxylation. In the current work, we report the intrinsic reactivity
Autor:
Sybren S. Wijmenga, Eduardo Vottero, Vanina Rea, Ard J. Kolkman, Nico P. E. Vermeulen, Kirsten A.M. Ampt, Jan N. M. Commandeur, E.J. Stronks, Maarten Honing
Publikováno v:
Biochemistry, 51, 750-760
Biochemistry, 51(3), 750-760. American Chemical Society
Rea, V, Kolkman, A J, Vottero, E R, Stronks, E J, Ampt, K A, Honing, M, Vermeulen, N P E, Wijmenga, S S & Commandeur, J N M 2012, ' Active Site Substitution A82W Improves the Regioselectivity of Steroid Hydroxylation by Cytochrome P450 BM3 Mutants As Rationalized by Spin Relaxation Nuclear Magnetic Resonance Studies ', Biochemistry, vol. 51, no. 3, pp. 750-760 . https://doi.org/10.1021/bi201433h
Biochemistry, 51, 3, pp. 750-760
Biochemistry, 51(3), 750-760. American Chemical Society
Rea, V, Kolkman, A J, Vottero, E R, Stronks, E J, Ampt, K A, Honing, M, Vermeulen, N P E, Wijmenga, S S & Commandeur, J N M 2012, ' Active Site Substitution A82W Improves the Regioselectivity of Steroid Hydroxylation by Cytochrome P450 BM3 Mutants As Rationalized by Spin Relaxation Nuclear Magnetic Resonance Studies ', Biochemistry, vol. 51, no. 3, pp. 750-760 . https://doi.org/10.1021/bi201433h
Biochemistry, 51, 3, pp. 750-760
Cytochrome P450 BM3 from Bacillus megaterium is a monooxygenase with great potential for biotechnological applications. In this paper, we present engineered drug-metabolizing P450 BM3 mutants as a novel tool for regioselective hydroxylation of steroi
Autor:
Jan Simon Boerma, Jan N. M. Commandeur, Vanina Rea, Sanja Dragovic, Nico P. E. Vermeulen, Frans J. J. de Kanter
Publikováno v:
Drug Metabolism and Disposition. 39:2411-2420
In the present study, a site-saturation mutagenesis library of drug-metabolizing CYP102A1 M11H with all 20 amino acids at position 87 was applied as a biocatalyst for the production of stable and reactive metabolites of clozapine. Clozapine is an aty
Cytochrome P450 BM3 Mutants as NOVEL Biocatalytic TOOLS for Regioselective Hydroxylation of Steroids
Autor:
Vanina Rea, Kolkman, J. A., Vottero, E., Honing, M., Wijmenga, S., Nico P.E. Vermeulen, Commandeur, Jan N. M.
Publikováno v:
Drug Metabolism Reviews, 42, pp. 285-286
Drug Metabolism Reviews, 42, 285-286. Informa Healthcare
Vrije Universiteit Amsterdam
Rea, V, Kolkman, J A, Vottero, E, Honing, M, Wijmenga, S, Vermeulen, N P E & Commandeur, J N M 2010, ' Cytochrome P450 BM3 Mutants as NOVEL Biocatalytic TOOLS for Regioselective Hydroxylation of Steroids ', Drug Metabolism Reviews, vol. 42, pp. 285-286 .
Drug Metabolism Reviews, 42, 285-286
Drug Metabolism Reviews, 42, 285-286. Informa Healthcare
Vrije Universiteit Amsterdam
Rea, V, Kolkman, J A, Vottero, E, Honing, M, Wijmenga, S, Vermeulen, N P E & Commandeur, J N M 2010, ' Cytochrome P450 BM3 Mutants as NOVEL Biocatalytic TOOLS for Regioselective Hydroxylation of Steroids ', Drug Metabolism Reviews, vol. 42, pp. 285-286 .
Drug Metabolism Reviews, 42, 285-286
Item does not contain fulltext 2 p.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::3e1aa597f532dfb6c6343df34500f72a
https://hdl.handle.net/2066/83716
https://hdl.handle.net/2066/83716
Autor:
Nico P. E. Vermeulen, Vanina Rea, Jeroen Lastdrager, Maarten Honing, Eduardo Vottero, Jan N. M. Commandeur
Publikováno v:
Journal of Biological Inorganic Chemistry-JBIC, 16(6), 899-912. Springer Verlag
Vottero, E R, Rea, V, Lastdrager, J, Honing, M, Vermeulen, N P E & Commandeur, J N M 2011, ' Role of residue 87 in substrate selectivity and regioselectivity of drug-metabolizing cytochrome P450 CYP102A1 M11 ', Journal of Biological Inorganic Chemistry-JBIC, vol. 16, no. 6, pp. 899-912 . https://doi.org/10.1007/s00775-011-0789-4
Journal of Biological Inorganic Chemistry
Vottero, E R, Rea, V, Lastdrager, J, Honing, M, Vermeulen, N P E & Commandeur, J N M 2011, ' Role of residue 87 in substrate selectivity and regioselectivity of drug-metabolizing cytochrome P450 CYP102A1 M11 ', Journal of Biological Inorganic Chemistry-JBIC, vol. 16, no. 6, pp. 899-912 . https://doi.org/10.1007/s00775-011-0789-4
Journal of Biological Inorganic Chemistry
CYP102A1, originating from Bacillus megaterium, is a highly active enzyme which has attracted much attention because of its potential applicability as a biocatalyst for oxidative reactions. Previously we developed drug-metabolizing mutant CYP102A1 M1