Literature DB >> 20506361

Recombinant human cytochrome P450 monooxygenases for drug metabolite synthesis.

Kirsten Schroer1, Matthias Kittelmann, Stephan Lütz.   

Abstract

Cytochrome P450 monooxygenases (CYPs) are important enzymes in the metabolism of xenobiotics. Therefore, several approaches to clone and overexpress the human isoforms have been made. In addition to microsomes or S9 preparations, these recombinant human isoforms have found diverse application in drug development. We discuss and give examples of the use of bacterial whole cell systems with rec. human CYPs for the preparative scale synthesis of drug metabolites. (c) 2010 Wiley Periodicals, Inc.

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Year:  2010        PMID: 20506361     DOI: 10.1002/bit.22775

Source DB:  PubMed          Journal:  Biotechnol Bioeng        ISSN: 0006-3592            Impact factor:   4.530


  17 in total

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3.  Molecular Determinants of Substrate Affinity and Enzyme Activity of a Cytochrome P450BM3 Variant.

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5.  Tertiary alcohol preferred: Hydroxylation of trans-3-methyl-L-proline with proline hydroxylases.

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Journal:  Oxid Med Cell Longev       Date:  2015-06-09       Impact factor: 6.543

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Journal:  Toxicol Res       Date:  2014-09

8.  Draft Genome Sequences of Three Actinobacteria Strains Presenting New Candidate Organisms with High Potentials for Specific P450 Cytochromes.

Authors:  Christian Grumaz; Yevhen Vainshtein; Philipp Kirstahler; Stephan Luetz; Matthias Kittelmann; Kirsten Schroer; Fabian K Eggimann; Rico Czaja; Andreas Vogel; Thomas Hilberath; Anne Worsch; Marco Girhard; Vlada B Urlacher; Marcel Sandberg; Kai Sohn
Journal:  Genome Announc       Date:  2017-07-13

9.  Charged Tags for the Identification of Oxidative Drug Metabolites Based on Electrochemistry and Mass Spectrometry.

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10.  Co-expression of active human cytochrome P450 1A2 and cytochrome P450 reductase on the cell surface of Escherichia coli.

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Journal:  Microb Cell Fact       Date:  2016-02-02       Impact factor: 5.328

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