Literature DB >> 17073788

Function and engineering of the 15beta-hydroxylase CYP106A2.

C Virus1, M Lisurek, B Simgen, F Hannemann, R Bernhardt.   

Abstract

CYP106A2 from Bacillus megaterium ATCC 13368 is a bacterial cytochrome P450 that is capable of transforming steroid hormones. It can be easily expressed in Escherichia coli with a high yield. Its activity in vitro can be achieved by using the adrenal redox proteins adrenodoxin and adrenodoxin reductase. So far, it was not possible to crystallize CYP106A2 because of degradation during the crystallization process. Nevertheless, CYP106A2 is an interesting enzyme for biotechnological use. It hydroxylates pharmaceutically important steroids such as progesterone and 11-deoxycortisol. However, it will be necessary for efficient application of CYP106A2 in biotechnology to improve the hydroxylation activity and manipulate the regiospecificity. The present paper gives an overview of recent developments in protein engineering of CYP106A2.

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Year:  2006        PMID: 17073788     DOI: 10.1042/BST0341215

Source DB:  PubMed          Journal:  Biochem Soc Trans        ISSN: 0300-5127            Impact factor:   5.407


  5 in total

1.  Role of residue 87 in substrate selectivity and regioselectivity of drug-metabolizing cytochrome P450 CYP102A1 M11.

Authors:  Eduardo Vottero; Vanina Rea; Jeroen Lastdrager; Maarten Honing; Nico P E Vermeulen; Jan N M Commandeur
Journal:  J Biol Inorg Chem       Date:  2011-05-13       Impact factor: 3.358

2.  Molecular evolution of a steroid hydroxylating cytochrome P450 using a versatile steroid detection system for screening.

Authors:  Cornelia Virus; Rita Bernhardt
Journal:  Lipids       Date:  2008-10-01       Impact factor: 1.880

3.  Steroid conversion with CYP106A2 - production of pharmaceutically interesting DHEA metabolites.

Authors:  Daniela Schmitz; Josef Zapp; Rita Bernhardt
Journal:  Microb Cell Fact       Date:  2014-06-05       Impact factor: 5.328

4.  Process development for the production of 15β-hydroxycyproterone acetate using Bacillus megaterium expressing CYP106A2 as whole-cell biocatalyst.

Authors:  Flora M Kiss; Marie T Lundemo; Josef Zapp; John M Woodley; Rita Bernhardt
Journal:  Microb Cell Fact       Date:  2015-03-05       Impact factor: 5.328

5.  Binding modes of CYP106A2 redox partners determine differences in progesterone hydroxylation product patterns.

Authors:  Tanja Sagadin; Jan L Riehm; Mohammed Milhim; Michael C Hutter; Rita Bernhardt
Journal:  Commun Biol       Date:  2018-07-30
  5 in total

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