Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Nanne M. Kamerbeek"'
Publikováno v:
Journal of Biotechnology, 124(4), 670-689. Elsevier
Journal of Biotechnology 124 (2006) 4
Journal of Biotechnology, 124(4), 670-689
Journal of Biotechnology 124 (2006) 4
Journal of Biotechnology, 124(4), 670-689
During the last decades a large number of flavin-dependent monooxygenases have been isolated and studied. This has revealed that flavoprotein monooxygenases are able to catalyze a remarkable wide variety of oxidative reactions such as regioselective
Publikováno v:
European Journal of Biochemistry. 271:2107-2116
The Baeyer-Villiger monooxygenase (BVMO), 4-hydroxyacetophenone monooxygenase (HAPMO), uses NADPH and O(2) to oxidize a variety of aromatic ketones and sulfides. The FAD-containing enzyme has a 700-fold preference for NADPH over NADH. Sequence alignm
Autor:
NM Kamerbeek, Willem J. H. van Berkel, Wjh van Berkel, Marco W. Fraaije, Dick B. Janssen, Nanne M. Kamerbeek
Publikováno v:
Advanced Synthesis and Catalysis, 345(6-7), 667-678
Advanced Synthesis and Catalysis 345 (2003) 6-7
Advanced Synthesis and Catalysis 345 (2003) 6-7
Baeyer-Villiger monooxygenases (BVMOs) are flavoenzymes that catalyze a remarkably wide variety of oxidative reactions such as regio- and enantioselective Baeyer-Villiger oxidations and sulfoxidations. Several of these conversions are difficult to ac
Autor:
Mariëlle J. H. Moonen, Nanne M. Kamerbeek, Willem J. H. van Berkel, Jos G.M. van der Ven, Marco W. Fraaije, Dick B. Janssen
Publikováno v:
European Journal of Biochemistry 268 (2001) 9
European Journal of Biochemistry, 268(9), 2547-2557. Blackwell Publishing Ltd
European Journal of Biochemistry, 268(9), 2547-2557
European Journal of Biochemistry, 268(9), 2547-2557. Blackwell Publishing Ltd
European Journal of Biochemistry, 268(9), 2547-2557
A novel flavoprotein that catalyses the NADPH-dependent oxidation of 4-hydroxyacetophenone to 4-hydroxyphenyl acetate, was purified to homogeneity from Pseudomonas fluorescens ACB. Characterization of the purified enzyme showed that 4-hydroxyacetophe
Autor:
Nanne M. Kamerbeek, Dick B. Janssen, Riccardo Fortin, Annelies J. Heidekamp, Marco W. Fraaije
Publikováno v:
The Journal of Biological Chemistry, 279(11), 3354-3360. AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
EtaA is a newly identified FAD-containing monooxygenase that is responsible for activation of several thioamide prodrugs in Mycobacterium tuberculosis. It was found that purified EtaA displays a remarkably low activity with the antitubercular prodrug
Publikováno v:
Advanced Synthesis & Catalysis; Jun2003, Vol. 345 Issue 6/7, p667, 12p