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Diketocamphane monooxygenase

Diketocamphane 1,2-monooxygenase Pseudomonas putida ATCC 17453 2 2 identical substrate oxygenating subunits + NADH dehydrogenase NADH 78 (39 each) 1 FMN per subunit 7.2 [64]... [Pg.1215]

Figure 16.5-40. Cubic space filling models of active sites of right, 3,6-diketocam-phane 1,6-monooxygenase and left, 2,5-diketocamphane, 1,2-monooxygenase based on results of sulfoxidations of a series of sulfide substrates. Figure 16.5-40. Cubic space filling models of active sites of right, 3,6-diketocam-phane 1,6-monooxygenase and left, 2,5-diketocamphane, 1,2-monooxygenase based on results of sulfoxidations of a series of sulfide substrates.
Two diketocamphane monooxygenases from Pseudomonas putida were found to catalyze the oxidation of a wide range of sulfides with modest enantioselectivities, and predictive active-site models were proposed [133],... [Pg.352]

Jones KH, RT Smith, PW Trudgill (1993) Diketocamphane enantiomer-specific Bayer-Villiger monooxygenases from camphor-grown Pseudomonas putida ATCC 17453. J Gen Microbiol 139 797-805. [Pg.348]

See other pages where Diketocamphane monooxygenase is mentioned: [Pg.23]    [Pg.1210]    [Pg.867]    [Pg.1216]    [Pg.867]    [Pg.23]    [Pg.1210]    [Pg.1225]    [Pg.173]    [Pg.265]   
See also in sourсe #XX -- [ Pg.22 ]



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