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Bacterial Model P450 Systems

The P450 cam camphor hydroxylase from Pseudomonas putida is one of the best characterised of all enzymes. It catalyses the 5-exo hydroxyla-tion of camphor, the first step in the breakdown of the eompound as an energy source (Sligar and Gunsalus, 1976). The atomie strueture of the P450 has been solved in a variety of different forms (substrate-free, eamphor-bound, inhibitor-bound, mutant forms) and was the first P450 for which a [Pg.302]


Gunsalus laboratory, the P450(, system allowed biochemical and biophysical investigation of the CYP catalytic cycle as well as of the genetics of a bacterial catabolic plasmid. This typical CYP system was found to require a ferredoxin and ferredoxin reductase for catalytic activity, unlike the model for eukaryote CYPs, CYP102A1 or P450g 3, which was discovered in the Fulco laboratory and consisted of a fusion polypeptide containing CYP and reductase domains. ... [Pg.586]


See other pages where Bacterial Model P450 Systems is mentioned: [Pg.302]    [Pg.302]    [Pg.131]    [Pg.303]    [Pg.1722]    [Pg.695]    [Pg.219]    [Pg.202]    [Pg.260]    [Pg.267]    [Pg.260]    [Pg.443]    [Pg.1610]    [Pg.95]    [Pg.135]    [Pg.88]    [Pg.278]    [Pg.339]    [Pg.342]    [Pg.413]    [Pg.112]    [Pg.219]   


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P450 Systems

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