Structural Analysis of CYP101C1 from Novosphingobium aromaticivorans DSM12444.

Journal article

CYP101C1 from Novosphingobium aromaticivorans DSM12444 is a homologue of CYP101D1 and CYP101D2 enzymes from the same bacterium and CYP101A1 from Pseudomonas putida. CYP101C1 does not bind camphor but is capable of binding and hydroxylating ionone derivatives including α- and β-ionone and β-damascone. The activity of CYP101C1 was highest with β-damascone (k(cat)=86 s(-1)) but α-ionone oxidation was the most regioselective (98 % at C3). The crystal structures of hexane-2,5-diol- and β-ionone-bo...

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Authors: Ma, M; Bell, S; Yang, W; Hao, Y; Rees, N

• Publication status: Published
• Journal: Chembiochem : a European journal of chemical biology
• Volume: 12
• Issue: 1
• Pages: 88-99
• Publication date: 2011-01-01
• DOI: 10.1002/cbic.201000537
• EISSN: 1439-7633
• ISSN: 1439-4227
• Language: English
• Keywords: Heme; Models, Molecular; Substrate Specificity; Sphingomonadaceae; Camphor 5-Monooxygenase; Norisoprenoids; Kinetics; Catalytic Domain