Structural analysis of CYP101C1 from Novosphingobium aromaticivorans DSM12444

…, NH Rees, M Bartlam, W Zhou, LL Wong, Z Rao

Index: Ma, Ming; Bell, Stephen G.; Yang, Wen; Hao, Yiming; Rees, Nicholas H.; Bartlam, Mark; Zhou, Weihong; Wong, Luet-Lok; Rao, Zihe ChemBioChem, 2011 , vol. 12, # 1 p. 88 - 99

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Citation Number: 19

Abstract

Abstract 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 ...

~74%

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