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Structural Analysis of CYP101C1 from Novosphingobium aromaticivorans DSM12444.

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 the most regioselective (98 % at C3). The crystal structures of hexane-2,5-diol- and β-ionone-bo...

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Publication status:
Published

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Publisher copy:
10.1002/cbic.201000537

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Institution:
University of Oxford
Department:
Oxford, MPLS, Chemistry, Inorganic Chemistry
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Journal:
Chembiochem : a European journal of chemical biology
Volume:
12
Issue:
1
Pages:
88-99
Publication date:
2011-01-05
DOI:
EISSN:
1439-7633
ISSN:
1439-4227
URN:
uuid:106cc90c-347b-4125-86fa-8bf30a93e488
Source identifiers:
118881
Local pid:
pubs:118881

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