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Structure and function of CYP108D1 from Novosphingobium aromaticivorans DSM12444: an aromatic hydrocarbon-binding P450 enzyme.

Abstract:

CYP108D1 from Novosphingobium aromaticivorans DSM12444 binds a range of aromatic hydrocarbons such as phenanthrene, biphenyl and phenylcyclohexane. Its structure, which is reported here at 2.2 Å resolution, is closely related to that of CYP108A1 (P450terp), an α-terpineol-oxidizing enzyme. The compositions and structures of the active sites of these two enzymes are very similar; the most significant changes are the replacement of Glu77 and Thr103 in CYP108A1 by Thr79 and Val105 in CYP108D1. O...

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Publication status:
Published

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Publisher copy:
10.1107/s090744491200145x

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Journal:
Acta crystallographica. Section D, Biological crystallography
Volume:
68
Issue:
Pt 3
Pages:
277-291
Publication date:
2012-03-05
DOI:
EISSN:
1399-0047
ISSN:
0907-4449
URN:
uuid:adc04479-3d18-4c71-9fa3-82aab6cd0155
Source identifiers:
312965
Local pid:
pubs:312965

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