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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 -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. Ot...

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Publisher copy:
10.1107/S090744491200145X

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Journal:
Acta Crystallographica Section D: Biological Crystallography
Volume:
68
Issue:
3
Pages:
277-291
Publication date:
2012-03-01
DOI:
EISSN:
1399-0047
ISSN:
0907-4449
Source identifiers:
342920
Language:
English
Keywords:
Pubs id:
pubs:342920
UUID:
uuid:5c5bb2c2-87d7-4852-a36c-9edcd61f5a50
Local pid:
pubs:342920
Deposit date:
2012-12-19

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