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Crystal structure of CYP199A2, a para-substituted benzoic acid oxidizing cytochrome P450 from Rhodopseudomonas palustris.

Abstract:

CYP199A2, a cytochrome P450 enzyme from Rhodopseudomonas palustris, oxidatively demethylates 4-methoxybenzoic acid to 4-hydroxybenzoic acid. 4-Ethylbenzoic acid is converted to a mixture of predominantly 4-(1-hydroxyethyl)-benzoic acid and 4-vinylbenzoic acid, the latter being a rare example of CC bond dehydrogenation of an unbranched alkyl group. The crystal structure of CYP199A2 has been determined at 2.0-A resolution. The enzyme has the common P450 fold, but the B' helix is missing and the...

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Publication status:
Published

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Publisher copy:
10.1016/j.jmb.2008.08.033

Authors


Forward, I More by this author
Bartlam, M More by this author
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Journal:
Journal of molecular biology
Volume:
383
Issue:
3
Pages:
561-574
Publication date:
2008-11-05
DOI:
EISSN:
1089-8638
ISSN:
0022-2836
URN:
uuid:c0e654ea-8f23-4f72-8d00-aaeecbe679ae
Source identifiers:
34365
Local pid:
pubs:34365

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