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Journal article

The structure of CYP101D2 unveils a potential path for substrate entry into the active site.

Abstract:

The cytochrome P450 CYP101D2 from Novosphingobium aromaticivorans DSM12444 is closely related to CYP101D1 from the same bacterium and to P450cam (CYP101A1) from Pseudomonas putida. All three are capable of oxidizing camphor stereoselectively to 5-exo-hydroxycamphor. The crystal structure of CYP101D2 revealed that the likely ferredoxin-binding site on the proximal face is largely positively charged, similar to that of CYP101D1. However, both the native and camphor-soaked forms of CYP101D2 had ...

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Publication status:
Published

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Publisher copy:
10.1042/bj20101017

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Journal:
Biochemical journal
Volume:
433
Issue:
1
Pages:
85-93
Publication date:
2011-01-01
DOI:
EISSN:
1470-8728
ISSN:
0264-6021
Source identifiers:
139018
Language:
English
Keywords:
Pubs id:
pubs:139018
UUID:
uuid:3873c3ab-1fbf-4040-a1ee-88ece1bde722
Local pid:
pubs:139018
Deposit date:
2012-12-19

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