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Structural basis for cofactor-independent dioxygenation of N-heteroaromatic compounds at the alpha/beta-hydrolase fold.

Abstract:

Enzymatic catalysis of oxygenation reactions in the absence of metal or organic cofactors is a considerable biochemical challenge. The CO-forming 1-H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase (HOD) from Arthrobacter nitroguajacolicus Rü61a and 1-H-3-hydroxy-4-oxoquinoline 2,4-dioxygenase (QDO) from Pseudomonas putida 33/1 are homologous cofactor-independent dioxygenases involved in the breakdown of N-heteroaromatic compounds. To date, they are the only dioxygenases suggested to belong to the ...

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Publication status:
Published

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Publisher copy:
10.1073/pnas.0909033107

Authors


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Institution:
University of Oxford
Division:
MSD
Department:
Pathology Dunn School
Role:
Author
Journal:
Proceedings of the National Academy of Sciences of the United States of America More from this journal
Volume:
107
Issue:
2
Pages:
657-662
Publication date:
2010-01-01
DOI:
EISSN:
1091-6490
ISSN:
0027-8424
Language:
English
Keywords:
Pubs id:
pubs:46151
UUID:
uuid:c7a20337-1965-4126-b84e-c15b70a23a53
Local pid:
pubs:46151
Source identifiers:
46151
Deposit date:
2012-12-19

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