Structural basis for cofactor-independent dioxygenation of N -heteroaromatic compounds at the α/β-hydrolase fold
Date
2010
Authors
Steiner, Roberto A
Janssen, Helge J
Roversi, Pietro
Oakley, Aaron
Fetzner, Susanne
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Publisher
National Academy of Sciences (USA)
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-hydr
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Keywords
Keywords: 1h 3 hydroxy 4 oxoquinaldine 2,4 dioxygenase; 1h 3 hydroxy 4 oxoquinoline 2,4 dioxygenase; dioxygenase; hydrolase; unclassified drug; Arthrobacter; Arthrobacter nitroguajacolicus; article; catalysis; crystal structure; enzyme active site; enzyme activity; Oxygen chemistry; Oxygenase; Structural enzymology
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PNAS - Proceedings of the National Academy of Sciences of the United States of America
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Journal article
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2037-12-31
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