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Structural basis for cofactor-independent dioxygenation of N -heteroaromatic compounds at the α/β-hydrolase fold

Date

Authors

Steiner, Roberto A

Janssen, Helge J

Roversi, Pietro

Oakley, Aaron

Fetzner, Susanne

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

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

URI

http://hdl.handle.net/1885/55935

Collections

ANU Research Publications

Source

PNAS - Proceedings of the National Academy of Sciences of the United States of America

Type

Journal article

DOI

10.1073/pnas.0909033107

Restricted until

2037-12-31

Downloads

File

Description

01_Steiner_Structural_basis_for_2010.pdf (930.3 KB)

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