Cloning, sequence analysis, and expression of the Pseudomonas putida 33/1 1H-3-hydroxy-4-oxoquinoline 2,4-dioxygenase gene, encoding a carbon monoxide forming dioxygenase

1H-3-hydroxy-4-oxoquinoline 2,4-dioxygenase (Qdo) from the 1H-4-oxoquinoline utilizing Pseudomonas putida strain 33/1, which catalyzes the cleavage of 1H-3-hydroxy-4-oxoquinoline to carbon monoxide and N-formylanthranilate, is devoid of any transition metal ion or other cofactor and thus represents...

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Bibliographic Details
Published in:Biochimica et biophysica acta 1999-05, Vol.1431 (2), p.547-552
Main Authors: Max, N, Betz, A, Facey, S, Lingens, F, Hauer, B, Fetzner, S
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Base Sequence
Dioxygenases
Molecular Sequence Data
Oxygenases - biosynthesis
Oxygenases - chemistry
Oxygenases - genetics
Pseudomonas putida - enzymology
Pseudomonas putida - genetics
Sequence Alignment
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Summary:1H-3-hydroxy-4-oxoquinoline 2,4-dioxygenase (Qdo) from the 1H-4-oxoquinoline utilizing Pseudomonas putida strain 33/1, which catalyzes the cleavage of 1H-3-hydroxy-4-oxoquinoline to carbon monoxide and N-formylanthranilate, is devoid of any transition metal ion or other cofactor and thus represents a novel type of ring-cleavage dioxygenase. Gene qdo was cloned and sequenced. Its overexpression in Escherichia coli yielded recombinant His-tagged Qdo which was catalytically active. Qdo exhibited 36% and 16% amino acid identity to 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase (Hod) and atropinesterase (a serine hydrolase), respectively. Qdo as well as Hod possesses a SXSHG motif, resembling the motif GXSXG of the serine hydrolases which comprises the active-site nucleophile (X=arbitrary residue).
ISSN:0006-3002
0167-4838
DOI:10.1016/S0167-4838(99)00083-7