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J. Biol. Chem., Vol. 278, Issue 30, 27483-27494, July 25, 2003

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Gene Cluster of Arthrobacter ilicis Rü61a Involved in the Degradation of Quinaldine to Anthranilate

CHARACTERIZATION AND FUNCTIONAL EXPRESSION OF THE QUINALDINE 4-OXIDASE qoxLMS GENES^*

Katja Parschat  , Bernhard Hauer ¶, Reinhard Kappl ||, Roswitha Kraft ||, Jürgen Hüttermann || and Susanne Fetzner   **

From the AG Mikrobiologie, Institut für Chemie und Biologie des Meeres, Carl von Ossietzky Universität Oldenburg, D-26111 Oldenburg, the Institut für Molekulare Mikrobiologie und Biotechnologie, Westfälische Wilhelms-Universität Münster, D-48149 Münster, ^¶BASF AG, ZHFD-B009, D-67056 Ludwigshafen, and the ^||Fachrichtung Biophysik und Physikalische Grundlagen der Medizin, Universität des Saarlandes, D-66421 HomburgSaar, Germany

A genetic analysis of the anthranilate pathway of quinaldine degradation was performed. A 23-kb region of DNA from Arthrobacter ilicis Rü61a was cloned into the cosmid pVK100. Although Escherichia coli clones containing the recombinant cosmid did not transform quinaldine, cosmids harboring the 23-kb region, or a 10.8-kb stretch of this region, conferred to Pseudomonas putida KT2440 the ability to cometabolically convert quinaldine to anthranilate. The 10.8-kb fragment thus contains the genes coding for quinaldine 4-oxidase (Qox), 1H-4-oxoquinaldine 3-monooxygenase, 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase, and N-acetylanthranilate amidase. The qoxLMS genes coding for the molybdopterin cytosine dinucleotide-(MCD-), FeSI-, FeSII-, and FAD-containing Qox were inserted into the expression vector pJB653, generating pKP1. Qox is the first MCD-containing enzyme to be synthesized in a catalytically fully competent form by a heterologous host, P. putida KT2440 pKP1; the catalytic properties and the UV-visible and EPR spectra of Qox purified from P. putida KT2440 pKP1 were essentially like those of wild-type Qox. This provides a starting point for the construction of protein variants of Qox by site-directed mutagenesis. Downstream of the qoxLMS genes, a putative gene whose deduced amino acid sequence showed 37% similarity to the cofactor-inserting chaperone XdhC was located. Additional open reading frames identified on the 23-kb segment may encode further enzymes (a glutamyl tRNA synthetase, an esterase, two short-chain dehydrogenases/reductases, an ATPase belonging to the AAA family, a 2-hydroxyhepta-2,4-diene-1,7-dioate isomerase/5-oxopent-3-ene-1,2,5-tricarboxylate decarboxylase-like protein, and an enzyme of the mandelate racemase group) and hypothetical proteins involved in transcriptional regulation, and metabolite transport.

Received for publication, February 6, 2003 , and in revised form, April 30, 2003.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBank^TM/EBI Data Bank with accession number(s) AJ537472.

^* This work was supported by the Deutsche Forschungsgemeinschaft (Grant FE 383/4-4) and the Fonds der Chemischen Industrie. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

^** To whom correspondence should be addressed. Tel.: 49-251-833-9824; Fax: 49-251-833-8388; E-mail: fetzner{at}uni-muenster.de.

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