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Applied and Environmental Microbiology, July 2006, p. 5126-5131, Vol. 72, No. 7
0099-2240/06/$08.00+0     doi:10.1128/AEM.00437-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

SHORT REPORT

A Functional mobA Gene for Molybdopterin Cytosine Dinucleotide Cofactor Biosynthesis Is Required for Activity and Holoenzyme Assembly of the Heterotrimeric Nicotine Dehydrogenases of Arthrobacter nicotinovorans

Paula Sachelaru,1 Emile Schiltz,2 and Roderich Brandsch1*

Institute of Biochemistry and Molecular Biology,1 Institute of Organic Chemistry and Biochemistry, University of Freiburg, Freiburg, Germany2

Received 23 February 2006/ Accepted 4 May 2006

Two Arthrobacter nicotinovorans molybdenum enzymes hydroxylate the pyridine ring of nicotine. Molybdopterin cytosine dinucleotide (MCD) was determined to be a cofactor of these enzymes. A mobA gene responsible for the formation of MCD could be identified and its function shown to be required for assembly of the heterotrimeric molybdenum enzymes.

* Corresponding author. Mailing address: Institute for Biochemistry and Molecular Biology, University of Freiburg, Hermann-Herder-Strasse 7, 79104 Freiburg, Germany. Phone: 49-761-2035231. Fax: 49-761-2035253. E-mail: roderich.brandsch{at}biochemie.uni-freiburg.de.

Applied and Environmental Microbiology, July 2006, p. 5126-5131, Vol. 72, No. 7
0099-2240/06/$08.00+0     doi:10.1128/AEM.00437-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Ganas, P., Brandsch, R. (2009). Uptake of L-nicotine and of 6-hydroxy-L-nicotine by Arthrobacter nicotinovorans and by Escherichia coli is mediated by facilitated diffusion and not by passive diffusion or active transport. Microbiology 155: 1866-1877 [Abstract] [Full Text]  


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