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Journal of Bacteriology, December 2005, p. 8516-8519, Vol. 187, No. 24
0021-9193/05/$08.00+0     doi:10.1128/JB.187.24.8516-8519.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

An /ß-Fold CC Bond Hydrolase Is Involved in a Central Step of Nicotine Catabolism by Arthrobacter nicotinovorans

Institut für Biochemie und Molekularbiologie,¹ Institut für Organische Chemie und Biochemie,² Institut für Biologie III, Universität Freiburg, Freiburg, Germany³

Received 15 September 2005/ Accepted 22 September 2005

The enzyme catalyzing the hydrolytic cleavage of 2,6-dihydroxypseudooxynicotine to 2,6-dihydroxypyridine and -N-methylaminobutyrate was found to be encoded on pAO1 of Arthrobacter nicotinovorans. The new enzyme answers an old question about nicotine catabolism and may be the first CC bond hydrolase that is involved in the biodegradation of a heterocyclic compound.

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