Journal of Bacteriology 2005-12-01

An alpha/beta-fold C--C bond hydrolase is involved in a central step of nicotine catabolism by Arthrobacter nicotinovorans.

Paula Sachelaru, Emile Schiltz, Gabor L Igloi, Roderich Brandsch

Index: J. Bacteriol. 187(24) , 8516-9, (2005)

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Abstract

The enzyme catalyzing the hydrolytic cleavage of 2,6-dihydroxypseudooxynicotine to 2,6-dihydroxypyridine and gamma-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 C--C bond hydrolase that is involved in the biodegradation of a heterocyclic compound.

Related Compounds

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2,6-pyridinediol, hydrochloride Structure 2,6-pyridinediol, hydrochloride
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