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Journal of Bacteriology, November 2005, p. 7866-7869, Vol. 187, No. 22
0021-9193/05/$08.00+0 doi:10.1128/JB.187.22.7866-7869.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.
Department of Chemistry, Muhlenberg College, 2400 Chew Street, Allentown, Pennsylvania 18104,1 Department of Chemistry and Chemical Biology, 120 Baker Laboratory, Cornell University, Ithaca, New York 148532
Received 4 June 2005/ Accepted 24 August 2005
A new tryptophan catabolic pathway is characterized from Burkholderia cepacia J2315. In this pathway, tryptophan is converted to 2-amino-3-carboxymuconate semialdehyde, which is enzymatically degraded to pyruvate and acetate via the intermediates 2-aminomuconate and 4-oxalocrotonate. This pathway differs from the proposed mammalian pathway which converts 2-aminomuconate to 2-ketoadipate and, ultimately, glutaryl-coenzyme A.
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