Tryptophan Catabolism: Identification and Characterization of a New Degradative Pathway-Reference-Cited by-同舟云学术

Tryptophan Catabolism: Identification and Characterization of a New Degradative Pathway

Published:2005-11-15 Issue:22 Volume:187 Page:7866-7869
ISSN:0021-9193
Container-title:Journal of Bacteriology
language:en
Short-container-title:J Bacteriol

Author:

Colabroy Keri L.¹,Begley Tadhg P.²

Affiliation:

1. Department of Chemistry, Muhlenberg College, 2400 Chew Street, Allentown, Pennsylvania 18104

2. Department of Chemistry and Chemical Biology, 120 Baker Laboratory, Cornell University, Ithaca, New York 14853

Abstract

ABSTRACT 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.

Publisher

American Society for Microbiology

Subject

Molecular Biology,Microbiology

Link

https://journals.asm.org/doi/pdf/10.1128/JB.187.22.7866-7869.2005

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4. Colabroy K. L. 2005. Mechanistic and structural studies in tryptophan catabolism. Ph.D. thesis. Cornell University Ithaca N.Y.

5. Colabroy, K. L., and T. P. Begley. 2005. The pyridine ring of NAD is formed by a nonenzymatic pericyclic reaction. J. Am. Chem. Soc.127:840-841.

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