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Comparative Study
. 2005 Nov;187(22):7866-9.
doi: 10.1128/JB.187.22.7866-7869.2005.

Tryptophan catabolism: identification and characterization of a new degradative pathway

Keri L Colabroy  1 , Tadhg P Begley
Affiliations
Comparative Study

Tryptophan catabolism: identification and characterization of a new degradative pathway

Keri L Colabroy et al. J Bacteriol. 2005 Nov.

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.

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Figures

FIG. 1.
FIG. 1.
KEGG pathway for tryptophan degradation in eukaryotes. CoA, coenzyme A.
FIG. 2.
FIG. 2.
Region of Burkholderia cepacia J2315 chromosomal DNA containing genomic clusters of tryptophan catabolic genes.
FIG. 3.
FIG. 3.
New tryptophan catabolic pathway in B. cepacia J2315.
FIG. 4.
FIG. 4.
Sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis of tryptophan catabolic enzymes. Lane 1, molecular weight markers. Lane 2, cell extracts of the HAD overexpression strain. Lane 3, purified HAD. Lane 4, cell extracts of the ACMSD overexpression strain. Lane 5, purified ACMSD. Lane 6, cell extracts of the AMDH overexpression strain. Lane 7, purified AMDH. Lane 8, cell extracts of the AMD overexpression strain. Lane 9, purified AMD.
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References

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