Tryptophan catabolism in Bacillus megaterium

Author:

Bouknight R R,Sadoff H L

Abstract

Bacillus megaterium grows in a medium containing L-tryptophan as the sole carbon, nitrogen, and energy source. Kynurenine, anthranilic acid, and catechol are metabolic intermediates, suggesting that this organism used the anthranilic acid pathway for tryptophan degradation. Cells that grow on L-tryptophan oxidize kynurenine, alanine, and anthranilic acid and the presence of tryptophan oxygenase (EC 1.13.1.12), kynureninase (EC 3.7.1.3), and catechol oxygenase (EC 1.13.1.1) in cell extracts provide additional evidence for the degradative pathway in B. megaterium. Tryptophan oxygenase is inhibited by sodium azide, potassium cyanide, and hydroxylamine, indicating that the enzyme has a functional heme group. D-Tryptophan is not a substrate for tryptophan oxygenase, and the D-isomer does not inhibit this enzyme. Formamidase (EC 3.5.1.9) and anthranilate hydroxylase are not detectable in extracts. Tryptophan catabolism is inducible in B megaterium and is subject to catabolite repression by glucose and glutamate. Arginine does not cause repression, and kynurenine induces both tryptophan oxygenase and kynureninase.

Publisher

American Society for Microbiology

Subject

Molecular Biology,Microbiology

Reference19 articles.

1. Bernlohr R. W. 1965. Role of amino acids in sporulation p. 75-87. In L. L. Campbell and H. 0. Halvorson (ed.) Spores Ill. American Society for Microbiology Ann Arbor.

2. Regulation of enzymes involved in the conversion of tryptophan to nicotinamide adenine dinucleotide in a colorless strain of Xanthomonas pruni;Brown T.;J. Bacteriol.,1970

3. Differential amino acid requirements for sporulation in Bacillus subtilis;Doering L.;J. Bacteriol.,1972

4. On the activation and catalytic mechanism of microbial tryptophan pyrrolase;Feigelson P.;Biochem. Biophys. Res. Commun.,1964

5. Evidence for distinct kynureninase and hydroxykynureninase activities in Neurospora crassa;Gaertner F. H.;J. Bacteriol.,1971

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