Literature DB >> 7264603

Metabolism of tryptophan by Pseudomonas aureofaciens and its relationship to pyrrolnitrin biosynthesis.

O Salcher, F Lingens.   

Abstract

Studies on the metabolism of tryptophan in Pseudomonas aureofaciens ATCC 15926 revealed different metabolic routes for the L- and D-isomer besides the biosynthetic pathway for pyrrolnitrin synthesis. L-Tryptophan catabolism follows the aromatic route via anthranilic acid. Tryptophan 2,3-dioxygenase were induced by L-tryptophan. Kynureninase and anthranilate 1,2-dioxygenase were induced by L-tryptophan, L-kynurenine and anthranilic acid. Anthranilate 1,2-dioxygenase was absent from a mutant strain of P. aureofaciens ATCC 19526 which produced about 30-fold increased amounts of pyrrolnitrin. The Km values of tryptophan 2,3-dioxygenase and kynureninase did not differ substantially between the two strains. Kynurenine 3-monooxygenase, 3-hydroxyanthranilate 3,4-dioxygenase, tryptophanase and indolyl-3-alkane alpha-hydroxylase activities were not detected. D- and L-tryptophan were converted to indole-3-acetic acid. This additional catabolic pathway was well as tryptophan racemase activity was constitutive and present in both strains.

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Year:  1980        PMID: 7264603     DOI: 10.1099/00221287-121-2-465

Source DB:  PubMed          Journal:  J Gen Microbiol        ISSN: 0022-1287


  3 in total

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Authors:  K S Lam; S Forenza; T W Doyle; C J Pearce
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2.  Purification of bromoperoxidase from Pseudomonas aureofaciens.

Authors:  K H van Pée; F Lingens
Journal:  J Bacteriol       Date:  1985-03       Impact factor: 3.490

3.  Bacterial NAD(P)-independent quinate dehydrogenase is a quinoprotein.

Authors:  M A van Kleef; J A Duine
Journal:  Arch Microbiol       Date:  1988-05       Impact factor: 2.552

  3 in total

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