Literature DB >> 11684181

Induction of phenylalanine ammonia-lyase activity by tryptophan in Ustilago maydis.

S H Kim1, J W Kronstad, B E Ellis.   

Abstract

To understand the regulation of phenylalanine ammonia-lyase (PAL) activity in the corn smut fungus, Ustilago maydis, we examined the effects of different media, metabolic effectors (including aromatic amino acids), and environmental factors on induction and repression of PAL activity. PAL was detected only in cell extracts and not in the culture medium. U. maydis PAL is constitutively produced at a low level in all media tested but its regulation can be influenced by aromatic amino acids. L-Tryptophan (0.3 mM) induces PAL activity 3- to 5-fold but tryptophan analogs and tryptophan-related metabolites do not. The enzyme is most readily induced during the early stationary phase of growth and the induced activity remains relatively constant during stationary stage. No induction or inhibition of PAL activity was observed as a function of culture temperature, pH or light. PAL induction was repressed by glucose but not by its reaction product, t-cinnamic acid. Induction did not require de novo protein synthesis, suggesting that some form of post-translational protein modification or a metabolic effect may be involved. This study shows that the regulation of U. maydis PAL is very different from the patterns known for plants and other fungi.

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Year:  2001        PMID: 11684181     DOI: 10.1016/s0031-9422(01)00327-2

Source DB:  PubMed          Journal:  Phytochemistry        ISSN: 0031-9422            Impact factor:   4.072


  1 in total

1.  Cloning and Expression Analysis of Phenylalanine Ammonia-Lyase Gene in the Mycelium and Fruit Body of the Edible Mushroom Flammulina velutipes.

Authors:  Yeo Hong Yun; Ja Sun Koo; Seong Hwan Kim; Won Sik Kong
Journal:  Mycobiology       Date:  2015-09-30       Impact factor: 1.858

  1 in total

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