Literature DB >> 11570515

Cloning and disruption of a phenylalanine ammonia-lyase gene from Ustilago maydis.

S H Kim1, D Virmani, K Wake, K MacDonald, J W Kronstad, B E Ellis.   

Abstract

The enzyme L-phenylalanine ammonia-lyase (PAL) catalyzes the non-oxidative deamination of L-phenylalanine to form trans-cinnamic acid and ammonia. This enzyme is universally present in higher plants and it catalyzes the starting reaction for a central pathway that generates hundreds of different phenylpropanoid metabolites. Genes encoding PAL have been identified in fungi, but the role of the enzyme has not been determined. We cloned and characterized a gene that encodes PAL from the phytopathogenic fungus Ustilago maydis and we constructed fungal strains carrying a null mutation in the gene. These mutants behaved like wild-type strains in terms of growth, mating, and pathogenicity. These results indicate that PAL does not play a major role in the life cycle of U. maydis under laboratory conditions.

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Year:  2001        PMID: 11570515     DOI: 10.1007/s002940100230

Source DB:  PubMed          Journal:  Curr Genet        ISSN: 0172-8083            Impact factor:   3.886


  3 in total

1.  Fungal and Plant Phenylalanine Ammonia-lyase.

Authors:  Min Woo Hyun; Yeo Hong Yun; Jun Young Kim; Seong Hwan Kim
Journal:  Mycobiology       Date:  2011-12-07       Impact factor: 1.858

2.  Metabolic networks of microbial systems.

Authors:  Sumana Bhattacharya; Subhra Chakrabarti; Amiya Nayak; Sanjoy K Bhattacharya
Journal:  Microb Cell Fact       Date:  2003-04-11       Impact factor: 5.328

3.  Transcriptome analysis reveals new insight into appressorium formation and function in the rice blast fungus Magnaporthe oryzae.

Authors:  Yeonyee Oh; Nicole Donofrio; Huaqin Pan; Sean Coughlan; Douglas E Brown; Shaowu Meng; Thomas Mitchell; Ralph A Dean
Journal:  Genome Biol       Date:  2008-05-20       Impact factor: 13.583

  3 in total

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