Literature DB >> 6209929

Hydrolytic ability of acid protease of Fusarium culmorum and its possible role in phytopathogenesis.

H Urbanek, G Yirdaw.   

Abstract

It was found that the acid protease of Fusarium culmorum can hydrolyze various proteins of plant origin including polygalacturonase inhibitor from bean (BPI) and soybean trypsin inhibitor (STI). The highest hydrolysis extent of BPI and STI by the enzyme was only 5% and 3% respectively. The partially hydrolyzed BPI lost its inhibition ability to fungal polyglacturonases. Similarly, the partially hydrolyzed STI lost its inhibition ability to trypsin and fungal alkaline protease. The F. culmorum acid protease showed broad substrate specificity towards synthetic dipeptides.

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Year:  1984        PMID: 6209929

Source DB:  PubMed          Journal:  Acta Microbiol Pol        ISSN: 0137-1320


  2 in total

1.  Widespread signatures of selection for secreted peptidases in a fungal plant pathogen.

Authors:  Parvathy Krishnan; Xin Ma; Bruce A McDonald; Patrick C Brunner
Journal:  BMC Evol Biol       Date:  2018-01-24       Impact factor: 3.260

2.  Unveiling the Secretome of the Fungal Plant Pathogen Neofusicoccum parvum Induced by In Vitro Host Mimicry.

Authors:  Forough Nazar Pour; Bruna Pedrosa; Micaela Oliveira; Cátia Fidalgo; Bart Devreese; Gonzalez Van Driessche; Carina Félix; Nuno Rosa; Artur Alves; Ana Sofia Duarte; Ana Cristina Esteves
Journal:  J Fungi (Basel)       Date:  2022-09-17
  2 in total

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