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Literature summary for 3.5.1.98 extracted from

  • Baidyaroy, D.; Brosch, G.; Graessle, S.; Trojer, P.; Walton, J.D.
    Characterization of inhibitor-resistant histone deacetylase activity in plant-pathogenic fungi (2002), Eukaryot. Cell, 1, 538-547.
    View publication on PubMedView publication on EuropePMC

Inhibitors

Inhibitors Comment Organism Structure
HC-toxin cyclic peptide inhibitor from Cochliobolus carbonum. Histone deacetylase in crude extracts of Alternaria brassicola is relatively insensitive to inhibition, such as enzyme from Cochliobolus carbonum. Comparison of sensitivity in various Cochliobolus carbonum strains and in several other fungi Alternaria brassicicola
HC-toxin cyclic peptide inhibitor from Cochliobolus carbonum. Histone deacetylase in crude extracts of Cochliobolus carbonum is relatively insensitive to inhibition. Comparison of sensitivity in various Cochliobolus carbonum strains and in several other fungi. Resistance genetically cosegregates with toxin production Bipolaris zeicola
HC-toxin cyclic peptide inhibitor from Cochliobolus carbonum. Histone deacetylase in crude extracts of Diheterospora chlamydosporia is relatively insensitive to inhibition, such as enzyme from Cochliobolus carbonum. Comparison of sensitivity in various Cochliobolus carbonum strains and in several other fungi Pochonia chlamydosporia

Organism

Organism UniProt Comment Textmining
Alternaria brassicicola
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Bipolaris zeicola Q8X1S4
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Pochonia chlamydosporia
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