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Literature summary extracted from

  • Cano-Monreal, G.; Williams, J.; Heidner, H.
    An arthropod enzyme, Dfurin1, and a vertebrate furin homolog display distinct cleavage site sequence preferences for a shared viral proprotein substrate (2010), J. Insect Sci., 10, 29.
    View publication on PubMedView publication on EuropePMC

Organism

EC Number Organism UniProt Comment Textmining
3.4.21.75 Drosophila melanogaster P26016
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.21.75 additional information alternative PE2 cleavage phenotypes observed in vertebrate and arthropod cells are due to differences in substrate specificity between the arthropod and vertebrate furin enzymes and not to differences in host cell glycoprotein processing pathways Drosophila melanogaster ?
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3.4.21.75 PE2 glycoprotein precursor + H2O enzyme is involved in maturation of PE2 glycoprotein of alphaviruses. Enzyme cleaves efficiently PE2 glycoprotein mutants with residues arginine, serine, phenylalanine, histidine, asparagine, or aspartic acid at the +1 position Drosophila melanogaster ?
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Synonyms

EC Number Synonyms Comment Organism
3.4.21.75 Dfurin1
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Drosophila melanogaster

General Information

EC Number General Information Comment Organism
3.4.21.75 physiological function expression of Dfurin1 enhances Sindbis virus titers in RPE.40 cells by a factor of 100-1000, and this increase correlates with efficient cleavage of PE2 glycoprotein Drosophila melanogaster