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Literature summary for 3.4.22.65 extracted from

  • Takahashi, K.; Takai, T.; Yasuhara, T.; Yokota, T.; Okumura, Y.
    Effects of site-directed mutagenesis in the cysteine residues and the N-glycosylation motif in recombinant Der f1 on secretion and protease activity (2001), Int. Arch. Allergy Immunol., 124, 454-460.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
wild-type pro-Der f1 is secreted to culture medium of baculovirus-transfeceted SF9 cells, pro-N53Q is not secreted in insect Sf9 cells although secreted in Pichia pastoris Dermatophagoides farinae

Protein Variants

Protein Variants Comment Organism
C104S/N53Q proform of mutant enzyme is not efficiently secreted into culture medium Dermatophagoides farinae
C118S/N53Q proform of mutant enzyme is not efficiently secreted into culture medium Dermatophagoides farinae
C32S/C72S/N63Q proform of mutant enzyme is not efficiently secreted into culture medium Dermatophagoides farinae
C32S/N53Q proform of mutant enzyme is not efficiently secreted into culture medium Dermatophagoides farinae
C35S/N53Q proform of mutant enzyme is efficiently secreted into culture medium. The secreted pro-C35S/N53Q is converted to the mature form by treatment in acidic conditions. Cysteine protease activity of the processed C35S/N53Q is lower than that of native Der f1 but significantly higher than that of the proenzyme Dermatophagoides farinae
C4S/N53Q proform of mutant enzyme is not efficiently secreted into culture medium Dermatophagoides farinae
C66S/C104S/N53Q proform of mutant enzyme is not efficiently secreted into culture medium Dermatophagoides farinae
C66S/N53Q proform of mutant enzyme is not efficiently secreted into culture medium Dermatophagoides farinae
C72S/N53Q proform of mutant enzyme is not efficiently secreted into culture medium Dermatophagoides farinae

Organism

Organism UniProt Comment Textmining
Dermatophagoides farinae
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Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein N-glycosylation is essential for secretion in insect Sf9 cells but not in Pichia pastoris Dermatophagoides farinae

Source Tissue

Source Tissue Comment Organism Textmining
culture medium wild-type pro-Der f1 is secreted to culture medium of baculovirus-transfeceted SF9 cells, but pro-N53Q is not Dermatophagoides farinae
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin + H2O
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Dermatophagoides farinae butyloxycarbonyl-Val-Leu-Lys + 7-amino-4-methylcoumarin
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