This is an abbreviated version, for detailed information about Phytepsin, go to the full flat file.
Prefers hydrophobic residues Phe, Val, Ile, Leu, and Ala at P1 and P1', but also cleaves -Phe-/-Asp- and -Asp-/-Asp- bonds in 2S albumin from plant seeds
Acid protease, Ap1, Aspartic proteinase, Aspartyl endoproteinase, Barley grain aspartic proteinase, Carboxyl proteinase, CardA, cardB, Cardosin, cardosin A, cardosin B, Cynarase, cynarase A, cynarase B, cynarase C, Edestinase, HvAP, Nepenthesin, Oryzasin
Posttranslational Modification on EC 126.96.36.199 - Phytepsin
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structure contains two glycosylated peptide chains of 31 and 15 kDa. 19 sugar rings are attached to residues Asn67 and Asn257 localized on the molecular surface away from the conserved active site
isoform cynarase a, cynarase B, and cynarase C. Cynarase A contains N-linked high mannose-type glycans
sequence has a signal peptide of 27 amino acids and a prosegment containing Lys36 which is important for the stability of the enzyme and for the correct alignmentof the active-center residues
autocatalytic processing, optimal processing at pH 4.0
optimum pH for proteolytic activation of recombinant enzyme is pH 4.0
either the plant-specific insert domain or the C-terminal peptide VGFAEAA is necessary and sufficient to direct proteins to the vacuole. Both domains are vacuolar sorting determinants
autocatalytic processing of 48000 Da protein between N65s-D66s to 34000 Da and 14000 Da subunits, further processing of 34000 Da subunit to yield a 29000 Da subunit, enzyme consists of 29000 Da subunit plus 9000 Da subunit, connected by two disulfide bonds