3.4.23.24: Candidapepsin
This is an abbreviated version!
For detailed information about Candidapepsin, go to the full flat file.
Reaction
Preferential cleavage at the carboxyl of hydrophobic amino acids, but fails to cleave Leu15-Tyr, Tyr16-Leu and Phe24-Phe of insulin B chain. Activates trypsinogen, and degrades keratin
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Synonyms
Aspartate protease, aspartic protease, aspartic protease 2, aspartic protease Sap2p, aspartic proteinase 3, aspartyl protease, aspartyl protease Sap2p, aspartyl protease Sap4, aspartyl protease Sap5, aspartyl protease Sap6, aspartyl proteinase, candialbicin, Candida albicans aspartic proteinase, Candida albicans carboxyl proteinase, Candida albicans secretory acid proteinase, Candida albicans-secreted aspartic proteinase, Candida olea acid proteinase, Candidapepsin-1, candidapepsin-2, EC 3.4.23.6, EC 3.4.4.17, Proteinase, Candida albicans aspartic, Proteinase, Candida aspartic, Proteinase, Candida olea aspartic, S-aspartyl proteinase, SAP, SAP1, Sap10, SAP11, Sap1p, SAP2, Sap2p, SAP2X, SAP3, Sap3p, SAP4, Sap4p, SAP5, Sap5p, SAP6, Sap6p, Sap7, Sap7p, Sap8, Sap8p, Sap9, Sap9p, SAPP1, Sapp1p, SAPP2, Sapp2p, SAPP3, SAPT1, Sapt1p, SAPT2, SAPT3, SAPT4, secreted aspartic protease, secreted aspartic protease 1, secreted aspartic protease 2, secreted aspartic proteinase, secreted aspartic proteinase 1, secreted aspartic proteinase 2, secreted aspartic proteinase-2, secreted aspartyl peptidase, secreted aspartyl protease, secreted aspartyl protease 9, secreted aspartyl proteinase, secreted aspartyl proteinase 2, secreted aspartyl proteinase 5, secreted aspartyl proteinase2, secreted aspartyl proteinases, secreted aspartyl-type peptidase, secretory aspartyl proteinase, secretory aspartyl proteinase SAP1, secretory aspartyl proteinase SAP2p, secretory aspartyl proteinase SAP3p, secretory aspartyl proteinase SAP4p, secretory aspartyl proteinase SAP5p, secretory aspartyl proteinase SAP6p, yapsin, Yps
ECTree
Natural Substrates Products
Natural Substrates Products on EC 3.4.23.24 - Candidapepsin
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Bovine serum albumin + H2O
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complement component 3b + H2O
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substrate for isoforms Sapp1p and Sapp2p
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complement component 4b + H2O
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substrate for isoforms Sapp1p and Sapp2p
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complement component C3b + H2O
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complement component C4b + H2O
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complement component C5 + H2O
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factor H-related protein 5 + H2O
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substrate for isoform Sapp2p
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macrophage factor H-receptor CR3 + H2O
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the enzyme cleaves and inactivates macrophage factor H-receptor CR3
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macrophage factor H-receptor CR4 + H2O
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the enzyme cleaves and inactivates macrophage factor H-receptor CR4
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protein + H2O
hydrolyzed protein
additional information
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casein + H2O
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factor H + H2O
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the enzyme cleaves and inactivates factor H, diminishing its complement regulatory activity
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factor H + H2O
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substrate for isoforms Sapp1p and Sapp2p
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protein + H2O
hydrolyzed protein
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protein + H2O
hydrolyzed protein
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additional information
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the enzyme plays an important role in superficial infection by affecting the human stratum corneum of the skin and nail
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additional information
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the enzyme enables Candida albicans to use exogenous proteins as the sole source of nitrogen
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additional information
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candidapepsin is implicated in the degradation of host proteins involved in defense and barrier function
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additional information
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candidapepsin is implicated in the degradation of host proteins involved in defense and barrier function
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additional information
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candidapepsin is implicated in the degradation of host proteins involved in defense and barrier function. Sap2p degrades the Fc portion of IgG, IgA, complement factor C3 and endogenous protease inhibitors in human serum
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additional information
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candidapepsin is implicated in the degradation of host proteins involved in defense and barrier function. Sap2p degrades the Fc portion of IgG, IgA, complement factor C3 and endogenous protease inhibitors in human serum
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additional information
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distinct secreted aspartic proteinase plays a crucial role in the induction of chemokine response during Candida albicans vaginal infections
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additional information
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isoenzyme SAP1 is related to the vaginopathic potential of Candida albicans
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additional information
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isoenzyme SAP1 is related to the vaginopathic potential of Candida albicans
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additional information
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isoenzyme SAP1 is related to the vaginopathic potential of Candida albicans
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additional information
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isoenzyme SAP1 is related to the vaginopathic potential of Candida albicans
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additional information
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isoenzyme SAP1 is related to the vaginopathic potential of Candida albicans
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additional information
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isoenzyme SAP1 is related to the vaginopathic potential of Candida albicans
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additional information
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isoenzyme SAP1 is related to the vaginopathic potential of Candida albicans
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additional information
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isoenzyme SAP2 is related to the vaginopathic potential of Candida albicans
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additional information
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isoenzyme SAP2 is related to the vaginopathic potential of Candida albicans
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additional information
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isoenzyme SAP2 is related to the vaginopathic potential of Candida albicans
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additional information
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isoenzyme SAP2 is related to the vaginopathic potential of Candida albicans
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additional information
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isoenzyme SAP2 is related to the vaginopathic potential of Candida albicans
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additional information
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isoenzyme SAP2 is related to the vaginopathic potential of Candida albicans
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additional information
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isoenzyme SAP2 is related to the vaginopathic potential of Candida albicans
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additional information
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isoenzyme SAP3 is related to the vaginopathic potential of Candida albicans
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additional information
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isoenzyme SAP3 is related to the vaginopathic potential of Candida albicans
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additional information
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isoenzyme SAP3 is related to the vaginopathic potential of Candida albicans
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additional information
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isoenzyme SAP3 is related to the vaginopathic potential of Candida albicans
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additional information
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isoenzyme SAP3 is related to the vaginopathic potential of Candida albicans
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additional information
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isoenzyme SAP3 is related to the vaginopathic potential of Candida albicans
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additional information
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isoenzyme SAP3 is related to the vaginopathic potential of Candida albicans
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additional information
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isoenzyme SAP4 is correlated with systemic infections by Candida albicans
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additional information
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isoenzyme SAP4 is correlated with systemic infections by Candida albicans
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additional information
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isoenzyme SAP4 is correlated with systemic infections by Candida albicans
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additional information
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isoenzyme SAP4 is correlated with systemic infections by Candida albicans
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additional information
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isoenzyme SAP4 is correlated with systemic infections by Candida albicans
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additional information
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isoenzyme SAP4 is correlated with systemic infections by Candida albicans
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additional information
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isoenzyme SAP4 is correlated with systemic infections by Candida albicans
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additional information
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isoenzyme SAP5 is correlated with systemic infections by Candida albicans
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additional information
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isoenzyme SAP5 is correlated with systemic infections by Candida albicans
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additional information
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isoenzyme SAP5 is correlated with systemic infections by Candida albicans
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additional information
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isoenzyme SAP5 is correlated with systemic infections by Candida albicans
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additional information
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isoenzyme SAP5 is correlated with systemic infections by Candida albicans
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additional information
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isoenzyme SAP5 is correlated with systemic infections by Candida albicans
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additional information
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isoenzyme SAP5 is correlated with systemic infections by Candida albicans
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additional information
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isoenzyme SAP6 is correlated with systemic infections by Candida albicans
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additional information
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isoenzyme SAP6 is correlated with systemic infections by Candida albicans
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additional information
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isoenzyme SAP6 is correlated with systemic infections by Candida albicans
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additional information
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isoenzyme SAP6 is correlated with systemic infections by Candida albicans
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additional information
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isoenzyme SAP6 is correlated with systemic infections by Candida albicans
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additional information
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isoenzyme SAP6 is correlated with systemic infections by Candida albicans
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additional information
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isoenzyme SAP6 is correlated with systemic infections by Candida albicans
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additional information
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isoform Sap9 preferentially cleaves a peptide backbone at adjacent basic residues e.g. Lys-Arg or Arg-Arg when these are followed by an acidic amino acid residue
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