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2-methoxy-2,4-diphenyl-3(2H)furanone + H2O
?
4-(4-dimethylaminophenylazo)benzoyl-gamma-aminobutyryl-Ile-His-Pro-Phe-His-Leu-Val-Ile-His-Thr-[5-(2-aminoethyl)-amino]naphthalene-1-sulfonic acid + H2O
4-(4-dimethylaminophenylazo)benzoyl-gamma-aminobutyryl-Ile-His-Pro-Phe-His-Leu-Val-Ile-His + Thr-[5-(2-aminoethyl)-amino]naphthalene-1-sulfonic acid
-
-
-
?
4-(4-dimethylaminophenylazo)benzoyl-gamma-aminobutyryl-Ile-His-Pro-Phe-His-Leu-Val-Ile-His-Thr-[5-(2-aminoethyl)-amino]naphthalene-1-sulfonic acid + H2O
?
-
-
-
?
4-(4-dimethylaminophenylazo)benzyl-Glu-His-Val-Lys-Leu-Val-Glu-5-(2-aminoethylamino)-1-naphthalenesulfonic acid + H2O
4-(4-dimethylaminophenylazo)benzyl-Glu-His-Val-Lys + Leu-Val-Glu-5-(2-aminoethylamino)-1-naphthalenesulfonic acid
4-(4-dimethylaminophenylazo)benzyl-Glu-His-Val-Lys-Leu-Val-Glu-5-(2-aminoethylamino)-1-naphthalenesulfonic acid + H2O
4-(4-dimethylaminophenylazo)benzyl-Glu-His-Val-Lys-Leu + Val-Glu-5-(2-aminoethylamino)-1-naphthalenesulfonic acid
4-(4-dimethylaminophenylazo)benzyl-Pro-Lys-Val-Glu-Leu-Thr-Gly-Glu-5-(2-aminoethylamino)-1-naphthalenesulfonic acid + H2O
4-(4-dimethylaminophenylazo)benzyl-Pro-Lys-Val-Glu + Leu-Thr-Gly-Glu-5-(2-aminoethylamino)-1-naphthalenesulfonic acid
Ala-Thr-His-Gln-Val-Tyr-4-nitrophenylalanine-Val-Arg-Lys-Ala + H2O
Ala-Thr-His-Gln-Val-Tyr + 4-nitrophenylalanine-Val-Arg-Lys-Ala
-
-
-
-
?
Arg-Glu-[5-(aminoethyl)aminonaphthalene sulfonate]-Ile-His-Pro-Phe-His-Leu-Val-Ile-His-Thr-Lys-[4'-dimethylaminoazobenzene-4-carboxylate]-Arg + H2O
?
azocasein + H2O
?
-
-
-
-
?
Azocoll + H2O
?
-
-
-
-
?
Bovine serum albumin + H2O
?
Bovine serum albumin + H2O
Hydrolyzed bovine serum albumin
complement component 3b + H2O
?
substrate for isoforms Sapp1p and Sapp2p
-
-
?
complement component 4b + H2O
?
substrate for isoforms Sapp1p and Sapp2p
-
-
?
complement component C3b + H2O
?
-
-
-
-
?
complement component C4b + H2O
?
-
-
-
-
?
complement component C5 + H2O
?
-
-
-
-
?
complement components C3b + H2O
?
-
substrate for isoforms Sap1, Sap2, Sap3, but not for Sap9
-
-
?
complement components C4b + H2O
?
-
substrate for isoforms Sap1, Sap2, Sap3, but not for Sap9
-
-
?
complement components C5 + H2O
?
-
substrate for isoforms Sap1, Sap2, Sap3, but not for Sap9
-
-
?
Dabcyl-EHVKLVE-EDANS + H2O
?
-
-
-
-
?
dabcyl-Glu-His-Val-Lys-Leu-Val-Glu-EDANS
dabcyl-Glu-His-Val-Lys-COOH + Leu-Val-Glu-EDANS
dabcyl-Glu-His-Val-Lys-Leu-Val-Glu-EDANS + H2O
dabcyl-Glu-His-Val-Lys-Leu + Val-Glu-EDANS
dabcyl-Pro-Lys-Val-Glu-Leu-Thr-Gly-Glu-EDANS
dabcyl-Pro-Lys-Val-Glu-COOH + Leu-Thr-Gly-Glu-EDANS
E-cadherin + H2O
?
-
Candida albicans strains JKC19 and SC5314 degrade E-cadherin at pH 4.0, the 10fold concentrated growth media of the strains HLC-52, HLC-54, 32723 and B1134 cause degradation at pH 4.0, strains HLC-52 and HLC-54 also at pH 6.0
-
-
?
ELSKRSSPS + H2O
ELSK + L-Arg + SSPS
factor H-related protein 5 + H2O
?
substrate for isoform Sapp2p
-
-
?
fluorescein-labeled casein + H2O
?
FRETS-25Ala + H2O
?
isozyme Sap1 shows highest activity towards FRETS-25Ala
-
-
?
FRETS-25Xaa + H2O
?
all Sap isozymes prefer Arg and Lys at the Xaa position
-
-
?
hide powder azure + H2O
?
-
-
-
-
?
Human stratum corneum + H2O
?
-
-
-
-
?
L-Arg-7-amido-4-methylcoumarin + H2O
L-Arg + 7-amino-4-methylcoumarin
LPVNATSE + H2O
LPVN + ATSE
LTEKRDSIS + H2O
LTEKR + L-Asp + Ser-Ile-Ser
Lys-Pro-Ala-Arg-Phe-Nph-Arg-Leu + H2O
?
-
-
-
?
Lys-Pro-Ala-Arg-Phe-Nph-Arg-Leu + H2O
Lys-Pro-Ala-Arg-Phe + Nph-Arg-Leu
-
-
-
?
Lys-Pro-Ala-Glu-Phe-4-nitrophenylalanine-Ala-Leu + H2O
Lys-Pro-Ala-Glu-Phe + 4-nitrophenylalanine-Ala-Leu
-
-
-
-
?
Lys-Pro-Leu-Glu-Met-4-nitrophenylalanine-Ala-Leu + H2O
Lys-Pro-Leu-Glu-Met + 4-nitrophenylalanine-Ala-Leu
-
-
-
-
?
macrophage factor H-receptor CR3 + H2O
?
-
the enzyme cleaves and inactivates macrophage factor H-receptor CR3
-
-
?
macrophage factor H-receptor CR4 + H2O
?
-
the enzyme cleaves and inactivates macrophage factor H-receptor CR4
-
-
?
Myeloma proteins of the type A1 and A2 + H2O
?
oxidized insulin B chain + H2O
?
cleavage sites of Sap2p: FV-/-NQHLCGSHL-/-V-/-EA-/-LYLVCGERGFF-/-YTPKA
-
-
?
Oxidized insulin B-chain + H2O
?
-
low side-chain specificity, preferential attack on hydrophobic amino acid residues
-
-
?
PMVELAGE + H2O
PMVE + L-Leu + AGE
PMVELAGE + H2O
PMVEL + AGE
cleavage of Sapp1p, 100% conversion
-
-
?
PMVELGGE + H2O
PMVEL + GGE
100% conversion
-
-
?
PMVELHGE + H2O
PMVEL + HGE
100% conversion
-
-
?
PMVELPGE + H2O
PMVEL + PGE
100% conversion
-
-
?
PMVELQGE + H2O
PMVE + L-Leu + QGE
cleavage of Sapp2p, 18% conversion
-
-
?
PMVELQGE + H2O
PMVEL + QGE
cleavage of Sapp1p, 100% conversion
-
-
?
PMVELTGE + 2 H2O
PMVE + L-Leu + TGE
cleavage of Sapp2p, 35% conversion
-
-
?
PMVELTGE + H2O
PMVEL + TGE
cleavage of Sapp1p, 100% conversion
-
-
?
PMVELWGE + H2O
PMVE + L-Leu + WGE
cleavage of Sapp2p, 40% conversion
-
-
?
PMVELWGE + H2O
PMVEL + WGE
cleavage of Sapp1p, 76% conversion
-
-
?
PMVEMWGE + H2O
PMVEM + WGE
100% conversion
-
-
?
PMVMLWGE + H2O
PMVML + WGE
protein + H2O
hydrolyzed protein
Proteinase inhibitors of human serum + H2O
?
-
-
-
-
?
additional information
?
-
2-methoxy-2,4-diphenyl-3(2H)furanone + H2O
?
-
-
-
?
2-methoxy-2,4-diphenyl-3(2H)furanone + H2O
?
-
-
-
?
4-(4-dimethylaminophenylazo)benzyl-Glu-His-Val-Lys-Leu-Val-Glu-5-(2-aminoethylamino)-1-naphthalenesulfonic acid + H2O
4-(4-dimethylaminophenylazo)benzyl-Glu-His-Val-Lys + Leu-Val-Glu-5-(2-aminoethylamino)-1-naphthalenesulfonic acid
Sapp2p preferentially cleaves the Lys-Leu bond
-
-
?
4-(4-dimethylaminophenylazo)benzyl-Glu-His-Val-Lys-Leu-Val-Glu-5-(2-aminoethylamino)-1-naphthalenesulfonic acid + H2O
4-(4-dimethylaminophenylazo)benzyl-Glu-His-Val-Lys + Leu-Val-Glu-5-(2-aminoethylamino)-1-naphthalenesulfonic acid
Sapp2p preferentially cleaves the Lys-Leu bond
-
-
?
4-(4-dimethylaminophenylazo)benzyl-Glu-His-Val-Lys-Leu-Val-Glu-5-(2-aminoethylamino)-1-naphthalenesulfonic acid + H2O
4-(4-dimethylaminophenylazo)benzyl-Glu-His-Val-Lys-Leu + Val-Glu-5-(2-aminoethylamino)-1-naphthalenesulfonic acid
Sapp1p preferentially cleaves the Leu-Val bond
-
-
?
4-(4-dimethylaminophenylazo)benzyl-Glu-His-Val-Lys-Leu-Val-Glu-5-(2-aminoethylamino)-1-naphthalenesulfonic acid + H2O
4-(4-dimethylaminophenylazo)benzyl-Glu-His-Val-Lys-Leu + Val-Glu-5-(2-aminoethylamino)-1-naphthalenesulfonic acid
Sapp1p preferentially cleaves the Leu-Val bond
-
-
?
4-(4-dimethylaminophenylazo)benzyl-Pro-Lys-Val-Glu-Leu-Thr-Gly-Glu-5-(2-aminoethylamino)-1-naphthalenesulfonic acid + H2O
4-(4-dimethylaminophenylazo)benzyl-Pro-Lys-Val-Glu + Leu-Thr-Gly-Glu-5-(2-aminoethylamino)-1-naphthalenesulfonic acid
the substrate is hydrolyzed preferentially at the Glu-Leu bond, however, when reaction times are prolonged, additional cleavage occurs at the Lys-Val position
-
-
?
4-(4-dimethylaminophenylazo)benzyl-Pro-Lys-Val-Glu-Leu-Thr-Gly-Glu-5-(2-aminoethylamino)-1-naphthalenesulfonic acid + H2O
4-(4-dimethylaminophenylazo)benzyl-Pro-Lys-Val-Glu + Leu-Thr-Gly-Glu-5-(2-aminoethylamino)-1-naphthalenesulfonic acid
the substrate is hydrolyzed preferentially at the Glu-Leu bond, however, when reaction times are prolonged, additional cleavage occurs at the Lys-Val position
-
-
?
Albumin + H2O
?
-
-
-
-
?
Albumin + H2O
?
-
low side-chain specificity, preferential attack on hydrophobic amino acid residues
-
-
?
Albumin + H2O
?
cleavage by Sap2p shows a low side-chain specificity
-
-
?
Albumin + H2O
?
-
-
-
-
?
Arg-Glu-[5-(aminoethyl)aminonaphthalene sulfonate]-Ile-His-Pro-Phe-His-Leu-Val-Ile-His-Thr-Lys-[4'-dimethylaminoazobenzene-4-carboxylate]-Arg + H2O
?
-
-
-
?
Arg-Glu-[5-(aminoethyl)aminonaphthalene sulfonate]-Ile-His-Pro-Phe-His-Leu-Val-Ile-His-Thr-Lys-[4'-dimethylaminoazobenzene-4-carboxylate]-Arg + H2O
?
-
-
-
?
Bovine serum albumin + H2O
?
-
-
-
?
Bovine serum albumin + H2O
?
-
-
-
-
?
Bovine serum albumin + H2O
?
-
-
-
-
?
Bovine serum albumin + H2O
?
-
-
-
-
?
Bovine serum albumin + H2O
?
-
-
-
-
?
Bovine serum albumin + H2O
?
-
-
-
-
?
Bovine serum albumin + H2O
?
-
-
-
-
?
Bovine serum albumin + H2O
?
-
-
-
-
?
Bovine serum albumin + H2O
Hydrolyzed bovine serum albumin
-
-
-
?
Bovine serum albumin + H2O
Hydrolyzed bovine serum albumin
-
-
-
?
casein + H2O
?
-
isoforms Sap1, Sap2, Sap3, and Sap9 cleave casein
-
-
?
casein + H2O
?
isozyme Sap6 shows highest activity towards casein
-
-
?
Collagen + H2O
?
-
-
-
-
?
Collagen + H2O
?
-
-
-
-
?
dabcyl-Glu-His-Val-Lys-Leu-Val-Glu-EDANS
dabcyl-Glu-His-Val-Lys-COOH + Leu-Val-Glu-EDANS
-
-
-
?
dabcyl-Glu-His-Val-Lys-Leu-Val-Glu-EDANS
dabcyl-Glu-His-Val-Lys-COOH + Leu-Val-Glu-EDANS
-
-
-
?
dabcyl-Glu-His-Val-Lys-Leu-Val-Glu-EDANS + H2O
dabcyl-Glu-His-Val-Lys-Leu + Val-Glu-EDANS
-
-
-
-
?
dabcyl-Glu-His-Val-Lys-Leu-Val-Glu-EDANS + H2O
dabcyl-Glu-His-Val-Lys-Leu + Val-Glu-EDANS
-
-
-
-
?
dabcyl-Pro-Lys-Val-Glu-Leu-Thr-Gly-Glu-EDANS
dabcyl-Pro-Lys-Val-Glu-COOH + Leu-Thr-Gly-Glu-EDANS
-
-
-
?
dabcyl-Pro-Lys-Val-Glu-Leu-Thr-Gly-Glu-EDANS
dabcyl-Pro-Lys-Val-Glu-COOH + Leu-Thr-Gly-Glu-EDANS
-
-
-
?
ELSKRSSPS + H2O
ELSK + L-Arg + SSPS
98% conversion
-
-
?
ELSKRSSPS + H2O
ELSK + L-Arg + SSPS
98% conversion
-
-
?
factor H + H2O
?
-
the enzyme cleaves and inactivates factor H, diminishing its complement regulatory activity
-
-
?
factor H + H2O
?
substrate for isoforms Sapp1p and Sapp2p
-
-
?
fluorescein-labeled casein + H2O
?
-
-
-
?
fluorescein-labeled casein + H2O
?
-
-
-
?
Hemoglobin + H2O
?
-
-
-
-
?
Hemoglobin + H2O
?
-
-
-
-
?
Hemoglobin + H2O
?
-
-
-
-
?
Keratin + H2O
?
-
-
-
-
?
Keratin + H2O
?
-
-
-
-
?
Keratin + H2O
?
-
-
-
-
?
L-Arg-7-amido-4-methylcoumarin + H2O
L-Arg + 7-amino-4-methylcoumarin
-
-
-
?
L-Arg-7-amido-4-methylcoumarin + H2O
L-Arg + 7-amino-4-methylcoumarin
-
-
-
?
LPVNATSE + H2O
LPVN + ATSE
28% conversion
-
-
?
LPVNATSE + H2O
LPVN + ATSE
28% conversion
-
-
?
LTEKRDSIS + H2O
LTEKR + L-Asp + Ser-Ile-Ser
100% conversion
-
-
?
LTEKRDSIS + H2O
LTEKR + L-Asp + Ser-Ile-Ser
100% conversion
-
-
?
Myeloma proteins of the type A1 and A2 + H2O
?
-
-
-
-
?
Myeloma proteins of the type A1 and A2 + H2O
?
-
-
-
-
?
PMVELAGE + H2O
PMVE + L-Leu + AGE
cleavage of Sapp2p, 81% conversion
-
-
?
PMVELAGE + H2O
PMVE + L-Leu + AGE
cleavage of Sapp2p, 81% conversion
-
-
?
PMVMLWGE + H2O
PMVML + WGE
13% conversion
-
-
?
PMVMLWGE + H2O
PMVML + WGE
98% conversion
-
-
?
protein + H2O
hydrolyzed protein
-
-
-
?
protein + H2O
hydrolyzed protein
-
-
-
?
additional information
?
-
-
substrate specificity
-
-
?
additional information
?
-
-
trypsinogen kinase activity
-
-
?
additional information
?
-
-
not: horse ferritin
-
-
?
additional information
?
-
-
synthetic anilides
-
-
?
additional information
?
-
-
clots milk at pH 5.5
-
-
?
additional information
?
-
-
the enzyme plays an important role in superficial infection by affecting the human stratum corneum of the skin and nail
-
-
?
additional information
?
-
-
the enzyme enables Candida albicans to use exogenous proteins as the sole source of nitrogen
-
-
?
additional information
?
-
candidapepsin is implicated in the degradation of host proteins involved in defense and barrier function
-
-
?
additional information
?
-
candidapepsin is implicated in the degradation of host proteins involved in defense and barrier function
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
distinct secreted aspartic proteinase plays a crucial role in the induction of chemokine response during Candida albicans vaginal infections
-
-
?
additional information
?
-
isoenzyme SAP1 is related to the vaginopathic potential of Candida albicans
-
-
?
additional information
?
-
isoenzyme SAP1 is related to the vaginopathic potential of Candida albicans
-
-
?
additional information
?
-
isoenzyme SAP1 is related to the vaginopathic potential of Candida albicans
-
-
?
additional information
?
-
isoenzyme SAP1 is related to the vaginopathic potential of Candida albicans
-
-
?
additional information
?
-
isoenzyme SAP1 is related to the vaginopathic potential of Candida albicans
-
-
?
additional information
?
-
isoenzyme SAP1 is related to the vaginopathic potential of Candida albicans
-
-
?
additional information
?
-
-
isoenzyme SAP1 is related to the vaginopathic potential of Candida albicans
-
-
?
additional information
?
-
isoenzyme SAP2 is related to the vaginopathic potential of Candida albicans
-
-
?
additional information
?
-
isoenzyme SAP2 is related to the vaginopathic potential of Candida albicans
-
-
?
additional information
?
-
isoenzyme SAP2 is related to the vaginopathic potential of Candida albicans
-
-
?
additional information
?
-
isoenzyme SAP2 is related to the vaginopathic potential of Candida albicans
-
-
?
additional information
?
-
isoenzyme SAP2 is related to the vaginopathic potential of Candida albicans
-
-
?
additional information
?
-
isoenzyme SAP2 is related to the vaginopathic potential of Candida albicans
-
-
?
additional information
?
-
-
isoenzyme SAP2 is related to the vaginopathic potential of Candida albicans
-
-
?
additional information
?
-
isoenzyme SAP3 is related to the vaginopathic potential of Candida albicans
-
-
?
additional information
?
-
isoenzyme SAP3 is related to the vaginopathic potential of Candida albicans
-
-
?
additional information
?
-
isoenzyme SAP3 is related to the vaginopathic potential of Candida albicans
-
-
?
additional information
?
-
isoenzyme SAP3 is related to the vaginopathic potential of Candida albicans
-
-
?
additional information
?
-
isoenzyme SAP3 is related to the vaginopathic potential of Candida albicans
-
-
?
additional information
?
-
isoenzyme SAP3 is related to the vaginopathic potential of Candida albicans
-
-
?
additional information
?
-
-
isoenzyme SAP3 is related to the vaginopathic potential of Candida albicans
-
-
?
additional information
?
-
isoenzyme SAP4 is correlated with systemic infections by Candida albicans
-
-
?
additional information
?
-
isoenzyme SAP4 is correlated with systemic infections by Candida albicans
-
-
?
additional information
?
-
isoenzyme SAP4 is correlated with systemic infections by Candida albicans
-
-
?
additional information
?
-
isoenzyme SAP4 is correlated with systemic infections by Candida albicans
-
-
?
additional information
?
-
isoenzyme SAP4 is correlated with systemic infections by Candida albicans
-
-
?
additional information
?
-
isoenzyme SAP4 is correlated with systemic infections by Candida albicans
-
-
?
additional information
?
-
-
isoenzyme SAP4 is correlated with systemic infections by Candida albicans
-
-
?
additional information
?
-
isoenzyme SAP5 is correlated with systemic infections by Candida albicans
-
-
?
additional information
?
-
isoenzyme SAP5 is correlated with systemic infections by Candida albicans
-
-
?
additional information
?
-
isoenzyme SAP5 is correlated with systemic infections by Candida albicans
-
-
?
additional information
?
-
isoenzyme SAP5 is correlated with systemic infections by Candida albicans
-
-
?
additional information
?
-
isoenzyme SAP5 is correlated with systemic infections by Candida albicans
-
-
?
additional information
?
-
isoenzyme SAP5 is correlated with systemic infections by Candida albicans
-
-
?
additional information
?
-
-
isoenzyme SAP5 is correlated with systemic infections by Candida albicans
-
-
?
additional information
?
-
isoenzyme SAP6 is correlated with systemic infections by Candida albicans
-
-
?
additional information
?
-
isoenzyme SAP6 is correlated with systemic infections by Candida albicans
-
-
?
additional information
?
-
isoenzyme SAP6 is correlated with systemic infections by Candida albicans
-
-
?
additional information
?
-
isoenzyme SAP6 is correlated with systemic infections by Candida albicans
-
-
?
additional information
?
-
isoenzyme SAP6 is correlated with systemic infections by Candida albicans
-
-
?
additional information
?
-
isoenzyme SAP6 is correlated with systemic infections by Candida albicans
-
-
?
additional information
?
-
-
isoenzyme SAP6 is correlated with systemic infections by Candida albicans
-
-
?
additional information
?
-
extremely broad specificity range
-
-
?
additional information
?
-
extremely broad specificity range
-
-
?
additional information
?
-
-
Candida albicans strain SC5314 Sap1-6 mutants do not degrade E-cadherin
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
trypsinogen kinase activity
-
-
?
additional information
?
-
-
not: horse ferritin
-
-
?
additional information
?
-
-
clots milk at pH 5.5
-
-
?
additional information
?
-
sapp2p fails to cleave Lys-Pro-Ala-Glu-Phe-Phe(p-NO2)-Ala-Leu
-
-
?
additional information
?
-
-
sapp2p fails to cleave Lys-Pro-Ala-Glu-Phe-Phe(p-NO2)-Ala-Leu
-
-
?
additional information
?
-
isoform Sapp2p has a more restricted substrate specificity and significantly lower catalytic activity than isoform Sapp1p
-
-
?
additional information
?
-
isoform Sapp2p has a more restricted substrate specificity and significantly lower catalytic activity than isoform Sapp1p
-
-
?
additional information
?
-
-
isoform Sapp2p has a more restricted substrate specificity and significantly lower catalytic activity than isoform Sapp1p
-
-
?
additional information
?
-
no hydrolysis of PMVELPGE, PMVELHGE, PMVELGGE, PMVEMWGE, LPVNATSE, LTEKRDSIS, and ELSKRSSPS
-
-
?
additional information
?
-
no hydrolysis of PMVELPGE, PMVELHGE, PMVELGGE, PMVEMWGE, LPVNATSE, LTEKRDSIS, and ELSKRSSPS
-
-
?
additional information
?
-
-
no hydrolysis of PMVELPGE, PMVELHGE, PMVELGGE, PMVEMWGE, LPVNATSE, LTEKRDSIS, and ELSKRSSPS
-
-
?
additional information
?
-
sapp2p fails to cleave Lys-Pro-Ala-Glu-Phe-Phe(p-NO2)-Ala-Leu
-
-
?
additional information
?
-
isoform Sapp2p has a more restricted substrate specificity and significantly lower catalytic activity than isoform Sapp1p
-
-
?
additional information
?
-
isoform Sapp2p has a more restricted substrate specificity and significantly lower catalytic activity than isoform Sapp1p
-
-
?
additional information
?
-
no hydrolysis of PMVELPGE, PMVELHGE, PMVELGGE, PMVEMWGE, LPVNATSE, LTEKRDSIS, and ELSKRSSPS
-
-
?
additional information
?
-
no hydrolysis of PMVELPGE, PMVELHGE, PMVELGGE, PMVEMWGE, LPVNATSE, LTEKRDSIS, and ELSKRSSPS
-
-
?
additional information
?
-
-
Candida glabrata does not degrade E-cadherin
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(1R,5R,7R)-3-benzyl-7-(piperidin-1-ylcarbonyl)-6,8-dioxa-3-azabicyclo[3.2.1]octan-2-one
-
74% inhibition at 0.02 mM
(1R,5R,7R)-3-benzyl-N-(2-hydroxyethyl)-2-oxo-6,8-dioxa-3-azabicyclo[3.2.1]octane-7-carboxamide
-
71% inhibition at 0.02 mM
(1R,5R,7R)-3-benzyl-N-(3-hydroxypropyl)-2-oxo-6,8-dioxa-3-azabicyclo[3.2.1]octane-7-carboxamide
-
23% inhibition at 0.02 mM
(1R,5R,7R)-3-benzyl-N-[(1R)-2-hydroxy-1-phenylethyl]-2-oxo-6,8-dioxa-3-azabicyclo[3.2.1]octane-7-carboxamide
-
31% inhibition at 0.02 mM
(1R,5R,7R)-3-benzyl-N-[(2R)-1-hydroxy-3-phenylpropan-2-yl]-2-oxo-6,8-dioxa-3-azabicyclo[3.2.1]octane-7-carboxamide
-
29% inhibition at 0.02 mM
(1R,5R,7R)-3-benzyl-N-[(2S)-1-hydroxy-3-phenylpropan-2-yl]-2-oxo-6,8-dioxa-3-azabicyclo[3.2.1]octane-7-carboxamide
-
30% inhibition at 0.02 mM
(1R,5R,7R)-3-benzyl-N-[(2S)-1-hydroxy-4-methylpentan-2-yl]-2-oxo-6,8-dioxa-3-azabicyclo[3.2.1]octane-7-carboxamide
-
71% inhibition at 0.02 mM
(1R,5R,7R)-3-benzyl-N-[(2S)-1-hydroxypropan-2-yl]-2-oxo-6,8-dioxa-3-azabicyclo[3.2.1]octane-7-carboxamide
-
35% inhibition at 0.02 mM
(1R,5R,7R)-N-(2-aminoethyl)-3-benzyl-2-oxo-6,8-dioxa-3-azabicyclo[3.2.1]octane-7-carboxamide
-
63% inhibition at 0.02 mM
(1R,5S,7R)-3-benzyl-7-(1,4-diazepan-1-ylcarbonyl)-6,8-dioxa-3-azabicyclo[3.2.1]octan-2-one
-
63% inhibition at 0.02 mM
(1R,5S,7R)-3-benzyl-7-(morpholin-4-ylcarbonyl)-6,8-dioxa-3-azabicyclo[3.2.1]octan-2-one
-
62% inhibition at 0.02 mM
(1R,5S,7R)-3-benzyl-7-(thiomorpholin-4-ylcarbonyl)-6,8-dioxa-3-azabicyclo[3.2.1]octan-2-one
-
58% inhibition at 0.02 mM
(1R,5S,7R)-3-benzyl-7-[[(2R)-2-(hydroxymethyl)pyrrolidin-1-yl]carbonyl]-6,8-dioxa-3-azabicyclo[3.2.1]octan-2-one
-
34% inhibition at 0.02 mM
(1R,5S,7R)-3-benzyl-7-[[(2S)-2-(hydroxymethyl)pyrrolidin-1-yl]carbonyl]-6,8-dioxa-3-azabicyclo[3.2.1]octan-2-one
-
48% inhibition at 0.02 mM
(1R,5S,7R)-3-benzyl-7-[[4-(2-hydroxyethyl)piperazin-1-yl]carbonyl]-6,8-dioxa-3-azabicyclo[3.2.1]octan-2-one
-
58% inhibition at 0.02 mM
(1R,5S,7S)-3-benzyl-2-oxo-6,8-dioxa-3-azabicyclo[3.2.1]octane-7-carboxylic acid [1-hydroxymethyl-3(R)-methylbutyl]amide
-
60% inhibition at 0.02 mM
(1R,5S,7S)-3-benzyl-2-oxo-6,8-dioxa-3-azabicyclo[3.2.1]octane-7-carboxylic acid [1-hydroxymethyl-3(S)-methylbutyl]amide
-
33% inhibition at 0.02 mM
(1S,5R,7R)-3-benzyl-2-oxo-6,8-dioxa-3-azabicyclo[3.2.1]octane-7-carboxylic acid benzyl-(1-hydroxymethyl-3-methylbutyl)amide
-
35% inhibition at 0.02 mM
(1S,5R,7R)-3-benzyl-2-oxo-6,8-dioxa-3-azabicyclo[3.2.1]octane-7-carboxylic acid [1-hydroxymethyl-3(R)-methylbutyl]amide
-
29% inhibition at 0.02 mM
(1S,5S,7S)-3-benzyl-7-(piperidine-1-carbonyl)-6,8-dioxa-3-azabicyclo[3.2.1]octan-2-one
-
50% inhibition at 0.02 mM
1,2-epoxy-3-(4-nitrophenoxy)propane
acetyl-Phe-Ile-Phe-psi[OH-OH]-Phe-Glu-Phe-acetyl
-
transition-state peptidomimetic TS-41
acetyl-Trp-Phe-psi[OH-OH]-Phe-Trp-acetyl
-
transition-state peptidomimetic TS-49
acetyl-Trp-Ser-Phe-psi[OH-OH]-Phe-kynurenic acid
-
transition-state peptidomimetic TS-57
acetyl-Trp-Val-Phe-psi[OH-OH]-Phe-Glu-Phe-acetyl
-
transition-state peptidomimetic TS-43
acetyl-Trp-Val-Phe-psi[OH-OH]-Phe-Val-acetyl
-
transition-state peptidomimetic TS-75
acetyl-Trp-Val-Phe-psi[OH-OH]-Phe-Val-Trp-acetyl
-
transition-state peptidomimetic TS-42
amprenavir
-
most effective inhibitor of Sap2, about 92% inhibition at 0.1 mM
Arg-Ile-Phe-psi[CH2-NH]-Phe-Gln-Arg
-
transition-state peptidomimetic TS-2
benzyloxycarbonyl-L-Val-((3S,4S)-4-amino-3-hydroxy-5-phenylpentanoic acid)-L-Ala-((3S,4S)-4-amino-3-hydroxy-5-phenylpentanoic acid)-OMe
-
benzyloxycarbonyl-L-Val-L-Val-((3R,4R)-4-amino-3-hydroxy-5-phenylpentanoic acid)-L-Ala-((3S,4S)-4-amino-3-hydroxy-5-phenylpentanoic acid)-OMe
-
benzyloxycarbonyl-L-Val-L-Val-((3S,4S)-4-amino-3-hydroxy-5-phenylpentanoic acid)-L-Ala-( (3S,4S)-4-amino-3-hydroxy-5-phenylpentanoic acid)-OMe
-
benzyloxycarbonyl-L-Val-L-Val-((3S,4S)-4-amino-3-hydroxy-5-phenylpentanoic acid)-L-Ala-((3R,4R)-4-amino-3-hydroxy-5-phenylpentanoic acid)-OMe
-
benzyloxycarbonyl-L-Val-L-Val-((3S,4S)-4-amino-3-hydroxy-5-phenylpentanoic acid)-L-Ala-((3S,4S)-4-amino-3-hydroxy-5-phenylpentanoic acid)-NH2
-
benzyloxycarbonyl-L-Val-L-Val-((3S,4S)-4-amino-3-hydroxy-5-phenylpentanoic acid)-L-Ala-((3S,4S)-4-amino-3-hydroxy-5-phenylpentanoic acid)-OH
-
benzyloxycarbonyl-L-Val-L-Val-((3S,4S)-4-amino-3-hydroxy-5-phenylpentanoic acid)-L-Ala-OMe
-
benzyloxycarbonyl-L-Val-L-Val-statine-L-Ala-statine-OH
-
Diazoacetylnorleucine methyl ester
ethyl 4-[[(1R,5S,7R)-3-benzyl-2-oxo-6,8-dioxa-3-azabicyclo[3.2.1]oct-7-yl]carbonyl]piperazine-1-carboxylate
-
74% inhibition at 0.02 mM
isovaleryl-Val-Val-statyl-Ala-statyl-OH
-
-
kynurenic acid-Dtg-Phe-psi(S,R,S)[OH]-Phe-dimethylphenoxyacetic acid
-
transition-state peptidomimetic TS-92
kynurenic acid-Dtg-Phe-psi[OH-OH]-Phe-phenoxyacetic acid
-
transition-state peptidomimetic TS-63
kynurenic acid-Thr-Phe-psi(S,R,S)[OH]-Phe-dimethylphenoxyacetic acid
-
transition-state peptidomimetic TS-93
kynurenic acid-Thr-Phe-psi[OH-OH]-Phe-kynurenic acid
-
transition-state peptidomimetic TS-59
kynurenic acid-Val-Phe-psi(S,R,S)[OH]-Phe-dimethylphenoxyacetic acid
-
transition-state peptidomimetic TS-94
kynurenic acid-Val-Phe-psi(S,R,S)[OH]-Phe-Val-kynurenic acid
-
transition-state peptidomimetic TS-91
kynurenic acid-Val-Phe-psi[OH-OH]-Phe-Val-kynurenic acid
-
best inhibitor; transition-state peptidomimetic TS-70
Lys-Ile-Phe-psi[CH2-NH]-Phe-Gln-Arg
-
transition-state peptidomimetic TS-23
mycogenic silver nanoparticles
-
phenylmethylsulfonyl fluoride
-
SDS
-
tolerated at 0.01% w/v, decrease of activity at 0.1% w/v, 1% completely destroys activity within a few min
t-butoxylcarbonyl-Phe-psi[OH-OH]-Phe-Dtg-phenoxyacetic acid
-
transition-state peptidomimetic TS-54
t-butoxylcarbonyl-Phe-psi[OH-OH]-Phe-Glu-Phe-acetyl
-
transition-state peptidomimetic TS-53
tert-butoxycarbonyl-Val-Val-(3R,4R)-4-amino-3-hydroxy-5-phenylpentanoyl-Ala-phenylstatyl-O-methyl ester
-
-
tert-butoxycarbonyl-Val-Val-phenylstatyl-Ala-(3R,4R)-4-amino-3-hydroxy-5-phenylpentanoyl-OH
-
-
tert-butoxycarbonyl-Val-Val-phenylstatyl-Ala-O-methyl ester
-
-
tert-butoxycarbonyl-Val-Val-phenylstatyl-Ala-phenylstatyl-NH2
-
-
tert-butoxycarbonyl-Val-Val-phenylstatyl-Ala-phenylstatyl-O-methyl ester
-
-
tert-butoxycarbonyl-Val-Val-phenylstatyl-Ala-phenylstatyl-OH
-
-
Trp-Ile-Phe-psi[CH2-NH]-Phe-Gln-Trp
-
transition-state peptidomimetic TS-10
Xan-Dtg-Val-psi(S,R,S)[OH]-Val-Dtg-Xan
-
transition-state peptidomimetic TS-90
(2R,3S)-phenylnorstatine
the 2R hydroxyl compound is 100- to 1000fold more potent than the 2S hydroxyl derivative
(2R,3S)-phenylnorstatine
the 2R hydroxyl compound is 100- to 1000fold more potent than the 2S hydroxyl derivative
(2R,3S)-phenylnorstatine
the 2R hydroxyl compound is 100- to 1000fold more potent than the 2S hydroxyl derivative
(2S,3S)-phenylnorstatine
the 2R hydroxyl compound is 100- to 1000fold more potent than the 2S hydroxyl derivative
(2S,3S)-phenylnorstatine
the 2R hydroxyl compound is 100- to 1000fold more potent than the 2S hydroxyl derivative
(2S,3S)-phenylnorstatine
the 2R hydroxyl compound is 100- to 1000fold more potent than the 2S hydroxyl derivative
(3S,4S)-phenylstatine
-
(3S,4S)-statine
-
1,2-epoxy-3-(4-nitrophenoxy)propane
-
not
1,2-epoxy-3-(4-nitrophenoxy)propane
Candida olea
-
not
1,2-epoxy-3-(4-nitrophenoxy)propane
-
-
Diazoacetylnorleucine methyl ester
-
not
Diazoacetylnorleucine methyl ester
Candida olea
-
-
Diazoacetylnorleucine methyl ester
-
not
mycogenic silver nanoparticles
-
after 24 h of incubation, significant reduction (87%) in metabolic activity is observed with 100 ppm mycogenic silver nanoparticles
-
mycogenic silver nanoparticles
-
after 24 h of incubation, significant reduction (74%) in metabolic activity is observed with 100ppm mycogenic silver nanoparticles
-
mycogenic silver nanoparticles
-
after 24 h of incubation, significant reduction (56%) in metabolic activity is observed with 100ppm mycogenic silver nanoparticles
-
mycogenic silver nanoparticles
-
after 24 h of incubation, significant reduction (80%) in metabolic activity is observed with 100ppm mycogenic silver nanoparticles
-
mycogenic silver nanoparticles
-
after 24 h of incubation, significant reduction (83%) in metabolic activity is observed with 100 ppm mycogenic silver nanoparticles
-
pepstatin
-
-
pepstatin
Candida olea
-
-
pepstatin A
IC50 for sap2p: 27 nM; IC50 for sap2p: 27 nM
pepstatin A
isozymes 1-10 except 7
pepstatin A
strong inhibitor; strong inhibitor
pepstatin A
-
potent inhibitor
ritonavir
-
saquinavir
-
additional information
-
methyl 2-diazoacetamidohexanoate
-
additional information
-
heavy metal ions; p-bromophenacyl bromide; SH-blocking reagents
-
additional information
-
not: soybean trypsin inhibitor; phenylmethylsulfonyl fluoride; tosyl-L-Phe chloromethyl ketone
-
additional information
cis-configured epoxides and aziridines containing hydrophobic moieties and amino acid esters as new potential inhibitors
-
additional information
-
cis-configured epoxides and aziridines containing hydrophobic moieties and amino acid esters as new potential inhibitors
-
additional information
-
isozyme Sap7 is not inhibited by pepstatin A, leupeptin, phenylmethylsulfonyl fluoride and EDTA
-
additional information
isozyme Sap7 is not inhibited by pepstatin A, leupeptin, phenylmethylsulfonyl fluoride and EDTA
-
additional information
isozyme Sap7 is not inhibited by pepstatin A, leupeptin, phenylmethylsulfonyl fluoride and EDTA
-
additional information
isozyme Sap7 is not inhibited by pepstatin A, leupeptin, phenylmethylsulfonyl fluoride and EDTA
-
additional information
isozyme Sap7 is not inhibited by pepstatin A, leupeptin, phenylmethylsulfonyl fluoride and EDTA
-
additional information
Candida olea
-
compounds inhibiting serine, thiol or metallo proteases
-
additional information
not inhibited by indinavir and nelfinavir; not inhibited by indinavir and nelfinavir
-
additional information
not inhibited by indinavir and nelfinavir; not inhibited by indinavir and nelfinavir
-
additional information
-
not inhibited by indinavir and nelfinavir; not inhibited by indinavir and nelfinavir
-
additional information
-
2-mercaptoethanol; diisopropyl fluorophosphate; DTT; EDTA; iodoacetamide
-
additional information
EDTA does not affect the proteolytic activity of the enzyme
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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0.0000143 - 0.000044
benzyloxycarbonyl-L-Val-((3S,4S)-4-amino-3-hydroxy-5-phenylpentanoic acid)-L-Ala-((3S,4S)-4-amino-3-hydroxy-5-phenylpentanoic acid)-OMe
0.000174 - 0.002782
benzyloxycarbonyl-L-Val-L-Val-((3R,4R)-4-amino-3-hydroxy-5-phenylpentanoic acid)-L-Ala-((3S,4S)-4-amino-3-hydroxy-5-phenylpentanoic acid)-OMe
0.0000002 - 0.0000003
benzyloxycarbonyl-L-Val-L-Val-((3S,4S)-4-amino-3-hydroxy-5-phenylpentanoic acid)-L-Ala-( (3S,4S)-4-amino-3-hydroxy-5-phenylpentanoic acid)-OMe
0.0000001 - 0.0000004
benzyloxycarbonyl-L-Val-L-Val-((3S,4S)-4-amino-3-hydroxy-5-phenylpentanoic acid)-L-Ala-((3R,4R)-4-amino-3-hydroxy-5-phenylpentanoic acid)-OMe
0.0000001
benzyloxycarbonyl-L-Val-L-Val-((3S,4S)-4-amino-3-hydroxy-5-phenylpentanoic acid)-L-Ala-((3S,4S)-4-amino-3-hydroxy-5-phenylpentanoic acid)-NH2
0.0000018 - 0.0000066
benzyloxycarbonyl-L-Val-L-Val-((3S,4S)-4-amino-3-hydroxy-5-phenylpentanoic acid)-L-Ala-((3S,4S)-4-amino-3-hydroxy-5-phenylpentanoic acid)-OH
0.0000072 - 0.0000146
benzyloxycarbonyl-L-Val-L-Val-((3S,4S)-4-amino-3-hydroxy-5-phenylpentanoic acid)-L-Ala-OMe
0.00000003 - 0.0000003
benzyloxycarbonyl-L-Val-L-Val-statine-L-Ala-statine-OH
0.0000003
isovaleryl-Val-Val-statyl-Ala-statyl-OH
-
-
0.0000003 - 0.017
pepstatin A
0.0003 - 0.0019
ritonavir
0.005301
tert-butoxycarbonyl-Val-Val-(3R,4R)-4-amino-3-hydroxy-5-phenylpentanoyl-Ala-phenylstatyl-O-methyl ester
-
-
0.0000009
tert-butoxycarbonyl-Val-Val-phenylstatyl-Ala-(3R,4R)-4-amino-3-hydroxy-5-phenylpentanoyl-OH
-
-
0.0000065
tert-butoxycarbonyl-Val-Val-phenylstatyl-Ala-O-methyl ester
-
-
0.00000254
tert-butoxycarbonyl-Val-Val-phenylstatyl-Ala-phenylstatyl-NH2
-
-
0.0000004
tert-butoxycarbonyl-Val-Val-phenylstatyl-Ala-phenylstatyl-O-methyl ester
-
-
0.0000066
tert-butoxycarbonyl-Val-Val-phenylstatyl-Ala-phenylstatyl-OH
-
-
additional information
additional information
-
0.0000143
benzyloxycarbonyl-L-Val-((3S,4S)-4-amino-3-hydroxy-5-phenylpentanoic acid)-L-Ala-((3S,4S)-4-amino-3-hydroxy-5-phenylpentanoic acid)-OMe
isoform Sapp2p, in 150 mM sodium citrate buffer, pH 3.75, at 37°C
0.000044
benzyloxycarbonyl-L-Val-((3S,4S)-4-amino-3-hydroxy-5-phenylpentanoic acid)-L-Ala-((3S,4S)-4-amino-3-hydroxy-5-phenylpentanoic acid)-OMe
isoform Sapp1p, in 150 mM sodium citrate buffer, pH 3.75, at 37°C
0.000174
benzyloxycarbonyl-L-Val-L-Val-((3R,4R)-4-amino-3-hydroxy-5-phenylpentanoic acid)-L-Ala-((3S,4S)-4-amino-3-hydroxy-5-phenylpentanoic acid)-OMe
isoform Sapp1p, in 150 mM sodium citrate buffer, pH 3.75, at 37°C
0.002782
benzyloxycarbonyl-L-Val-L-Val-((3R,4R)-4-amino-3-hydroxy-5-phenylpentanoic acid)-L-Ala-((3S,4S)-4-amino-3-hydroxy-5-phenylpentanoic acid)-OMe
isoform Sapp2p, in 150 mM sodium citrate buffer, pH 3.75, at 37°C
0.0000002
benzyloxycarbonyl-L-Val-L-Val-((3S,4S)-4-amino-3-hydroxy-5-phenylpentanoic acid)-L-Ala-( (3S,4S)-4-amino-3-hydroxy-5-phenylpentanoic acid)-OMe
isoform Sapp2p, in 150 mM sodium citrate buffer, pH 3.75, at 37°C
0.0000003
benzyloxycarbonyl-L-Val-L-Val-((3S,4S)-4-amino-3-hydroxy-5-phenylpentanoic acid)-L-Ala-( (3S,4S)-4-amino-3-hydroxy-5-phenylpentanoic acid)-OMe
isoform Sapp1p, in 150 mM sodium citrate buffer, pH 3.75, at 37°C
0.0000001
benzyloxycarbonyl-L-Val-L-Val-((3S,4S)-4-amino-3-hydroxy-5-phenylpentanoic acid)-L-Ala-((3R,4R)-4-amino-3-hydroxy-5-phenylpentanoic acid)-OMe
isoform Sapp2p, in 150 mM sodium citrate buffer, pH 3.75, at 37°C
0.0000004
benzyloxycarbonyl-L-Val-L-Val-((3S,4S)-4-amino-3-hydroxy-5-phenylpentanoic acid)-L-Ala-((3R,4R)-4-amino-3-hydroxy-5-phenylpentanoic acid)-OMe
isoform Sapp1p, in 150 mM sodium citrate buffer, pH 3.75, at 37°C
0.0000001
benzyloxycarbonyl-L-Val-L-Val-((3S,4S)-4-amino-3-hydroxy-5-phenylpentanoic acid)-L-Ala-((3S,4S)-4-amino-3-hydroxy-5-phenylpentanoic acid)-NH2
isoform Sapp1p, in 150 mM sodium citrate buffer, pH 3.75, at 37°C
0.0000001
benzyloxycarbonyl-L-Val-L-Val-((3S,4S)-4-amino-3-hydroxy-5-phenylpentanoic acid)-L-Ala-((3S,4S)-4-amino-3-hydroxy-5-phenylpentanoic acid)-NH2
isoform Sapp2p, in 150 mM sodium citrate buffer, pH 3.75, at 37°C
0.0000018
benzyloxycarbonyl-L-Val-L-Val-((3S,4S)-4-amino-3-hydroxy-5-phenylpentanoic acid)-L-Ala-((3S,4S)-4-amino-3-hydroxy-5-phenylpentanoic acid)-OH
isoform Sapp2p, in 150 mM sodium citrate buffer, pH 3.75, at 37°C
0.0000066
benzyloxycarbonyl-L-Val-L-Val-((3S,4S)-4-amino-3-hydroxy-5-phenylpentanoic acid)-L-Ala-((3S,4S)-4-amino-3-hydroxy-5-phenylpentanoic acid)-OH
isoform Sapp1p, in 150 mM sodium citrate buffer, pH 3.75, at 37°C
0.0000072
benzyloxycarbonyl-L-Val-L-Val-((3S,4S)-4-amino-3-hydroxy-5-phenylpentanoic acid)-L-Ala-OMe
isoform Sapp2p, in 150 mM sodium citrate buffer, pH 3.75, at 37°C
0.0000146
benzyloxycarbonyl-L-Val-L-Val-((3S,4S)-4-amino-3-hydroxy-5-phenylpentanoic acid)-L-Ala-OMe
isoform Sapp1p, in 150 mM sodium citrate buffer, pH 3.75, at 37°C
0.00000003
benzyloxycarbonyl-L-Val-L-Val-statine-L-Ala-statine-OH
isoform Sapp2p, in 150 mM sodium citrate buffer, pH 3.75, at 37°C
0.0000003
benzyloxycarbonyl-L-Val-L-Val-statine-L-Ala-statine-OH
isoform Sapp1p, in 150 mM sodium citrate buffer, pH 3.75, at 37°C
0.0000003
pepstatin A
isoform Sapp1p, in 150 mM sodium citrate buffer, pH 3.75, at 37°C
0.0000004
pepstatin A
isoform Sapp2p, in 150 mM sodium citrate buffer, pH 3.75, at 37°C
0.0003
ritonavir
-
0.0003
ritonavir
isoform Sapp2p, in 150 mM sodium citrate buffer, pH 3.75, at 37°C
0.0019
ritonavir
isoform Sapp1p, in 150 mM sodium citrate buffer, pH 3.75, at 37°C
0.0169
saquinavir
isoform Sapp1p, in 150 mM sodium citrate buffer, pH 3.75, at 37°C
0.32
saquinavir
isoform Sapp2p, in 150 mM sodium citrate buffer, pH 3.75, at 37°C
additional information
additional information
second order inhibition rate constants between 56.000 and 121.000M(-1)min(-1) for cis-configured epoxides and aziridines
-
additional information
additional information
-
second order inhibition rate constants between 56.000 and 121.000M(-1)min(-1) for cis-configured epoxides and aziridines
-
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Candida parapsilosis (P32950), Candida parapsilosis, Candida parapsilosis CP386/IDE98 (P32950)
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The role of secreted aspartyl proteinases in Candida albicans keratitis
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The yeast Candida albicans evades human complement attack by secretion of aspartic proteases
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Candida albicans
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Candida albicans
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Mycopathologia
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Candida albicans, Candida parapsilosis
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Silva, S.; Hooper, S.J.; Henriques, M.; Oliveira, R.; Azeredo, J.; Williams, D.W.
The role of secreted aspartyl proteinases in Candida tropicalis invasion and damage of oral mucosa
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Candida tropicalis
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Sandini, S.; La Valle, R.; Deaglio, S.; Malavasi, F.; Cassone, A.; De Bernardis, F.
A highly immunogenic recombinant and truncated protein of the secreted aspartic proteases family (rSap2t) of Candida albicans as a mucosal anticandidal vaccine
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Candida albicans, Candida albicans ATCC 20955
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Correia, A.; Lermann, U.; Teixeira, L.; Cerca, F.; Botelho, S.; da Costa, R.M.; Sampaio, P.; Gaertner, F.; Morschhaeuser, J.; Vilanova, M.; Pais, C.
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Candida albicans
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Aoki, W.; Kitahara, N.; Miura, N.; Morisaka, H.; Yamamoto, Y.; Kuroda, K.; Ueda, M.
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Candida albicans, Candida albicans (P0CY27), Candida albicans (P0CY29), Candida albicans (P0DJ06), Candida albicans (P43094)
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Atomic resolution crystal structure of Sapp2p, a secreted aspartic protease from Candida parapsilosis
Acta Crystallogr. Sect. D
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Candida parapsilosis (G8B6Y8), Candida parapsilosis, Candida parapsilosis CDC-317 (G8B6Y8)
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Hamid, S.; Zainab, S.; Faryal, R.; Ali, N.; Sharafat, I.
Inhibition of secreted aspartyl proteinase activity in biofilms of Candida species by mycogenic silver nanoparticles
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Candida albicans, Pichia kudriavzevii, [Candida] glabrata, Candida parapsilosis, Candida tropicalis
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Paernaenen, P.; Meurman, J.; Nikula-Ijaes, P.
A novel Candida glabrata cell wall associated serine protease
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[Candida] glabrata (Q6FTZ7), [Candida] glabrata T-1639 (Q6FTZ7)
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Ibrisimovic, M.; Ibrisimovic-Mehmedinovic, N.; Dedic, J.; Kesic, A.; Maric, S.; Sestan, A.
Effects of various metal and drug agents on excretion of enzyme aspartyl proteinase in Candida albicans and its role in human physiological processes
CMBEBIH 2017. IFMBE Proceedings (Badnjevic A. ed.)
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Candida albicans
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Svoboda, E.; Schneider, A.E.; Sandor, N.; Lermann, U.; Staib, P.; Kremlitzka, M.; Bajtay, Z.; Barz, D.; Erdei, A.; Jozsi, M.
Secreted aspartic protease 2 of Candida albicans inactivates factor H and the macrophage factor H-receptors CR3 (CD11b/CD18) and CR4 (CD11c/CD18)
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Candida albicans
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Novel aggregation properties of Candida albicans secreted aspartyl proteinase SAP6 mediate virulence in oral candidiasis
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Candida albicans (Q5AC08), Candida albicans, Candida albicans CAI4 (Q5AC08)
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Willems, H.M.E.; Bruner, W.S.; Barker, K.S.; Liu, J.; Palmer, G.E.; Peters, B.M.
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Infect. Immun.
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Candida albicans
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Biswal, R.; Venkataraghavan, R.; Pazhamalai, V.; Romauld, S.
Molecular docking of various bioactive compounds from essential oil of Trachyaspermum ammi against the fungal enzyme candidapepsin-1
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2019
Candida albicans (P0CY27), Candida albicans SG5314 (P0CY27)
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Rasheed, M.; Battu, A.; Kaur, R.
Aspartyl proteases in Candida glabrata are required for suppression of the host innate immune response
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[Candida] glabrata, [Candida] glabrata BG2
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Khodavandi, A.; Alizadeh, F.; Abdolahi, M.; Jahangiri, M.
Differential expression levels of agglutinin-like sequence, lipase, and secreted aspartyl protease genes in Candida tropicalis treated with fluconazole alone and in combination with clotrimazole
J. Rep. Pharma. Sci.
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2019
Candida tropicalis, Candida tropicalis ATCC 750
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Singh, D.; Nemeth, T.; Papp, A.; Toth, R.; Lukacsi, S.; Heidingsfeld, O.; Dostal, J.; Vagvoelgyi, C.; Bajtay, Z.; Jozsi, M.; Gacser, A.
Functional characterization of secreted aspartyl proteases in Candida parapsilosis
mSphere
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Candida parapsilosis (P32951), Candida parapsilosis
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Dutton, L.C.; Jenkinson, H.F.; Lamont, R.J.; Nobbs, A.H.
Role of Candida albicans secreted aspartyl protease Sap9 in interkingdom biofilm formation
Pathog. Dis.
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Candida albicans
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Gogol, M.; Bochenska, O.; Zawrotniak, M.; Karkowska-Kuleta, J.; Zajac, D.; Rapala-Kozik, M.
Roles of Candida albicans aspartic proteases in host-pathogen interactions
Pathophysiological Aspects of Proteases (ed. Chakraborti S. and Dhalla N.)
1
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2017
Candida albicans
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Gabrielli, E.; Sabbatini, S.; Roselletti, E.; Kasper, L.; Perito, S.; Hube, B.; Cassone, A.; Vecchiarelli, A.; Pericolini, E.
In vivo induction of neutrophil chemotaxis by secretory aspartyl proteinases of Candida albicans
Virulence
7
819-825
2016
Candida albicans (P0DJ06), Candida albicans (Q5AC08)
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