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Information on EC 3.4.23.24 - Candidapepsin and Organism(s) Candida albicans and UniProt Accession P43095
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3.4.23.24 CandidapepsinSpecify your search results
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- 3.4.23.24
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amyloid
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endoproteolysis
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plasmepsin
- beta-protein
- phytoplasmas
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secretase
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intramembrane-cleaving
- indinavir
- endothiapepsin
- medicine
- saquinavir
- prorenin
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hydroxyethylamine
-
vulvovaginal
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isostere
The taxonomic range for the selected organisms is: Candida albicans
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
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
Synonyms
aspartyl protease, secreted aspartyl proteinase, sap11, secreted aspartyl proteinases, sapp1p, sap10, yapsin, secreted aspartic proteinase, secreted aspartic protease, secreted aspartyl protease, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Aspartate protease
-
-
-
-
aspartyl proteinase
Candida albicans aspartic proteinase
-
-
-
-
Candida albicans carboxyl proteinase
-
-
-
-
Candida albicans secretory acid proteinase
-
-
-
-
Candida olea acid proteinase
-
-
-
-
Proteinase, Candida albicans aspartic
-
-
-
-
Proteinase, Candida aspartic
-
-
-
-
Proteinase, Candida olea aspartic
-
-
-
-
SAP
SAP1
SAP2
SAP3
SAP4
SAP5
SAP6
Sap7
Sap9
secreted aspartic protease
secreted aspartyl protease
secreted aspartyl proteinase
secretory aspartyl proteinase
CAS REGISTRY NUMBER
COMMENTARY
69458-91-9
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
?
-
-
-
?
Arg-Glu-[5-(aminoethyl)aminonaphthalene sulfonate]-Ile-His-Pro-Phe-His-Leu-Val-Ile-His-Thr-Lys-[4'-dimethylaminoazobenzene-4-carboxylate]-Arg + 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
-
-
?
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
-
-
?
factor H + H2O
?
-
the enzyme cleaves and inactivates factor H, diminishing its complement regulatory activity
-
-
?
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
-
-
?
Lys-Pro-Ala-Arg-Phe-Nph-Arg-Leu + H2O
Lys-Pro-Ala-Arg-Phe + Nph-Arg-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
-
-
?
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
-
-
?
Albumin + H2O
?
-
low side-chain specificity, preferential attack on hydrophobic amino acid residues
-
-
?
Albumin + H2O
?
cleavage by Sap2p shows a low side-chain specificity
-
-
?
Bovine serum albumin + H2O
?
-
-
-
-
?
casein + H2O
?
isozyme Sap6 shows highest activity towards casein
-
-
?
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
?
-
-
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
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
factor H + H2O
?
-
the enzyme cleaves and inactivates factor H, diminishing its complement regulatory activity
-
-
?
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
-
-
?
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
?
-
-
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
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(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
(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
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
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
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
mycogenic silver nanoparticles
-
after 24 h of incubation, significant reduction (87%) in metabolic activity is observed with 100 ppm mycogenic silver nanoparticles
-
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
Xan-Dtg-Val-psi(S,R,S)[OH]-Val-Dtg-Xan
-
transition-state peptidomimetic TS-90
kynurenic acid-Val-Phe-psi[OH-OH]-Phe-Val-kynurenic acid
-
transition-state peptidomimetic TS-70
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
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
fluconazole
enhances expression of SAP4-GFP and SAP6-GFP and reduces growth of Candida albicans to 60% to 80% at 0.5 mg/l, respectively
nonionic detergents
-
Triton X-100, Tween-80, Nonidet P-40, slight improvement of activity
-
fluconazole
enhances expression of SAP4-GFP and SAP6-GFP and reduces growth of Candida albicans to 60% to 80% at 0.5 mg/l
fluconazole
enhances expression of SAP4-GFP and SAP6-GFP and reduces growth of Candida albicans to 60% to 80% at 0.5 mg/l, respectively
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4.3
4-(4-dimethylaminophenylazo)benzoyl-gamma-aminobutyryl-Ile-HIs-Pro-Phe-His-Leu-Val-Ile-His-Thr-[5-(2-aminoethyl)-amino]naphthalene-1-sulfonic acid
isoenzyme Sap2p
0.008
Lys-Pro-Ala-Arg-Phe-Nph-Arg-Leu
pH 3.25, isoenzyme Sap2p
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.02
(1S,5S,7S)-3-benzyl-7-(piperidine-1-carbonyl)-6,8-dioxa-3-azabicyclo[3.2.1]octan-2-one
Candida albicans
-
in 50 mM sodium citrate, pH 3.2, at 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
the specific activity ratio biofilm:planktonic is 3.1:1
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5
isoenzyme Sap2p, hydrolysis of 4-(4-dimethylaminophenylazo)benzoyl-gamma-aminobutyryl-Ile-HIs-Pro-Phe-His-Leu-Val-Ile-His-Thr-[5-(2-aminoethyl)-amino]naphthalene-1-sulfonic acid
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
biofilms of Candida albicans secrete more SAPs than the planktonic form
-
-
biofilms of Candida albicans secrete more SAPs than the planktonic form
the expression of SAP6 and the production of fungal hyphae are correlated
-
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
apical compartment of filamentous cell
additional information
apical compartment of filamentous cell
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
Sap1 to Sap6 do not play a significant role in Candida albicans virulence in a murine model of hematogenously disseminated candidiasis. In this model, Sap1 to Sap3 are not necessary for successful Candida albicans infection. A deficiency in SAP4 to SAP6 has no noticeable impact on the immune response elicited in the spleens and kidneys of Candida albicans-infected mice
physiological function
physiological function
-
isoforms Sap1, Sap2, and Sap3 degrade host complement components C3b, C4b and C5 and suppress host complement response. Saps inhibit C3b opsonization of Candida albicans and generation of the anaphylatoxin C5a in human plasma
physiological function
isoform Sap2 induces neutrophil migration and production of potent chemoattractive chemokines such as interleukin-8 and macrophage inflammatory protein-2 by vaginal epithelial cells
physiological function
isoform Sap6 induces neutrophil migration and production of potent chemoattractive chemokines such as interleukin-8 and macrophage inflammatory protein-2 by vaginal epithelial cells
physiological function
-
isoform Sap9 is associated with protein-receptor interactions between fungal cells, and with interkingdom communication in the formation of polymicrobial biofilm communities
physiological function
-
overexpression of Candida albicans secreted aspartyl proteinase 2 or 5 is not sufficient for exacerbation of immunopathology in a mouse model of vaginitis
physiological function
secreted aspartyl proteinase Sap6 mediates virulence in oral candidiasis. Mice infected sublingually with Candida albicans cells overexpressing Sap6 have thicker fungal plaques and more severe oral infection
physiological function
-
the enzyme deregulates the host biochemical homeostasis by impairing the major proteolytic cascades such as the blood coagulation, the kallikrein-kinin system, and the complement system, by unleashing the activity of host proteases due to the degradation of specific endogenous inhibitors and by the inactivation of antimicrobial peptides and proteins produced by host cells
physiological function
-
the enzyme is a cruical virulence determinant of Candida albicans and is involved in tissue degradation and dissamination of infection characteristic for oropharyngeal or vaginal candidasis
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). CARP6_CANAX
418
0
45469
Swiss-Prot
Secretory Pathway (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
11000
1 * 44000 + 1 * 11000, isozyme Sap9, SDS-PAGE
15000
1 * 52000 + 1 * 15000, isozyme Sap7, SDS-PAGE
35000
isozyme Sap8, calculated from amino acid sequence
36000
37000
38000
39000
40000
41000
42000
43000
44000
45000
47000
isozyme Sap7, calculated from amino acid sequence
52000
53000
isozyme Sap9, calculated from amino acid sequence
additional information
36000
isozyme Sap1, calculated from amino acid sequence
36000
isozyme Sap2, calculated from amino acid sequence
37000
isozyme Sap3, SDS-PAGE and calculated from amino acid sequence
37000
isozyme Sap4, calculated from amino acid sequence
37000
isozyme Sap5, calculated from amino acid sequence
37000
isozyme Sap6, calculated from amino acid sequence
40000
-
x * 40000, Candida albicans, Sap1, SDS-PAGE, x * 41000, Candida albicans, Sap3, SDS-PAGE, x * 43000, Candida albicans, Sap2, SDS-PAGE
41000
-
x * 40000, Candida albicans, Sap1, SDS-PAGE, x * 41000, Candida albicans, Sap3, SDS-PAGE, x * 43000, Candida albicans, Sap2, SDS-PAGE
43000
-
Candida albicans, the enzyme originates as a 45000 MW precursor protein which is processed to a 43000 protein prior to secretion
43000
-
x * 40000, Candida albicans, Sap1, SDS-PAGE, x * 41000, Candida albicans, Sap3, SDS-PAGE, x * 43000, Candida albicans, Sap2, SDS-PAGE
44000
1 * 44000 + 1 * 11000, isozyme Sap9, SDS-PAGE
45000
isozyme Sap10, calculated from amino acid sequence
52000
1 * 52000 + 1 * 15000, isozyme Sap7, SDS-PAGE
additional information
-
nucleotide sequence of Candida albicans enzyme, PRA10 and PRA11
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heterodimer
monomer
?
-
x * 40000, Candida albicans, Sap1, SDS-PAGE, x * 41000, Candida albicans, Sap3, SDS-PAGE, x * 43000, Candida albicans, Sap2, SDS-PAGE
heterodimer
1 * 44000 + 1 * 11000, isozyme Sap9, SDS-PAGE
heterodimer
1 * 52000 + 1 * 15000, isozyme Sap7, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
glycoprotein
-
number of potential N-linked glycosylation sites, Sap1: 0, Sap2: 2, Sap3: 1
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Sap3 with PepA in the presence of 10 mM zinc acetate, Sap3 without PepA in the presence of 0.2M potassium bromide, 15% PEG4000 and 0.1 M cacodylic acid/NaOH, pH 6.5. The Sap3 protein crystallizes in the trigonal space group P3(2)21 containing one molecule per asymmetric unit.
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
-
10 min, 85% loss of activity at pH 7.5, 5% loss of activity at pH 6.6 and 7.0
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Enzyme gradually loses activity by standing in solution in the cold or in the frozen state
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
DEAE Sephadex A-25 gel filtration and hydroxyapatite column chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
Candida albicans ATCC 10231 and ATCC 10261, contain two genes for a secreted aspartate proteinase, PRA10 and PRA11, cloned and expressed in Escherichia coli TG1 and DH5alpha
-
expressed in Pichia pastoris
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
for good Sap-inducing conditions, cells are incubated in 1.2% (w/v) yeast carbon base medium supplemented with 0.1% (w/v) bovine serum albumin, pH 5.0, at 37°C for 48 h under slight agitation (100 rpm)
-
isoforms SAP5 and SAP6 mRNA are expressed higher in Candida albicans strain SC5314 than strain VE175
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
if the SAP1 gene having a deletion of the propeptide is expressed in Pichia pastoris, the protein accumulates in the cell and fails to be secreted
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
biochemical target for drug development against clinically important fungal infections
medicine
protection against systemic candidiasis in mice immunized with secreted aspartic proteinase 2
medicine
-
recombinant truncated Sap2 is a candidate vaccine to fight vaginal candidiasis
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JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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Properties of a purified proteinase from the yeast Candida albicans
Biochim. Biophys. Acta
659
99-113
1981
Candida albicans, Candida albicans CBS-2730
Remold, H.; Fasold, H.; Staib, F.
Purification and characterization of a proteolytic enzyme from Candida albicans
Biochim. Biophys. Acta
167
399-406
1968
Candida albicans
Lott, T.J.; Page, L.S.; Boiron, P.; Benson, J.; Reiss, E.
Nucleotide sequence of the Candida albicans aspartyl proteinase gene
Nucleic Acids Res.
17
1779
1989
Candida albicans
Wright, R.J.; Carne, A.; Hieber, A.D.; Lamont, I.L.; Emerson, G.W.; Sullivan, P.A.
A second gene for a secreted aspartate proteinase in Candida albicans
J. Bacteriol.
174
7848-7853
1992
Candida albicans
White, T.C.; Miyasaki, S.H.; Agabian, N.
Three distinct secreted aspartyl proteinases in Candida albicans
J. Bacteriol.
175
6126-6133
1993
Candida albicans
Morrison, C.J.; Hurst, S.F.; Bragg, S.L.; Kuykendall, R.J.; Diaz, H.; McLaughlin, D.W.; Reiss, E.
Purification and characterization of the extracellular aspartyl proteinase of Candida albicans: removal of extraneous proteins and cell wall mannoprotein and evidence for lack of glycosylation
J. Gen. Microbiol.
139
1177-1186
1993
Candida albicans
Homma, M.; Chibana, H.; Tanaka, K.
Induction of extracellular proteinase in Candida albicans
J. Gen. Microbiol.
139
1187-1193
1993
Candida albicans
Cutfield, S.; Marshall, C.; Moody, P.; Sullivan, P.; Cutfield, J.
Crystallization of inhibited aspartic proteinase from Candida albicans
J. Mol. Biol.
234
1266-1269
1993
Candida albicans
Portillo, F.; Gancedo, C.
Purification and properties of three intracellular proteinases from Candida albicans
Biochim. Biophys. Acta
881
229-235
1986
Candida albicans
Ruechel, R.; Boening, B.; Jahn, E.
Identification and partial characterization of two proteinases from the cell envelope of Candida albicans blastospores
Zentralbl. Bakteriol. Mikrobiol. Hyg. A
260
523-538
1985
Candida albicans
Negi, M.; Tsuboi, R.; Matsui, T.; Ogawa, H.
Isolation and characterization of proteinase from Candida albicans: substrate specificity
J. Invest. Dermatol.
83
32-36
1984
Candida albicans
Skrbec, D.; Romeo, D.
Inhibition of Candida albicans secreted aspartic protease by a novel series of peptidomimetics, also active on the HIV-1 protease
Biochem. Biophys. Res. Commun.
297
1350-1353
2002
Candida albicans, Candida albicans H12
Pranav Kumar, S.K.; Kulkarni, V.M.
Insights into the selective inhibition of Candida albicans secreted aspartyl protease: a docking analysis study
Bioorg. Med. Chem.
10
1153-1170
2002
Candida albicans (P0CS83), Candida albicans
Kalkanci, A.; Bozdayi, G.; Biri, A.; Kustimur, S.
Distribution of secreted aspartyl proteinases using a polymerase chain reaction assay with SAP specific primers in Candida albicans isolates
Folia Microbiol. (Praha)
50
409-413
2005
Candida albicans (P0CY27), Candida albicans (P0CY29), Candida albicans (P0DJ06), Candida albicans (P43094), Candida albicans (Q5A8N2), Candida albicans (Q5AC08), Candida albicans
Foundling, S.I.
Candidapepsin
Handbook of proteolytic enzymes (Barrett, A. J. , Rawlings, N. D. , Woessner, J. F. , eds. ) Academic Press
1
115-120
2004
Candida albicans (P0CY27), Candida albicans (P0DJ06)
-
Vilanova, M.; Teixeira, L.; Caramalho, I.; Torrado, E.; Marques, A.; Madureira, P.; Ribeiro, A.; Ferreira, P.; Gama, M.; Demengeot, J.
Protection against systemic candidiasis in mice immunized with secreted aspartic proteinase 2
Immunology
111
334-342
2004
Candida albicans (P0DJ06), Candida albicans
Taylor, B.N.; Staib, P.; Binder, A.; Biesemeier, A.; Sehnal, M.; Roellinghoff, M.; Morschhaeuser, J.; Schroeppel, K.
Profile of Candida albicans-secreted aspartic proteinase elicited during vaginal infection
Infect. Immun.
73
1828-1835
2005
Candida albicans
Schaller, M.; Korting, H.C.; Borelli, C.; Hamm, G.; Hube, B.
Candida albicans-secreted aspartic proteinases modify the epithelial cytokine response in an in vitro model of vaginal candidiasis
Infect. Immun.
73
2758-2765
2005
Candida albicans
Tavanti, A.; Pardini, G.; Campa, D.; Davini, P.; Lupetti, A.; Senesi, S.
Differential expression of secretory aspartyl proteinase genes (SAP1-10) in oral Candida albicans isolates with distinct karyotypes
J. Clin. Microbiol.
42
4726-4734
2004
Candida albicans
Staib, P.; Lermann, U.; Blass-Warmuth, J.; Degel, B.; Wuerzner, R.; Monod, M.; Schirmeister, T.; Morschhaeuser, J.
Tetracycline-inducible expression of individual secreted aspartic proteases in Candida albicans allows isoenzyme-specific inhibitor screening
Antimicrob. Agents Chemother.
52
146-156
2008
Candida albicans, Candida albicans (P0CY27), Candida albicans (P0CY29), Candida albicans (P0DJ06), Candida albicans (P43094), Candida albicans (Q59SU1), Candida albicans (Q59VH7), Candida albicans (Q5A8N2), Candida albicans (Q5AEM6)
Majer, F.; Pavlickova, L.; Majer, P.; Hradilek, M.; Dolejsi, E.; Hruskova-Heidingsfeldova, O.; Pichova, I.
Structure-based specificity mapping of secreted aspartic proteases of Candida parapsilosis, Candida albicans, and Candida tropicalis using peptidomimetic inhibitors and homology modeling
Biol. Chem.
387
1247-1254
2006
Candida albicans (P0DJ06), Candida albicans, Candida parapsilosis (P32951), Candida parapsilosis, Candida tropicalis (Q00663), Candida tropicalis
Mendes, A.; Mores, A.U.; Carvalho, A.P.; Rosa, R.T.; Samaranayake, L.P.; Rosa, E.A.
Candida albicans biofilms produce more secreted aspartyl protease than the planktonic cells
Biol. Pharm. Bull.
30
1813-1815
2007
Candida albicans
Degel, B.; Staib, P.; Rohrer, S.; Scheiber, J.; Martina, E.; Buechold, C.; Baumann, K.; Morschhaeuser, J.; Schirmeister, T.
Cis-configured aziridines are new pseudo-irreversible dual-mode inhibitors of Candida albicans secreted aspartic protease 2
ChemMedChem
3
302-315
2008
Candida albicans (P0DJ06), Candida albicans
Jackson, B.E.; Wilhelmus, K.R.; Hube, B.
The role of secreted aspartyl proteinases in Candida albicans keratitis
Invest. Ophthalmol. Vis. Sci.
48
3559-3565
2007
Candida albicans (P43095), Candida albicans
Barelle, C.J.; Duncan, V.M.; Brown, A.J.; Gow, N.A.; Odds, F.C.
Azole antifungals induce up-regulation of SAP4, SAP5 and SAP6 secreted proteinase genes in filamentous Candida albicans cells in vitro and in vivo
J. Antimicrob. Chemother.
61
315-322
2008
Candida albicans (P43094), Candida albicans (P43095), Candida albicans (Q5A8N2)
Borelli, C.; Ruge, E.; Lee, J.H.; Schaller, M.; Vogelsang, A.; Monod, M.; Korting, H.C.; Huber, R.; Maskos, K.
X-ray structures of Sap1 and Sap5: Structural comparison of the secreted aspartic proteinases from Candida albicans
Proteins
272
1308-1319
2008
Candida albicans (P0CY29)
Borelli, C.; Ruge, E.; Lee, J.H.; Schaller, M.; Vogelsang, A.; Monod, M.; Korting, H.C.; Huber, R.; Maskos, K.
X-ray structures of Sap1 and Sap5: Structural comparison of the secreted aspartic proteinases from Candida albicans
Proteins
72
1308-1319
2008
Candida albicans (P0CY27), Candida albicans (P43094)
Low, C.F.; Chong, P.P.; Yong, P.V.; Lim, C.S.; Ahmad, Z.; Othman, F.
Inhibition of hyphae formation and SIR2 expression in Candida albicans treated with fresh Allium sativum (garlic) extract
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105
2169-2177
2008
Candida albicans (Q5A8N2), Candida albicans
Dabas, N.; Morschhaeuser, J.
A transcription factor regulatory cascade controls secreted aspartic protease expression in Candida albicans
Mol. Microbiol.
69
586-602
2008
Candida albicans (P0DJ06), Candida albicans
Lee, S.A.; Jones, J.; Hardison, S.; Kot, J.; Khalique, Z.; Bernardo, S.M.; Lazzell, A.; Monteagudo, C.; Lopez-Ribot, J.
Candida albicans VPS4 is required for secretion of aspartyl proteases and in vivo virulence
Mycopathologia
167
55-63
2009
Candida albicans, Candida albicans (P43093), Candida albicans (P43094), Candida albicans (P43095)
Falkensammer, B.; Pleyer, L.; Ressler, S.; Berg, A.; Borg-von Zepelin, M.; Nagl, M.; Lass-Floerl, C.; Speth, C.; Dierich, M.P.; Wuerzner, R.
Basidiomycete metabolites attenuate virulence properties of Candida albicans in vitro
Mycoses
51
505-514
2008
Candida albicans, Candida albicans CBS 5982
Braga-Silva, L.A.; Mesquita, D.G.; Ribeiro, M.D.; Carvalho, S.M.; Fracalanzza, S.E.; Santos, A.L.
Trailing end-point phenotype antibiotic-sensitive strains of Candida albicans produce different amounts of aspartyl peptidases
Braz. J. Med. Biol. Res.
42
765-770
2009
Candida albicans
Braga-Silva, L.A.; Mogami, S.S.; Valle, R.S.; Silva-Neto, I.D.; Santos, A.L.
Multiple effects of amprenavir against Candida albicans
FEMS Yeast Res.
10
221-224
2010
Candida albicans, Candida albicans 11
Trabocchi, A.; Mannino, C.; Machetti, F.; De Bernardis, F.; Arancia, S.; Cauda, R.; Cassone, A.; Guarna, A.
Identification of inhibitors of drug-resistant Candida albicans strains from a library of bicyclic peptidomimetic compounds
J. Med. Chem.
53
2502-2509
2010
Candida albicans
Paernaenen, P.; Meurman, J.H.; Samaranayake, L.; Virtanen, I.
Human oral keratinocyte E-cadherin degradation by Candida albicans and Candida glabrata
J. Oral Pathol. Med.
39
275-278
2010
Candida albicans, [Candida] glabrata
Parra-Ortega, B.; Cruz-Torres, H.; Villa-Tanaca, L.; Hernandez-Rodriguez, C.
Phylogeny and evolution of the aspartyl protease family from clinically relevant Candida species
Mem. Inst. Oswaldo Cruz
104
505-512
2009
Candida albicans, Pichia kudriavzevii, [Candida] glabrata, Meyerozyma guilliermondii, Kluyveromyces marxianus, Candida parapsilosis, Candida tropicalis, Clavispora lusitaniae, Candida dubliniensis
Gropp, K.; Schild, L.; Schindler, S.; Hube, B.; Zipfel, P.F.; Skerka, C.
The yeast Candida albicans evades human complement attack by secretion of aspartic proteases
Mol. Immunol.
47
465-475
2009
Candida albicans
Hua, X.; Yuan, X.; Mitchell, B.M.; Lorenz, M.C.; ODay, D.M.; Wilhelmus, K.R.
Morphogenic and genetic differences between Candida albicans strains are associated with keratomycosis virulence
Mol. Vis.
15
1476-1484
2009
Candida albicans
Costa, C.R.; Jesuino, R.S.; de Aquino Lemos, J.; de Fatima Lisboa Fernandes, O.; Hasimoto e Souza, L.K.; Passos, X.S.; do Rosario Rodrigues Silva, M.
Effects of antifungal agents in Sap activity of Candida albicans isolates
Mycopathologia
169
91-98
2010
Candida albicans, Candida parapsilosis
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
FEMS Immunol. Med. Microbiol.
62
215-224
2011
Candida albicans, Candida albicans ATCC 20955
Correia, A.; Lermann, U.; Teixeira, L.; Cerca, F.; Botelho, S.; da Costa, R.M.; Sampaio, P.; Gaertner, F.; Morschhaeuser, J.; Vilanova, M.; Pais, C.
Limited role of secreted aspartyl proteinases Sap1 to Sap6 in Candida albicans virulence and host immune response in murine hematogenously disseminated candidiasis
Infect. Immun.
78
4839-4849
2010
Candida albicans
Aoki, W.; Kitahara, N.; Miura, N.; Morisaka, H.; Yamamoto, Y.; Kuroda, K.; Ueda, M.
Comprehensive characterization of secreted aspartic proteases encoded by a virulence gene family in Candida albicans
J. Biochem.
150
431-438
2011
Candida albicans, Candida albicans (P0CY27), Candida albicans (P0CY29), Candida albicans (P0DJ06), Candida albicans (P43094)
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
Artif. Cells Nanomed. Biotechnol.
46
551-557
2018
Candida albicans, Pichia kudriavzevii, [Candida] glabrata, Candida parapsilosis, Candida tropicalis
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.)
62
731-735
2017
Candida albicans
-
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)
Immunol. Lett.
168
13-21
2015
Candida albicans
Kumar, R.; Saraswat, D.; Tati, S.; Edgerton, M.
Novel aggregation properties of Candida albicans secreted aspartyl proteinase SAP6 mediate virulence in oral candidiasis
Infect. Immun.
83
2614-2626
2015
Candida albicans (Q5AC08), Candida albicans, Candida albicans CAI4 (Q5AC08)
Willems, H.M.E.; Bruner, W.S.; Barker, K.S.; Liu, J.; Palmer, G.E.; Peters, B.M.
Overexpression of Candida albicans secreted aspartyl proteinase 2 or 5 is not sufficient for exacerbation of immunopathology in a murine model of vaginitis
Infect. Immun.
85
e00248-17
2017
Candida albicans
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
J. Appl. Pharm. Sci.
9
21-32
2019
Candida albicans (P0CY27), Candida albicans SG5314 (P0CY27)
-
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.
74
ftw005
2016
Candida albicans
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
353-380
2017
Candida albicans
-
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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