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Information on EC 3.4.23.24 - Candidapepsin and Organism(s) Candida parapsilosis and UniProt Accession P32951
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3.4.23.24 CandidapepsinSpecify your search results
Word Map
- 3.4.23.24
- alzheimer
-
amyloid
- cathepsins
- gamma-secretase
-
presenilins
- pepstatin
- abeta
- candidiasis
- beta-secretase
- renin
-
intramembrane
- beta-amyloid
- hyphal
- notch
-
nicastrin
-
beta-site
- parapsilosis
- beta-peptide
- bace-1
- amyloid-beta
- fluconazole
- tropicalis
-
peptidomimetic
- dubliniensis
-
app-cleaving
- broom
- ritonavir
-
endoproteolysis
-
witches
-
plasmepsin
- beta-protein
- phytoplasmas
-
secretase
-
intramembrane-cleaving
- indinavir
- endothiapepsin
- medicine
- saquinavir
- prorenin
-
hydroxyethylamine
-
vulvovaginal
-
isostere
The taxonomic range for the selected organisms is: Candida parapsilosis
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, sap1p, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Sapp1p
Aspartate protease
-
-
-
-
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
-
-
-
-
Sapp2p
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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)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
-
-
?
complement component 3b + H2O
?
substrate for isoforms Sapp1p and Sapp2p
-
-
?
complement component 4b + H2O
?
substrate for isoforms Sapp1p and Sapp2p
-
-
?
factor H-related protein 5 + H2O
?
substrate for isoform Sapp2p
-
-
?
LTEKRDSIS + H2O
LTEKR + L-Asp + Ser-Ile-Ser
100% conversion
-
-
?
PMVELAGE + H2O
PMVEL + AGE
cleavage of Sapp1p, 100% conversion
-
-
?
PMVELQGE + H2O
PMVEL + QGE
cleavage of Sapp1p, 100% conversion
-
-
?
PMVELTGE + H2O
PMVEL + TGE
cleavage of Sapp1p, 100% conversion
-
-
?
PMVELWGE + H2O
PMVEL + WGE
cleavage of Sapp1p, 76% conversion
-
-
?
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-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
-
-
?
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
-
-
-
-
?
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
-
-
-
?
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
-
-
-
-
?
PMVELAGE + H2O
PMVE + L-Leu + AGE
cleavage of Sapp2p, 81% conversion
-
-
?
PMVELQGE + H2O
PMVE + L-Leu + QGE
cleavage of Sapp2p, 18% conversion
-
-
?
PMVELTGE + 2 H2O
PMVE + L-Leu + TGE
cleavage of Sapp2p, 35% conversion
-
-
?
PMVELWGE + H2O
PMVE + L-Leu + WGE
cleavage of Sapp2p, 40% conversion
-
-
?
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
-
-
?
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
complement component 3b + H2O
?
substrate for isoforms Sapp1p and Sapp2p
-
-
?
complement component 4b + H2O
?
substrate for isoforms Sapp1p and Sapp2p
-
-
?
factor H-related protein 5 + H2O
?
substrate for isoform Sapp2p
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(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
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-((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
-
mycogenic silver nanoparticles
-
after 24 h of incubation, significant reduction (74%) in metabolic activity is observed with 100ppm mycogenic silver nanoparticles
-
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-phenylstatyl-O-methyl ester
-
-
additional information
not inhibited by indinavir and nelfinavir
-
additional information
not inhibited by indinavir and nelfinavir
-
additional information
not inhibited by indinavir and nelfinavir
-
additional information
not inhibited by indinavir and nelfinavir
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00113
4-(4-dimethylaminophenylazo)benzyl-Glu-His-Val-Lys-Leu-Val-Glu-5-(2-aminoethylamino)-1-naphthalenesulfonic acid
isoform Sapp1p, in 150 mM sodium citrate buffer, pH 3.75, at 37°C
0.0028
4-(4-dimethylaminophenylazo)benzyl-Glu-His-Val-Lys-Leu-Val-Glu-5-(2-aminoethylamino)-1-naphthalenesulfonic acid
isoform Sapp2p, in 150 mM sodium citrate buffer, pH 3.75, at 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
48.7
4-(4-dimethylaminophenylazo)benzyl-Glu-His-Val-Lys-Leu-Val-Glu-5-(2-aminoethylamino)-1-naphthalenesulfonic acid
isoform Sapp1p, in 150 mM sodium citrate buffer, pH 3.75, at 37°C
15.2
4-(4-dimethylaminophenylazo)benzyl-Glu-His-Val-Lys-Leu-Val-Glu-5-(2-aminoethylamino)-1-naphthalenesulfonic acid
isoform Sapp2p, in 150 mM sodium citrate buffer, pH 3.75, at 37°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
0.0000003
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
0.0000004
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
0.0000066
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
0.0000146
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
0.0000003
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
0.0019
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
0.0000143
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
0.002782
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
0.0000001
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
0.0000001
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
0.0000072
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
0.00000003
benzyloxycarbonyl-L-Val-L-Val-statine-L-Ala-statine-OH
isoform Sapp2p, in 150 mM sodium citrate buffer, pH 3.75, at 37°C
0.0000004
pepstatin A
isoform Sapp2p, in 150 mM sodium citrate buffer, pH 3.75, at 37°C
0.0003
ritonavir
isoform Sapp2p, 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
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
-
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
the enzyme is temporarily associated with the cell wall
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
isoforms SAPP1 and SAPP2, but not SAPP3, influence adhesion, host cell damage, phagosome-lysosome maturation, phagocytosis, killing capacity, and cytokine secretion by hu-man peripheral blood-derived macrophages
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). CARP1_CANPA
402
0
42833
Swiss-Prot
Secretory Pathway (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
-
the biologically relevant unit of Sapp1p is a monomer, gel filtration
tetramer
-
the tetrameric assembly of Sapp1p is a crystallization artifact
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
-
the Sapp1 precursor can be processed autocatalytically and by a membrane-bound processing proteinase. The pro-segment is indispensable for Sapp1p to attain an appropriate structure
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with pepstatin A, hanging drop vapor diffusion method, using 0.1 M MES pH 6.5, 30% (w/v) PEG 400
Sapp1p in complex with pepstatin A, hanging drop vapor diffusion method, using 0.1 M Tris-HCl, pH 7.0, 2.0 M ammonium sulfate and 10% (v/v) glycerol, at 19°C
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, MonoS column chromatography, and MonoP column chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of SAPP1 is induced only by the presence of exogenous protein as the sole nitrogen source
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Dostal, J.; Dlouha, H.; Malon, P.; Pichova, I.; Hruskova-Heidingsfeldova, O.
The precursor of secreted aspartic proteinase Sapp1p from Candida parapsilosis can be activated both autocatalytically and by a membrane-bound processing proteinase
Biol. Chem.
386
791-799
2005
Candida parapsilosis
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
Merkerova, M.; Dostal, J.; Hradilek, M.; Pichova, I.; Hruskova-Heidingsfeldova, O.
Cloning and characterization of Sapp2p, the second aspartic proteinase isoenzyme from Candida parapsilosis
FEMS Yeast Res.
6
1018-1026
2006
Candida parapsilosis (P32950), Candida parapsilosis, Candida parapsilosis CP386/IDE98 (P32950)
Hruskova-Heidingsfeldova, O.; Dostal, J.; Majer, F.; Havlikova, J.; Hradilek, M.; Pichova, I.
Two aspartic proteinases secreted by the pathogenic yeast Candida parapsilosis differ in expression pattern and catalytic properties
Biol. Chem.
390
259-268
2009
Candida parapsilosis (P32950), Candida parapsilosis (P32951), Candida parapsilosis, Candida parapsilosis P-69 (P32950), Candida parapsilosis P-69 (P32951)
Dostal, J.; Brynda, J.; Hruskova-Heidingsfeldova, O.; Sieglova, I.; Pichova, I.; Rezacova, P.
The crystal structure of the secreted aspartic protease 1 from Candida parapsilosis in complex with pepstatin A
J. Struct. Biol.
167
145-152
2009
Candida parapsilosis, Candida parapsilosis P-69
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
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
Vinterova, Z.; Sanda, M.; Dostal, J.; Hruskova-Heidingsfeldova, O.; Pichova, I.
Evidence for the presence of proteolytically active secreted aspartic proteinase 1 of Candida parapsilosis in the cell wall
Protein Sci.
20
2004-2012
2011
Candida parapsilosis
Dostal, J.; Pecina, A.; Hruskova-Heidingsfeldova, O.; Mareckova, L.; Pichova, I.; Rezacova, P.; Lepsik, M.; Brynda, J.
Atomic resolution crystal structure of Sapp2p, a secreted aspartic protease from Candida parapsilosis
Acta Crystallogr. Sect. D
71
2494-2504
2015
Candida parapsilosis (G8B6Y8), Candida parapsilosis, Candida parapsilosis CDC-317 (G8B6Y8)
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
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
4
e00484-19
2019
Candida parapsilosis (P32951), Candida parapsilosis
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