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(4-Nitro)Phe-Nle-Ala-Leu methyl ester + H2O
Nle-Ala-Leu methyl ester + (4-nitro)Phe
-
-
-
?
Ac-(Ala)m-Lys-(NO2)Phe-(Ala)n amide + H2O
?
-
-
-
-
?
Ac-(Ala)n-Lys-Nph-(Ala)m-amide + H2O
Ac-(Ala)n-Lys + Nph-(Ala)m-amide
-
-
-
?
Ac-Ala-Ala-Ala-Lys-(NO2)Phe-Ala-Ala-amide + H2O
?
Ac-Ala-Ala-Lys-(4-nitro)Phe-Ala-Ala amide + H2O
?
-
-
-
-
?
Ac-Ala-Ala-Lys-(4-nitro)Phe-Ala-Ala-Ala amide + H2O
Ac-Ala-Ala-Lys + (4-nitro)Phe-Ala-Ala-Ala amide
-
-
-
-
?
Ac-Ala-Ala-Lys-(NO2)Phe-Ala-Ala-amide + H2O
?
-
-
-
?
Ac-Ala-Ala-Lys-(NO2)Phe-Ala-amide + H2O
?
-
-
-
?
Ac-Ala-Ala-Lys-(NO2)Phe-amide + H2O
?
Ac-Ala-Ala-Lys-(p-NO2)Phe-Ala-Ala-NH2 + H2O
?
-
-
-
?
Ac-Ala-Lys-(NO2)Phe-Ala-Ala-amide + H2O
?
-
-
-
?
Ac-Ala-Lys-(NO2)Phe-Ala-amide + H2O
?
Ac-Ala-Lys-(NO2)Phe-amide + H2O
?
Ac-Ala-Lys-Ala-(NO2)Phe-amide + H2O
?
-
-
-
-
?
Ac-Gly-Lys-(4-nitro)Phe-Ala-Ala amide + H2O
Ac-Gly-Lys + (4-nitro)Phe-Ala-Ala amide
-
-
-
-
?
Ac-Lys 4-nitrophenyl amide + H2O
?
-
-
-
-
?
Ac-Lys-(NO2)Phe- Ala-amide + H2O
?
Ac-Lys-(NO2)Phe-Ala-Ala-amide + H2O
?
-
-
-
?
Ac-Lys-(NO2)Phe-amide + H2O
?
Ac-Val-Lys-(4-nitro)Phe-Ala amide + H2O
Ac-Val-Lys + (4-nitro)Phe-Ala amide
-
-
-
-
?
Ac-Xaa-Lys-(NO2)Phe-Ala-Ala amide + H2O
?
-
-
-
-
?
B-chain of S-sulfo-insulin + H2O
?
-
-
-
-
?
Bovine serum albumin + H2O
?
-
cleaves 15% of the peptide bonds
-
-
?
bovine trypsinogen + H2O
?
-
-
-
-
?
FVNQHLCGSHLVEALYLVCGERGFFYTPKA + H2O
FVNQHLCGSHLVEALYLVCG + ERGFFYTPKA
i.e. insulin B chain, cleavage site specificity
-
-
?
H-Leu-Ser-(4-nitro)Phe-Nle-Ala-Leu methyl ester + H2O
Nle-Ala-Leu methyl ester + Leu-Ser-(4-nitro)Phe
-
-
-
?
Leu-Ser-(4-nitro)Phe-Nle-Ala-Leu methyl ester + H2O
?
-
-
-
-
?
Pro-Thr-Glu-Phe-(4-nitro)Phe-Arg-Leu + H2O
Pro-Thr-Glu-Phe + (4-nitro)Phe-Arg-Leu
-
-
-
?
trypsin inhibitor + H2O
trypsin inhibitor fragments
-
substrate from Cucurbita maxima, specific cleavage of Leu7-Met8 bond at pH 3.3
-
-
?
trypsinogen + H2O
trypsin + propeptide Val(Asn)4-Lys-OH
substrate from Bos taurus, rapid activation
-
-
?
trypsinogen + H2O
trypsin + Val(Asn)4-Lys
additional information
?
-
Ac-Ala-Ala-Ala-Lys-(NO2)Phe-Ala-Ala-amide + H2O
?
-
-
-
-
?
Ac-Ala-Ala-Ala-Lys-(NO2)Phe-Ala-Ala-amide + H2O
?
-
-
-
?
Ac-Ala-Ala-Lys-(NO2)Phe-amide + H2O
?
-
-
-
-
?
Ac-Ala-Ala-Lys-(NO2)Phe-amide + H2O
?
-
-
-
?
Ac-Ala-Ala-Lys-(NO2)Phe-amide + H2O
?
-
-
-
?
Ac-Ala-Lys-(NO2)Phe-Ala-amide + H2O
?
-
-
-
?
Ac-Ala-Lys-(NO2)Phe-Ala-amide + H2O
?
-
-
-
?
Ac-Ala-Lys-(NO2)Phe-amide + H2O
?
-
-
-
-
?
Ac-Ala-Lys-(NO2)Phe-amide + H2O
?
-
-
-
?
Ac-Ala-Lys-(NO2)Phe-amide + H2O
?
-
-
-
?
Ac-Lys-(NO2)Phe- Ala-amide + H2O
?
-
-
-
?
Ac-Lys-(NO2)Phe- Ala-amide + H2O
?
-
-
-
?
Ac-Lys-(NO2)Phe-amide + H2O
?
-
-
-
-
?
Ac-Lys-(NO2)Phe-amide + H2O
?
-
-
-
?
Ac-Lys-(NO2)Phe-amide + H2O
?
-
-
-
?
azocasein + H2O
?
-
-
-
-
?
azocasein + H2O
?
Penicillium candidum
-
-
-
-
?
azocasein + H2O
?
Penicillium candidum PCA 1/TT031
-
-
-
-
?
Egg albumin + H2O
?
Penicillium duponti
-
best substrate, 30% of the peptide bonds are split after 48 h, at 37øC, pH 3.0
-
-
?
Egg albumin + H2O
?
Penicillium duponti K 1014
-
best substrate, 30% of the peptide bonds are split after 48 h, at 37øC, pH 3.0
-
-
?
Hemoglobin + H2O
?
-
-
-
-
?
Hemoglobin + H2O
?
-
-
-
-
?
Hemoglobin + H2O
?
Penicillium duponti
-
best substrate, 30% of the peptide bonds are split after 48 h, at 37øC, pH 3.0
-
-
?
Hemoglobin + H2O
?
Penicillium duponti K 1014
-
best substrate, 30% of the peptide bonds are split after 48 h, at 37øC, pH 3.0
-
-
?
Milk casein + H2O
?
Penicillium duponti
-
-
-
-
?
Milk casein + H2O
?
Penicillium duponti K 1014
-
-
-
-
?
Trypsinogen + H2O
?
Penicillium duponti
-
-
-
-
?
Trypsinogen + H2O
?
Penicillium duponti K 1014
-
-
-
-
?
Trypsinogen + H2O
?
-
-
-
-
?
Trypsinogen + H2O
?
-
bovine, activation by cleavage of Lys6-Ile7
-
-
?
trypsinogen + H2O
trypsin + Val(Asn)4-Lys
-
rapid activation
-
-
?
trypsinogen + H2O
trypsin + Val(Asn)4-Lys
Penicillium duponti
-
rapid activation
-
-
?
trypsinogen + H2O
trypsin + Val(Asn)4-Lys
Penicillium duponti K1014
-
rapid activation
-
-
?
trypsinogen + H2O
trypsin + Val(Asn)4-Lys
-
rapid activation
-
-
?
wheat flour + H2O
?
-
-
-
-
?
wheat flour + H2O
?
-
-
-
-
?
additional information
?
-
-
broad protein substrate specificity
-
-
?
additional information
?
-
Penicillium duponti
-
broad protein substrate specificity
-
-
?
additional information
?
-
Penicillium duponti K1014
-
broad protein substrate specificity
-
-
?
additional information
?
-
-
milk clotting activity
-
-
?
additional information
?
-
-
acts on some small substrates with two hydrophobic amino acids at the N-terminus and a free amino group, in addition to removing the N-terminal amino acid hydrolytically a trans-peptidation reaction occurs: Leu-Leu is formed from Leu-Tyr-Leu, Phe-Phe from Phe-Tyr-Thr-Pro-Lys-Ala and Met-Met from Met-Leu-Gly
-
-
?
additional information
?
-
-
transpeptidation reaction of both the amino acid and the acyl transfer type
-
-
?
additional information
?
-
-
transpeptidation reaction of both the amino acid and the acyl transfer type
-
-
?
additional information
?
-
-
broad protein substrate specificity with preference for hydrophobic residues at positions P1 and P1', especially for Lys in P1 because the epsilon-amino group forms an ionic bond with the side-chain carboxylate of Asp77, substrate specificity involves the side chain of the P3 residue, mechanism, detailed overview
-
-
?
additional information
?
-
broad protein substrate specificity with preference for hydrophobic residues at positions P1 and P1', especially for Lys in P1 because the epsilon-amino group forms an ionic bond with the side-chain carboxylate of Asp77, substrate specificity involves the side chain of the P3 residue, mechanism, detailed overview
-
-
?
additional information
?
-
broad protein substrate specificity with preference for hydrophobic residues at positions P1 and P1', especially for Lys in P1 because the epsilon-amino group forms an ionic bond with the side-chain carboxylate of Asp77, substrate specificity involves the side chain of the P3 residue, mechanism, detailed overview
-
-
?
additional information
?
-
-
substrate binding specificity, cleavage site specificity, overview
-
-
?
additional information
?
-
substrate binding specificity, cleavage site specificity, overview
-
-
?
additional information
?
-
substrate binding specificity, cleavage site specificity, overview
-
-
?
additional information
?
-
-
broad protein substrate specificity
-
-
?
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1,2-epoxy-3-(4-nitrophenoxy)propane
2-mercaptoethanol
-
10.55% inhibition at 10 mM
alpha-Diazo-p-bromoacetophenone
Penicillium duponti
-
in presence of Cu2+
Benzyloxycarbonyl-Gln-Tyr
-
-
Benzyloxycarbonyl-Glu
-
-
Benzyloxycarbonyl-Val-Tyr
-
-
Ca2+
Penicillium candidum
-
23% residual activity at 10 mM
Diazoacetyl DL-norleucine methyl ester
Diazoacetyl-DL-norleucine methyl ester
Diazoacetylglycine ethyl ester
Penicillium duponti
-
in presence of Cu2+
Difluorostatine- and difluorostatone-containing peptides
-
-
-
EDTA
Penicillium candidum
-
7% residual activity at 10 mM
Fe3+
Penicillium candidum
-
complete inhibition at 10 mM
isovaleryl-Val-statine-ethoxy
pepstatin analogue
Isovaleryl-Val-Val-statyl ethyl ester
-
-
Isovaleryl-Val-Val-statyl-Ala ethyl ester
-
-
K+
Penicillium candidum
-
85% residual activity at 10 mM
KMnO4
Penicillium duponti
-
-
Leu-Gly-Leu
-
inhibits trypsinogen activation, activates cleavage of Leu-Tyr amide
methyl (2S)-2-({hydroxy[({N-[(naphthalen-1-yl)acetyl]-L-valyl}amino)methyl]phosphoryl}oxy)-3-phenylpropanoate
-
-
methyl (2S)-2-({[(4S,7R)-2,5-dioxo-4-(propan-2-yl)-2,3,4,5,6,7-hexahydro-1H-8,10-etheno-3,6-benzodiazacycloundecin-7-yl](hydroxy)phosphoryl}oxy)-3-phenylpropanoate
-
-
methyl (2S)-2-({[(R)-[(N-formyl-L-valyl)amino](naphthalen-2-yl)methyl](hydroxy)phosphoryl}oxy)-3-phenylpropanoate
-
-
methyl 10-hydroxy-6-[[N-(3-methylbutanoyl)valyl]amino]-9-(2-methylpropyl)-4,7-dioxo-11-oxa-3,8-diaza-10-phosphabicyclo[12.3.1]octadeca-1(18),14,16-triene-12-carboxylate 10-oxide
methyl cyclo[(2S)-2-[[(1R)-1-(N-(l-N-(3-methylbutanoyl)valyl-L-aspartyl)amino)-3-methylbutyl]hydroxyphosphinyloxy]-3-(3-aminomethyl)] phenylpropanoate
phosphonate-based macrocycle PPi4, macrocyclic pentapeptide inhibitor
methyl cyclo[(2S)-2-[[(1R)-1-(N-(l-N-(3-methylbutanoyl)valyl-L-aspartyl)amino)-3-methylbutyl]ydroxyphosphinyloxy]-3-(3-aminomethyl)] phenylpropanoate
-
Mg2+
Penicillium candidum
-
31% residual activity at 10 mM
Mn2+
Penicillium candidum
-
98% residual activity at 10 mM
N-(3-methylbutanoyl)valyl-N1-(1-[hydroxy[(1-methoxy-1-oxo-3-phenylpropan-2-yl)oxy]phosphoryl]-3-methylbutyl)aspartamide
-
N-bromosuccinimide
Penicillium duponti
-
-
pepstatin A
-
55.08% inhibition at 10 mM
phenylmethylsulfonyl fluoride
-
complete inhibition at 10 mM
Phosphorus-based peptide analogues
-
-
-
SDS
Penicillium candidum
-
33% residual activity at 10 mM
sodium lauryl sulfate
Penicillium duponti
-
-
Specific pepsin inhibitor produced by Streptomyces naniwaensis
Penicillium duponti
-
-
-
Streptomycin inhibitor
-
weak
-
Zn2+
Penicillium candidum
-
92% residual activity at 10 mM
1,2-epoxy-3-(4-nitrophenoxy)propane
-
-
1,2-epoxy-3-(4-nitrophenoxy)propane
-
enzyme previously inactivated with diazoacetylnorleucine methyl ester does not react, pH-dependence of inhibition
1,2-epoxy-3-(4-nitrophenoxy)propane
-
-
Diazoacetyl DL-norleucine methyl ester
Penicillium duponti
-
in presence of Cu2+
Diazoacetyl DL-norleucine methyl ester
-
in presence of Cu2+
Diazoacetyl DL-norleucine methyl ester
-
-
Diazoacetyl-DL-norleucine methyl ester
-
i.e. DAN, active-site directed inhibitor
Diazoacetyl-DL-norleucine methyl ester
Penicillium duponti
-
i.e. DAN, active-site directed inhibitor, inactivation, also by related compounds
Diazoacetyl-DL-norleucine methyl ester
i.e. DAN, active-site directed inhibitor
methyl 10-hydroxy-6-[[N-(3-methylbutanoyl)valyl]amino]-9-(2-methylpropyl)-4,7-dioxo-11-oxa-3,8-diaza-10-phosphabicyclo[12.3.1]octadeca-1(18),14,16-triene-12-carboxylate 10-oxide
-
-
methyl 10-hydroxy-6-[[N-(3-methylbutanoyl)valyl]amino]-9-(2-methylpropyl)-4,7-dioxo-11-oxa-3,8-diaza-10-phosphabicyclo[12.3.1]octadeca-1(18),14,16-triene-12-carboxylate 10-oxide
includes a methylene bridge between the Asn(P2) and Phe(P1') side chains
additional information
-
not inhibited by EDTA and iodoacetic acid
-
additional information
Penicillium candidum
-
not inhibited by phenylmethylsulfonyl fluoride
-
additional information
Penicillium duponti
-
p-bromophenacylbromide
-
additional information
Penicillium duponti
-
chelating agents; potato inhibitor
-
additional information
-
benzyloxycarbonyl-Phe; not: benzyloxycarbonyl-Tyr; p-bromophenacylbromide
-
additional information
-
investigation of the protonation state penicillopepsin in complex with phosphinate and phosphonate inhibitors
-
additional information
-
p-bromophenacylbromide
-
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Carcinoma
Leucine amino peptidase a better indicator of carcinoma of liver, biliary tract and pancreas.
Cystinuria
Erythropoietic protoporphyria, heterozygous cystinuria, and reduced peptidase A activity in a patient with 46,XX/46,XX,18q--mosaicism.
Hepatitis C
Sequential processing of hepatitis C virus core protein by host cell signal peptidase and signal peptide peptidase: a reassessment.
Mitochondrial Diseases
Controlling proteolysis of Clp peptidase: a possible target for combating mitochondrial diseases.
Neoplasm Metastasis
Exploring the structural aspects of ureido-amino acid-based APN inhibitors: a validated comparative multi-QSAR modelling study.
Neoplasms
A Poly(Lactic-co-Glycolic) Acid Nanovaccine Based on Chimeric Peptides from Different Leishmania infantum Proteins Induces Dendritic Cells Maturation and Promotes Peptide-Specific IFN?-Producing CD8(+) T Cells Essential for the Protection against Experimental Visceral Leishmaniasis.
Neoplasms
Exploring the structural aspects of ureido-amino acid-based APN inhibitors: a validated comparative multi-QSAR modelling study.
Protoporphyria, Erythropoietic
Erythropoietic protoporphyria, heterozygous cystinuria, and reduced peptidase A activity in a patient with 46,XX/46,XX,18q--mosaicism.
Sarcoma
Sheep gene mapping: additional DNA markers included (CASB, CASK, LALBA, IGF-1 and AMH).
Trisomy 18 Syndrome
Fibroblasts of two patients with trisomy 18 show 1.5-fold increase in peptidase A activity over normal human diploid fibroblasts.
Tuberculosis
Lipoproteins are major targets of the polyclonal human T cell response to Mycobacterium tuberculosis.
Tuberculosis
TLR2-Modulating Lipoproteins of the Mycobacterium tuberculosis Complex Enhance the HIV Infectivity of CD4+ T Cells.
Virus Diseases
Exploring the structural aspects of ureido-amino acid-based APN inhibitors: a validated comparative multi-QSAR modelling study.
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0.075
Ac-Ala-Ala-Ala-Lys-(4-nitro)-Phe-Ala-Ala amide
-
pH 5.5 (pH-optimum for kcat)
0.39 - 0.68
Ac-Ala-Ala-Ala-Lys-(NO2)Phe-Ala-Ala-amide
0.25
Ac-Ala-Ala-Lys-(4-nitro)Phe amide
-
pH 4.5 (pH optimum for kcat)
0.078 - 0.44
Ac-Ala-Ala-Lys-(4-nitro)Phe-Ala-Ala amide
0.32 - 0.59
Ac-Ala-Ala-Lys-(NO2)Phe-Ala-Ala-amide
0.35 - 0.71
Ac-Ala-Ala-Lys-(NO2)Phe-Ala-amide
0.37 - 0.8
Ac-Ala-Ala-Lys-(NO2)Phe-amide
0.41
Ac-Ala-Lys-(4-nitro)Phe amide
-
pH 4.3 (optimum for kcat)
0.41 - 0.6
Ac-Ala-Lys-(NO2)Phe-Ala-Ala-amide
0.3 - 0.83
Ac-Ala-Lys-(NO2)Phe-Ala-amide
0.4 - 0.75
Ac-Ala-Lys-(NO2)Phe-amide
0.07
Ac-Gly-Lys-(4-nitro)Phe-Ala-Ala amide
-
pH 4.5
0.22
Ac-Lys 4-nitrophenyl amide
-
-
0.6
Ac-Lys-(4-nitro)Phe amide
-
pH 3.8-4.2 (optimum for kcat)
0.21 - 0.77
Ac-Lys-(NO2)Phe-Ala-Ala-amide
0.5 - 0.83
Ac-Lys-(NO2)Phe-Ala-amide
0.4 - 0.65
Ac-Lys-(NO2)Phe-amide
0.017
Ac-Val-Lys-(4-nitro)Phe-Ala amide
-
-
0.004 - 0.01
Leu-Ser-(4-nitro)Phe-Nle-Ala-Leu methyl ester
0.005
Pro-Thr-Glu-Phe-(4-nitro)Phe-Arg-Leu
-
-
additional information
additional information
-
0.39
Ac-Ala-Ala-Ala-Lys-(NO2)Phe-Ala-Ala-amide
-
pH 5.0, 25°C, mutant T291S
0.46
Ac-Ala-Ala-Ala-Lys-(NO2)Phe-Ala-Ala-amide
-
pH 5.0, 25°C, wild-type Pencillopepsin JT-2
0.55
Ac-Ala-Ala-Ala-Lys-(NO2)Phe-Ala-Ala-amide
-
pH 5.0, 25°C, mutant T291G
0.59
Ac-Ala-Ala-Ala-Lys-(NO2)Phe-Ala-Ala-amide
-
pH 5.0, 25°C, mutant T291V
0.68
Ac-Ala-Ala-Ala-Lys-(NO2)Phe-Ala-Ala-amide
-
pH 5.0, 25°C, mutant T291A
0.078
Ac-Ala-Ala-Lys-(4-nitro)Phe-Ala-Ala amide
-
pH 5.5
0.44
Ac-Ala-Ala-Lys-(4-nitro)Phe-Ala-Ala amide
-
-
0.32
Ac-Ala-Ala-Lys-(NO2)Phe-Ala-Ala-amide
-
pH 5.0, 25°C, wild-type Pencillopepsin JT-2
0.4
Ac-Ala-Ala-Lys-(NO2)Phe-Ala-Ala-amide
-
pH 5.0, 25°C, mutant T219G
0.48
Ac-Ala-Ala-Lys-(NO2)Phe-Ala-Ala-amide
-
pH 5.0, 25°C, mutant T219S
0.5
Ac-Ala-Ala-Lys-(NO2)Phe-Ala-Ala-amide
-
pH 5.0, 25°C, mutant T219V
0.59
Ac-Ala-Ala-Lys-(NO2)Phe-Ala-Ala-amide
-
pH 5.0, 25°C, mutant T219A
0.35
Ac-Ala-Ala-Lys-(NO2)Phe-Ala-amide
-
pH 5.0, 25°C, wild-type Pencillopepsin JT-2
0.45
Ac-Ala-Ala-Lys-(NO2)Phe-Ala-amide
-
pH 5.0, 25°C, mutant T219G
0.48
Ac-Ala-Ala-Lys-(NO2)Phe-Ala-amide
-
pH 5.0, 25°C, mutant T219S
0.71
Ac-Ala-Ala-Lys-(NO2)Phe-Ala-amide
-
pH 5.0, 25°C, mutant T219V and T219A
0.37
Ac-Ala-Ala-Lys-(NO2)Phe-amide
-
pH 5.0, 25°C, and mutant T219S
0.45
Ac-Ala-Ala-Lys-(NO2)Phe-amide
-
pH 5.0, 25°C, mutant T219G
0.5
Ac-Ala-Ala-Lys-(NO2)Phe-amide
-
pH 5.0, 25°C, wild-type Pencillopepsin JT-2
0.6
Ac-Ala-Ala-Lys-(NO2)Phe-amide
-
pH 5.0, 25°C, mutant T219V
0.8
Ac-Ala-Ala-Lys-(NO2)Phe-amide
-
pH 5.0, 25°C, mutant T219A
0.41
Ac-Ala-Lys-(NO2)Phe-Ala-Ala-amide
-
pH 5.0, 25°C, wild-type Pencillopepsin JT-2
0.45
Ac-Ala-Lys-(NO2)Phe-Ala-Ala-amide
-
pH 5.0, 25°C, mutant T219V
0.46
Ac-Ala-Lys-(NO2)Phe-Ala-Ala-amide
-
pH 5.0, 25°C, mutant T219S
0.6
Ac-Ala-Lys-(NO2)Phe-Ala-Ala-amide
-
pH 5.0, 25°C, mutant T219A
0.3
Ac-Ala-Lys-(NO2)Phe-Ala-amide
-
pH 5.0, 25°C, mutant T219S
0.5
Ac-Ala-Lys-(NO2)Phe-Ala-amide
-
pH 5.0, 25°C, wild-type Pencillopepsin JT-2
0.6
Ac-Ala-Lys-(NO2)Phe-Ala-amide
-
pH 5.0, 25°C, mutant T219A
0.8
Ac-Ala-Lys-(NO2)Phe-Ala-amide
-
pH 5.0, 25°C, mutant T219V
0.83
Ac-Ala-Lys-(NO2)Phe-Ala-amide
-
pH 5.0, 25°C, mutant T219G
0.4
Ac-Ala-Lys-(NO2)Phe-amide
-
pH 5.0, 25°C, wild-type Pencillopepsin JT-2
0.42
Ac-Ala-Lys-(NO2)Phe-amide
-
pH 5.0, 25°C, mutant T219S
0.54
Ac-Ala-Lys-(NO2)Phe-amide
-
pH 5.0, 25°C, mutant T219G
0.6
Ac-Ala-Lys-(NO2)Phe-amide
-
pH 5.0, 25°C, mutant T219V
0.75
Ac-Ala-Lys-(NO2)Phe-amide
-
pH 5.0, 25°C, mutant T219A
0.21
Ac-Lys-(NO2)Phe-Ala-Ala-amide
-
pH 5.0, 25°C, wild-type Pencillopepsin JT-2
0.55
Ac-Lys-(NO2)Phe-Ala-Ala-amide
-
pH 5.0, 25°C, mutant T219V
0.6
Ac-Lys-(NO2)Phe-Ala-Ala-amide
-
pH 5.0, 25°C, mutant T219G and T219S
0.77
Ac-Lys-(NO2)Phe-Ala-Ala-amide
-
pH 5.0, 25°C, mutant T219A
0.5
Ac-Lys-(NO2)Phe-Ala-amide
-
pH 5.0, 25°C, mutant T219S
0.57
Ac-Lys-(NO2)Phe-Ala-amide
-
pH 5.0, 25°C, mutant T219V
0.59
Ac-Lys-(NO2)Phe-Ala-amide
-
pH 5.0, 25°C, wild-type Pencillopepsin JT-2
0.74
Ac-Lys-(NO2)Phe-Ala-amide
-
pH 5.0, 25°C, mutant T219G
0.83
Ac-Lys-(NO2)Phe-Ala-amide
-
pH 5.0, 25°C, mutant T219A
0.4
Ac-Lys-(NO2)Phe-amide
-
pH 5.0, 25°C, wild-type Pencillopepsin JT-2
0.46
Ac-Lys-(NO2)Phe-amide
-
pH 5.0, 25°C, mutant T219V
0.48
Ac-Lys-(NO2)Phe-amide
-
pH 5.0, 25°C, mutant T219G
0.51
Ac-Lys-(NO2)Phe-amide
-
pH 5.0, 25°C, mutant T219S
0.65
Ac-Lys-(NO2)Phe-amide
-
pH 5.0, 25°C, mutant T219A
0.004
Leu-Ser-(4-nitro)Phe-Nle-Ala-Leu methyl ester
-
pH 5.5
0.01
Leu-Ser-(4-nitro)Phe-Nle-Ala-Leu methyl ester
-
pH 3.5
additional information
additional information
-
-
-
additional information
additional information
-
overview: Km values for the hydrolysis of the peptides of the series Ac-(Ala)m-Lys-(4-nitro)Phe-(Ala)n amide and of the series Ac-Xaa-Lys-(4-nitro)Phe-Ala-Ala amide at the pH optimum for kcat, at pH 5.5 and pH 6.0
-
additional information
additional information
-
substrate binding subsite kinetics
-
additional information
additional information
substrate binding subsite kinetics
-
additional information
additional information
substrate binding subsite kinetics
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.35 - 34
Ac-Ala-Ala-Ala-Lys-(NO2)Phe-Ala-Ala-amide
28.8 - 47
Ac-Ala-Ala-Lys-(4-nitro)Phe-Ala-Ala amide
45
Ac-Ala-Ala-Lys-(4-nitro)Phe-Ala-Ala-Ala amide
-
pH 5.5 (pH-optimum for kcat)
0.3 - 40
Ac-Ala-Ala-Lys-(NO2)Phe-Ala-Ala-amide
0.09 - 15
Ac-Ala-Ala-Lys-(NO2)Phe-Ala-amide
0.0019 - 0.36
Ac-Ala-Ala-Lys-(NO2)Phe-amide
0.021
Ac-Ala-Lys-(4-nitro)Phe amide
-
pH 4.3 (pH-optimum for kcat)
0.15 - 0.45
Ac-Ala-Lys-(NO2)Phe-Ala-Ala-amide
0.046 - 0.6
Ac-Ala-Lys-(NO2)Phe-Ala-amide
0.003 - 0.0054
Ac-Ala-Lys-(NO2)Phe-amide
0.003
Ac-Ala-Lys-Ala-(NO2)Phe-amide
-
pH 5.0, 25°C, mutant T219S
0.01
Ac-Lys 4-nitrophenyl amide
-
pH 5.5
0.026
Ac-Lys-(4-nitro)Phe amide
-
pH 3.8-4.2 (pH-optimum for kcat)
0.12 - 0.43
Ac-Lys-(NO2)Phe-Ala-Ala-amide
0.042 - 0.4
Ac-Lys-(NO2)Phe-Ala-amide
0.0016 - 0.005
Ac-Lys-(NO2)Phe-amide
5
bovine trypsinogen
-
-
-
6.4 - 11.4
Leu-Ser-(4-nitro)Phe-Nle-Ala-Leu methyl ester
37.3
Pro-Thr-Glu-Phe-(4-nitro)Phe-Arg-Leu
-
-
additional information
additional information
-
0.35
Ac-Ala-Ala-Ala-Lys-(NO2)Phe-Ala-Ala-amide
-
pH 5.0, 25°C, mutant T291V
0.36
Ac-Ala-Ala-Ala-Lys-(NO2)Phe-Ala-Ala-amide
-
pH 5.0, 25°C, mutant T291A
0.45
Ac-Ala-Ala-Ala-Lys-(NO2)Phe-Ala-Ala-amide
-
pH 5.0, 25°C, mutant T291G
16.1
Ac-Ala-Ala-Ala-Lys-(NO2)Phe-Ala-Ala-amide
-
pH 5.0, 25°C, mutant T291S
34
Ac-Ala-Ala-Ala-Lys-(NO2)Phe-Ala-Ala-amide
-
pH 5.0, 25°C, wild-type pencillopepsin JT-2
28.8
Ac-Ala-Ala-Lys-(4-nitro)Phe-Ala-Ala amide
-
pH 3.5
36
Ac-Ala-Ala-Lys-(4-nitro)Phe-Ala-Ala amide
-
pH 5.5
47
Ac-Ala-Ala-Lys-(4-nitro)Phe-Ala-Ala amide
-
pH 4.5 (pH-optimum for kcat)
0.3
Ac-Ala-Ala-Lys-(NO2)Phe-Ala-Ala-amide
-
pH 5.0, 25°C, mutant T219V
0.45
Ac-Ala-Ala-Lys-(NO2)Phe-Ala-Ala-amide
-
pH 5.0, 25°C, mutant T219A
0.5
Ac-Ala-Ala-Lys-(NO2)Phe-Ala-Ala-amide
-
pH 5.0, 25°C, mutant T219G
14.9
Ac-Ala-Ala-Lys-(NO2)Phe-Ala-Ala-amide
-
pH 5.0, 25°C, mutant T219S
40
Ac-Ala-Ala-Lys-(NO2)Phe-Ala-Ala-amide
-
pH 5.0, 25°C, wild-type pencillopepsin JT-2
0.09
Ac-Ala-Ala-Lys-(NO2)Phe-Ala-amide
-
pH 5.0, 25°C, mutant T219A
0.12
Ac-Ala-Ala-Lys-(NO2)Phe-Ala-amide
-
pH 5.0, 25°C, mutant T219V
0.35
Ac-Ala-Ala-Lys-(NO2)Phe-Ala-amide
-
pH 5.0, 25°C, mutant T219G
3.8
Ac-Ala-Ala-Lys-(NO2)Phe-Ala-amide
-
pH 5.0, 25°C, mutant T219S
15
Ac-Ala-Ala-Lys-(NO2)Phe-Ala-amide
-
pH 5.0, 25°C, wild-type pencillopepsin JT-2
0.0019
Ac-Ala-Ala-Lys-(NO2)Phe-amide
-
pH 5.0, 25°C, and mutant T219V
0.003
Ac-Ala-Ala-Lys-(NO2)Phe-amide
-
pH 5.0, 25°C, mutant T219G
0.004
Ac-Ala-Ala-Lys-(NO2)Phe-amide
-
pH 5.0, 25°C, mutant T219A
0.11
Ac-Ala-Ala-Lys-(NO2)Phe-amide
-
pH 5.0, 25°C, mutant T219S
0.36
Ac-Ala-Ala-Lys-(NO2)Phe-amide
-
pH 5.0, 25°C, wild-type pencillopepsin JT-2
0.15
Ac-Ala-Lys-(NO2)Phe-Ala-Ala-amide
-
pH 5.0, 25°C, mutant T219S
0.24
Ac-Ala-Lys-(NO2)Phe-Ala-Ala-amide
-
pH 5.0, 25°C, mutant T219G
0.3
Ac-Ala-Lys-(NO2)Phe-Ala-Ala-amide
-
pH 5.0, 25°C, mutant T219A
0.3
Ac-Ala-Lys-(NO2)Phe-Ala-Ala-amide
-
pH 5.0, 25°C, wild-type pencillopepsin JT-2
0.45
Ac-Ala-Lys-(NO2)Phe-Ala-Ala-amide
-
pH 5.0, 25°C, mutant T219V and T219G
0.046
Ac-Ala-Lys-(NO2)Phe-Ala-amide
-
pH 5.0, 25°C, mutant T219A
0.09
Ac-Ala-Lys-(NO2)Phe-Ala-amide
-
pH 5.0, 25°C, mutant T219S
0.13
Ac-Ala-Lys-(NO2)Phe-Ala-amide
-
pH 5.0, 25°C, mutant T219G
0.23
Ac-Ala-Lys-(NO2)Phe-Ala-amide
-
pH 5.0, 25°C, mutant T219V
0.6
Ac-Ala-Lys-(NO2)Phe-Ala-amide
-
pH 5.0, 25°C, wild-type pencillopepsin JT-2
0.003
Ac-Ala-Lys-(NO2)Phe-amide
-
pH 5.0, 25°C, mutant T219G
0.003
Ac-Ala-Lys-(NO2)Phe-amide
-
pH 5.0, 25°C, wild-type pencillopepsin JT-2
0.005
Ac-Ala-Lys-(NO2)Phe-amide
-
pH 5.0, 25°C, mutant T219A
0.0054
Ac-Ala-Lys-(NO2)Phe-amide
-
pH 5.0, 25°C, mutant T219V
0.12
Ac-Lys-(NO2)Phe-Ala-Ala-amide
-
pH 5.0, 25°C, mutant T219A
0.17
Ac-Lys-(NO2)Phe-Ala-Ala-amide
-
pH 5.0, 25°C, mutant T219V
0.29
Ac-Lys-(NO2)Phe-Ala-Ala-amide
-
pH 5.0, 25°C, wild-type pencillopepsin JT-2
0.33
Ac-Lys-(NO2)Phe-Ala-Ala-amide
-
pH 5.0, 25°C, mutant T219S
0.43
Ac-Lys-(NO2)Phe-Ala-Ala-amide
-
pH 5.0, 25°C, mutant T219G
0.042
Ac-Lys-(NO2)Phe-Ala-amide
-
pH 5.0, 25°C, mutant T219A
0.05
Ac-Lys-(NO2)Phe-Ala-amide
-
pH 5.0, 25°C, mutant T219V
0.07
Ac-Lys-(NO2)Phe-Ala-amide
-
pH 5.0, 25°C, mutant T219S
0.14
Ac-Lys-(NO2)Phe-Ala-amide
-
pH 5.0, 25°C, mutant T219G
0.4
Ac-Lys-(NO2)Phe-Ala-amide
-
pH 5.0, 25°C, wild-type pencillopepsin JT-2
0.0016
Ac-Lys-(NO2)Phe-amide
-
pH 5.0, 25°C, mutant T219V
0.002
Ac-Lys-(NO2)Phe-amide
-
pH 5.0, 25°C, wild-type pencillopepsin JT-2 and mutant T219A
0.003
Ac-Lys-(NO2)Phe-amide
-
pH 5.0, 25°C, mutant T219S
0.005
Ac-Lys-(NO2)Phe-amide
-
pH 5.0, 25°C, mutant T219G
6.4
Leu-Ser-(4-nitro)Phe-Nle-Ala-Leu methyl ester
-
pH 3.5
11.4
Leu-Ser-(4-nitro)Phe-Nle-Ala-Leu methyl ester
-
pH 5.5
additional information
additional information
-
-
-
additional information
additional information
-
overview: turnover numbers for the hydrolysis of the peptides of the series Ac-(Ala)m-Lys-(4-nitro)Phe-(Ala)n amide and of the series Ac-Xaa-Lys-(4-nitro)Phe-Ala-Ala amide at the pH optimum for kcat, at pH 5.5 and pH 6.0
-
additional information
additional information
-
effect of chain length of substrates and inhibitors of the turnover number
-
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Hofmann, T.
Penicillopepsin
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45
434-452
1976
Penicillium janthinellum
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Purification and properties of the thermostable acid protease of Penicillium duponti
Biochemistry
15
842-848
1976
Penicillium duponti, Penicillium duponti K 1014
brenda
Hsu, I.N.; Delbaere, L.T.J.; James, M.N.G.
Penicillopepsin from Penicillium janthinellum crystal structure at 2.8 A and sequence homology with porcine pepsin
Nature
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1977
Penicillium janthinellum
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Hofmann, T.; Allen, B.; Bendiner, M.; Blum, M.; Cunningham, A.
Effect of secondary substrate binding in penicillopepsin: contributions of subsites S3 and S2 to kcat
Biochemistry
27
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1988
Penicillium janthinellum
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Dunn, B.M.; Jimenez, M.; Parten, B.F.; Valler, M.J.; Rolph, C.E.; Kay, J.
A systematic series of synthetic chromophoric substrates for aspartic proteinases
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Penicillium janthinellum
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Mechanism of acid protease catalysis based on the crystal structure of penicillopepsin
Nature
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1977
Penicillium janthinellum
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Mains, G.; Hofmann, T.
The inactivation of penicillopepsin with 1,2-epoxy-3-(p-nitrophenoxy) propane, an active-site directed reagent
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Penicillium janthinellum
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Acyl and amino intermediates in penicillopepsin-catalysed reactions and activation by nonsubstrate peptides
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1977
Penicillium janthinellum
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The crystal structure of penicillopesin at 6 A resolution
Biochem. Biophys. Res. Commun.
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1976
Penicillium janthinellum
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A rennin-like enzyme from Penicillium expansum
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40
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1976
Penicillium expansum
-
brenda
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Some properties of acid protease from the thermophilic fungus, Penicillium duponti K1014
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25
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1973
Penicillium duponti, Penicillium duponti K 1014
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Hashimoto, H.; Kaneko, Y.; Iwaasa, T.; Yokotsuka, T.
Production and purification of acid protease from the thermophilic fungus, Penicillium duponti K1014
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25
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1973
Penicillium duponti, Penicillium duponti K 1014
brenda
Blum, M.; Cunningham, A.; Bendiner, M.; Hofmann, T.
Penicillopepsin, the aspartic proteinase from Penicillium janthinellum: substrate-binding effects and intermediates in transpeptidation reactions
Biochem. Soc. Trans.
13
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1985
Penicillium janthinellum
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James, M.N.G.; Sielecki, A.R.
Stereochemical analysis of peptide bond hydrolysis catalyzed by the aspartic proteinase penicillopepsin
Biochemistry
24
3701-3713
1985
Penicillium janthinellum
brenda
Hofmann, T.; Hodges, R.S.; James, M.N.G.
Effect of pH on the activities of penicillopepsin and Rhizopus pepsin and a proposal for the productive substrate binding mode in penicillopepsin
Biochemistry
23
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1984
Penicillium janthinellum
brenda
James, M.N.G.; Sielecki, A.R.
Structure and refinement of penicillopepsin at 1.8 A resolution
J. Mol. Biol.
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1983
Penicillium janthinellum
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James, M.N.G.; Sielecki, A.R.; Hayakawa, K.; Gelb, M.H.
Crystallographic analysis of transition state mimics bound to penicillopepsin: difluorostatine- and difluorostatone-containing peptides
Biochemistry
31
3872-3886
1992
Penicillium janthinellum
brenda
Fraser, M.E.; Strynadka, N.C.J.; Bartlett, P.A.; Hanson, J.E.; James, M.N.G.
Crystallographic analysis of transition-state mimics bound to penicillopepsin: phosphorus-containing peptide analogues
Biochemistry
31
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1992
Penicillium janthinellum
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Houmard, J.; Raymond, M.N.
Further characterization of the Penicillium roqueforti acid protease
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61
979-982
1979
Penicillium roqueforti
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Gripon, J.C.
Inactivation of Penicillium roqueforti acid protease by specific pepsin inhibitors
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58
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1976
Penicillium roqueforti
brenda
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Overcoming the unfavourable entropic contribution of ligand binding with a macrocyclic inhibitor bound to penicillopepsin
Adv. Exp. Med. Biol.
436
355-359
1998
Penicillium sp.
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Khan, A.R.; Parrish, J.C.; Fraser, M.E.; Smith, W.W.; Bartlett, P.A.; James, M.N.G.
Lowering the entropic barrier for binding conformationally flexible inhibitors to enzymes
Biochemistry
37
16839-16845
1998
Penicillium janthinellum (P00798)
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Cao, Q.N.; Stubbs, M.; Ngo, K.Q.; Ward, M.; Cunningham, A.; Pai, E.F.; Tu, G.C.; Hofmann, T.
Penicillopepsin-JT2, a recombinant enzyme from Penicillium janthinellum and the contribution of a hydrogen bond in subsite S3 to k(cat)
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9
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2000
Penicillium janthinellum, Penicillium janthinellum NRRL 905
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Hofmann, T.
Penicillopepsin
Handbook of Proteolytic Enzymes (Barrett, J. ; Rawlings, N. D. ; Woessner, J. F. , eds. )
1
99-104
2004
Penicillium camemberti, Penicillium duponti, Penicillium janthinellum, Penicillium janthinellum (P78735), Penicillium janthinellum (Q9HEZ3), Penicillium roqueforti, Penicillium duponti K1014
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Vidossich, P.; Carloni, P.
Binding of phosphinate and phosphonate inhibitors to aspartic proteases: a first-principles study
J. Phys. Chem. B
110
1437-1442
2006
Penicillium janthinellum
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Smirnova, I.; Sereda, A.; Kostyleva, E.; Tsurikova, N.; Bushina, E.; Rozhkova, A.; Sinitsyn, A.
A new enzyme preparation with high penicillopepsin activity based on the producer strain Penicillium canescens
Appl. Biochem. Microbiol.
51
660-666
2015
Penicillium canescens, Penicillium canescens RN3-11-7 niaD(-)
brenda
Alhelli, A.; Manap, M.; Mohammed, A.; Mirhosseini, H.; Suliman, E.; Shad, Z.; Mohammed, N.; Hussin, A.
Response surface methodology modelling of an aqueous two-phase system for purification of protease from Penicillium candidum (PCA 1/TT031) under solid state fermentation and its biochemical characterization
Int. J. Mol. Sci.
17
1872
2016
Penicillium candidum, Penicillium candidum PCA 1/TT031
brenda
Suarez, D.; Diaz, N.
Ligand strain and entropic effects on the binding of macrocyclic and linear inhibitors molecular modeling of penicillopepsin complexes
J. Chem. Inf. Model.
57
2045-2055
2017
Penicillium janthinellum (P00798)
brenda
Duarte Neto, J.; Wanderley, M.; Lima, C.; Porto, A.
Single step purification via magnetic nanoparticles of new broad pH active protease from Penicillium aurantiogriseum
Protein Expr. Purif.
147
22-28
2018
Penicillium aurantiogriseum
brenda