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Information on EC 3.4.23.20 - Penicillopepsin
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3.4.23.20 PenicillopepsinSpecify your search results
Word Map
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Hydrolysis of proteins with broad specificity similar to that of pepsin A, preferring hydrophobic residues at P1 and P1', but also cleaving Gly20-/-Glu in the B chain of insulin. Clots milk, and activates trypsinogen
Synonyms
penicillopepsin, peptidase a, mold kinase, acid protease a, penicillopepsin-jt2, penicillium janthinellum acid proteinase, penicillopepsin-jt1, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Acid protease A
-
-
-
-
EC 3.4.23.6
-
-
formerly
-
EC 3.4.23.7
-
-
formerly
-
EC 3.4.4.17
-
-
formerly, part transferred
-
pencillopepsin-JT1
pencillopepsin-JT2
Penicillium citrinum acid proteinase
-
-
-
-
Penicillium cyclopium acid proteinase
-
-
-
-
Penicillium expansum acid proteinase
-
-
-
-
Penicillium janthinellum acid proteinase
-
-
-
-
Penicillium janthinellum aspartic proteinase
Penicillium roqueforti acid proteinase
-
-
-
-
PEP
PepA
Peptidase A
Proteinase, Penicillium aspartic
-
-
-
-
Proteinase, Penicillium caseicolum aspartic
-
-
-
-
Proteinase, Penicillium citrinum aspartic
-
-
-
-
Proteinase, Penicillium cyclopium acid
-
-
-
-
Proteinase, Penicillium duponti aspartic
-
-
-
-
Proteinase, Penicillium expansum aspartic
-
-
-
-
Proteinase, Penicillium janthinellum acid
-
-
-
-
Proteinase, Penicillium roqueforti aspartic
-
-
-
-
additional information
Penicillium janthinellum aspartic proteinase
-
-
-
-
Peptidase A
-
-
-
-
additional information
-
the enzyme belongs to the A1 peptidase family
additional information
the enzyme belongs to the A1 peptidase family
additional information
the enzyme belongs to the A1 peptidase family
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Hydrolysis of proteins with broad specificity similar to that of pepsin A, preferring hydrophobic residues at P1 and P1', but also cleaving Gly20-/-Glu in the B chain of insulin. Clots milk, and activates trypsinogen
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
aspartic endopeptidase
-
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CAS REGISTRY NUMBER
COMMENTARY
9074-08-2
-
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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-Nitro)Phe-Nle-Ala-Leu methyl ester + H2O
Nle-Ala-Leu methyl ester + (4-nitro)Phe
-
-
-
?
Ac-(Ala)n-Lys-Nph-(Ala)m-amide + H2O
Ac-(Ala)n-Lys + Nph-(Ala)m-amide
-
-
-
?
Ac-Ala-Ala-Lys-(4-nitro)Phe-Ala-Ala-Ala amide + H2O
Ac-Ala-Ala-Lys + (4-nitro)Phe-Ala-Ala-Ala amide
-
-
-
-
?
Ac-Gly-Lys-(4-nitro)Phe-Ala-Ala amide + H2O
Ac-Gly-Lys + (4-nitro)Phe-Ala-Ala amide
-
-
-
-
?
Ac-Val-Lys-(4-nitro)Phe-Ala amide + H2O
Ac-Val-Lys + (4-nitro)Phe-Ala amide
-
-
-
-
?
Bovine serum albumin + H2O
?
-
cleaves 15% of the peptide bonds
-
-
?
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
-
-
-
?
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
-
-
?
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
?
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
-
-
?
Trypsinogen + H2O
?
-
bovine, activation by cleavage of Lys6-Ile7
-
-
?
additional information
?
-
-
broad protein substrate specificity
-
-
?
additional information
?
-
Penicillium duponti K1014
-
broad protein substrate specificity
-
-
?
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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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
N-(3-methylbutanoyl)valyl-N1-(1-[hydroxy[(1-methoxy-1-oxo-3-phenylpropan-2-yl)oxy]phosphoryl]-3-methylbutyl)aspartamide
-
1,2-epoxy-3-(4-nitrophenoxy)propane
-
enzyme previously inactivated with diazoacetylnorleucine methyl ester does not react, pH-dependence of inhibition
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
-
benzyloxycarbonyl-Phe; not: benzyloxycarbonyl-Tyr; p-bromophenacylbromide
-
additional information
-
investigation of the protonation state penicillopepsin in complex with phosphinate and phosphonate inhibitors
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Leu-Gly-Leu
-
inhibits trypsinogen activation, activates cleavage of Leu-Tyr amide
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
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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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.075
Ac-Ala-Ala-Ala-Lys-(4-nitro)-Phe-Ala-Ala amide
-
pH 5.5 (pH-optimum for kcat)
0.25
Ac-Ala-Ala-Lys-(4-nitro)Phe amide
-
pH 4.5 (pH optimum for kcat)
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
0.32
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
0.71
Ac-Ala-Ala-Lys-(NO2)Phe-Ala-amide
-
pH 5.0, 25°C, mutant T219V and T219A
0.5
Ac-Ala-Ala-Lys-(NO2)Phe-amide
-
pH 5.0, 25°C, wild-type Pencillopepsin JT-2
0.41
Ac-Ala-Lys-(NO2)Phe-Ala-Ala-amide
-
pH 5.0, 25°C, wild-type Pencillopepsin JT-2
0.5
Ac-Ala-Lys-(NO2)Phe-Ala-amide
-
pH 5.0, 25°C, wild-type Pencillopepsin JT-2
0.4
Ac-Ala-Lys-(NO2)Phe-amide
-
pH 5.0, 25°C, wild-type Pencillopepsin JT-2
0.21
Ac-Lys-(NO2)Phe-Ala-Ala-amide
-
pH 5.0, 25°C, wild-type Pencillopepsin JT-2
0.6
Ac-Lys-(NO2)Phe-Ala-Ala-amide
-
pH 5.0, 25°C, mutant T219G and T219S
0.59
Ac-Lys-(NO2)Phe-Ala-amide
-
pH 5.0, 25°C, wild-type Pencillopepsin JT-2
0.4
Ac-Lys-(NO2)Phe-amide
-
pH 5.0, 25°C, wild-type Pencillopepsin JT-2
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
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
45
Ac-Ala-Ala-Lys-(4-nitro)Phe-Ala-Ala-Ala amide
-
pH 5.5 (pH-optimum for kcat)
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
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
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
0.36
Ac-Ala-Ala-Lys-(NO2)Phe-amide
-
pH 5.0, 25°C, wild-type pencillopepsin JT-2
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
0.6
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, wild-type pencillopepsin JT-2
0.29
Ac-Lys-(NO2)Phe-Ala-Ala-amide
-
pH 5.0, 25°C, wild-type pencillopepsin JT-2
0.4
Ac-Lys-(NO2)Phe-Ala-amide
-
pH 5.0, 25°C, wild-type pencillopepsin JT-2
0.002
Ac-Lys-(NO2)Phe-amide
-
pH 5.0, 25°C, wild-type pencillopepsin JT-2 and mutant T219A
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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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.11
methyl (2S)-2-({hydroxy[({N-[(naphthalen-1-yl)acetyl]-L-valyl}amino)methyl]phosphoryl}oxy)-3-phenylpropanoate
-
-
0.0008
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
-
-
0.0076
methyl (2S)-2-({[(R)-[(N-formyl-L-valyl)amino](naphthalen-2-yl)methyl](hydroxy)phosphoryl}oxy)-3-phenylpropanoate
-
-
0.0000001
methyl cyclo[(2S)-2-[[(1R)-1-(N-(l-N-(3-methylbutanoyl)valyl-L-aspartyl)amino)-3-methylbutyl]ydroxyphosphinyloxy]-3-(3-aminomethyl)] phenylpropanoate
pH 4.6, macrocyclic pentapeptide inhibitor
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 6
-
about 45% activity at pH 3.0, 100% activity at pH 4.0, about 90% activity at pH 5.0, about 30% activity at pH 6.0
6 - 11
-
the purified enzyme maintains over 60% of activity from pH 6.0 to 11.0
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
75
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
15 - 55
-
the purified enzyme keeps more than 48% activity from 15 to 55°C
30 - 60
-
about 50% activity at 30°C, about 80% activity at 40°C, 100% activity at 50°C, about 35% activity at 60°C
4 - 50
Penicillium candidum
-
the enzyme retains more than 80% of its initial activity at 4-50 °C. The activity is reduced to 52% at 60°C
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Penicillium duponti
-
-
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
secreted by mycelium during phase of sporulation
-
brenda
Show AA Sequence and Transmembrane Helices (180 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
41590
additional information
additional information
-
amino acid sequence from Penicillium janthinellum enzyme
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
?
Penicillium candidum PCA 1/TT031
-
x * 100000-140000, SDS-PAGE
-
?
Penicillium duponti K1014
-
x * 41590
-
additional information
three-dimensional structure and comparison
additional information
three-dimensional structure and comparison
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
proteolytic modification
glycoprotein
Penicillium duponti K 1014
-
contains 4.33% carbohydrate expressed as glucose
-
glycoprotein
Penicillium duponti K1014
-
highly glycosylated enzyme
-
glycoprotein
-
PencillopepsinJT2, glycosylated form of the active enzyme
glycoprotein
-
PencillopepsinJT2, glycosylated form of the active enzyme
-
glycoprotein
-
2 mol glucose equivalent and 1 mol glucosamine equivalent per mol proteinase
proteolytic modification
autoprocessing of the zymogen
proteolytic modification
autoprocessing of the zymogen releasing the propeptide Val(Asn)4-Lys
proteolytic modification
autoprocessing of the zymogen releasing the propeptide Val(Asn)4-Lys-OH
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure in complex with inhibitor PPi3, monoclinic space group C2, a : 96.24 A, b : 46.47 A, c : 65.38 A, crystal structure in complex with inhibitor PPi4, monoclinic space group C2, a : 96.98 A, b : 46.65 A, c : 65.71 A
crystal structure of native penicillopepsin and of its complex with a synthetic analogue of the inhibitor pepstatin at 1.8 A resolution
-
crystallographic analysis of transition state mimics bound to penicillopepsin
-
purified penicillopepsin-JT1, free or bound to difluorostatine- and difluorostatone-containing peptides, X-ray diffraction structure determination and analysis at 0.95-2.8 A resolution
cocrystallized with inhibitor 1-L, space group C2, cell dimensions a 0 97.88 A, b = 46.64 A, c = 66.59 A
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
T219A
T219G
T219S
T219V
T219A
site-directed mutagenesis, comparison of substrate binding to the wild-type enzyme
T219G
site-directed mutagenesis, comparison of substrate binding to the wild-type enzyme
T219S
site-directed mutagenesis, comparison of substrate binding to the wild-type enzyme
T219V
site-directed mutagenesis, comparison of substrate binding to the wild-type enzyme
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2.5
Penicillium duponti
-
65°C, complete loss of activity after 15 min, 60°C, complete loss of activity after 60 min
30586
2.5 - 6
Penicillium duponti
-
30°C, 20 h, stable
30595
2.5 - 6.5
Penicillium duponti
-
30°C, 24 h, stable
30586
3 - 7
-
the enzyme maintains more than 70% activity after incubation for 24 h at pH 3.0-7.0 25°C
752532
3.5 - 5.5
Penicillium duponti
-
60°C, 1 h, stable
30586, 30595
4.5
6 - 11
-
the purified enzyme does not lose any activity after 24 h at pH 6.0-11.0
755308
8 - 9
Penicillium candidum
-
the enzyme retains less than 35% activity after 1 h at pH 8.0-9.0
753904
4.5
Penicillium duponti
-
at 65°C, stable for 15 min, at 60°C, stable for 60 min
30586
4.5
Penicillium duponti
-
70°C, 1 h, more than 65% of the activity is retained
30595
4.5
Penicillium duponti
-
80°C, 10 min, complete inactivation
30595
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 45
-
the purified enzyme does not lose any activity over 48 h at 25°C. The protease shows an activity loss of 77.56% at 45°C after 12 h
30
30 - 50
-
the enzyme remains stable after 80 min incubation at 30-50°C (pH 5.0). The activity drops to less than 20% after 80 min at 60°C. The enzyme shows about 75% activity after 2 h at 50°C
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
aqueous two-phase system system using 9% (w/v) PEG 8000, 5.2% (w/v) NaCl, and 15.9% (w/v) sodium citrate
Penicillium candidum
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene pepA, nucleotide sequence determined, inserted into expression vector pGPT-pyrG1, expressed in an aspartic proteinase-free strain of Aspergillus niger var. awamori
-
penicillopepsin-JT1, DNA and amino acid sequence determination and analysis
penicillopepsin-JT2, DNA and amino acid sequence determination and analysis
penicillopepsin-JT3, DNA and amino acid sequence determination and analysis
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
food industry
medicine
design of inhibitors with enhanced potency against proteolytic enzymes has many applications for treatment of human diseases
food industry
Penicillium candidum
-
the enzyme is used in the dairy industry such as in accelerated cheese ripening
food industry
Penicillium candidum PCA 1/TT031
-
the enzyme is used in the dairy industry such as in accelerated cheese ripening
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hofmann, T.
Penicillopepsin
Methods Enzymol.
45
434-452
1976
Penicillium janthinellum
brenda
Emi, S.; Myers, D.V.; Iacobucci, G.A.
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
266
140-145
1977
Penicillium janthinellum
brenda
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
1140-1146
1988
Penicillium janthinellum
brenda
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
Biochem. J.
237
899-906
1986
Penicillium janthinellum
brenda
James, M.N.G.; Hsu, I.N.; Delbaere, L.T.J.
Mechanism of acid protease catalysis based on the crystal structure of penicillopepsin
Nature
267
808-813
1977
Penicillium janthinellum
brenda
Mains, G.; Hofmann, T.
The inactivation of penicillopepsin with 1,2-epoxy-3-(p-nitrophenoxy) propane, an active-site directed reagent
Can. J. Biochem.
52
1018-1023
1974
Penicillium janthinellum
brenda
Wang, T.T.; Hofmann, T.
Acyl and amino intermediates in penicillopepsin-catalysed reactions and activation by nonsubstrate peptides
Can. J. Biochem.
55
286-294
1977
Penicillium janthinellum
brenda
Hsu, I.N.; Hofman, T.; Nyburg, S.C.
The crystal structure of penicillopesin at 6 A resolution
Biochem. Biophys. Res. Commun.
72
363-368
1976
Penicillium janthinellum
brenda
Mabrouk, S.S.; Amr, A.S.; Abdel-Fattah, A.F.
A rennin-like enzyme from Penicillium expansum
Agric. Biol. Chem.
40
419-420
1976
Penicillium expansum
-
brenda
Hashimoto, H.; Iwaasa, T.; Yokotsuka, T.
Some properties of acid protease from the thermophilic fungus, Penicillium duponti K1014
Appl. Microbiol.
25
578-583
1973
Penicillium duponti, Penicillium duponti K 1014
brenda
Hashimoto, H.; Kaneko, Y.; Iwaasa, T.; Yokotsuka, T.
Production and purification of acid protease from the thermophilic fungus, Penicillium duponti K1014
Appl. Microbiol.
25
584-588
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
1044-1046
1985
Penicillium janthinellum
brenda
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
635-643
1984
Penicillium janthinellum
brenda
James, M.N.G.; Sielecki, A.R.
Structure and refinement of penicillopepsin at 1.8 A resolution
J. Mol. Biol.
163
299-361
1983
Penicillium janthinellum
brenda
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
5201-5214
1992
Penicillium janthinellum
brenda
Houmard, J.; Raymond, M.N.
Further characterization of the Penicillium roqueforti acid protease
Biochimie
61
979-982
1979
Penicillium roqueforti
brenda
Gripon, J.C.
Inactivation of Penicillium roqueforti acid protease by specific pepsin inhibitors
Biochimie
58
747-749
1976
Penicillium roqueforti
brenda
Fraser, M.E.; Meyer, J.H.; Bartlett, P.A.; James, M.N.
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.
brenda
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)
brenda
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)
Protein Sci.
9
991-1001
2000
Penicillium janthinellum, Penicillium janthinellum NRRL 905
brenda
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
-
brenda
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
brenda
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
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