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Information on EC 3.4.23.20 - Penicillopepsin and Organism(s) Penicillium janthinellum and UniProt Accession P78735
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3.4.23.20 PenicillopepsinSpecify your search results
Word Map
The taxonomic range for the selected organisms is: Penicillium janthinellum
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected 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, penicillopepsin-jt1, penicillium janthinellum acid proteinase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Acid protease A
-
-
-
-
Penicillium citrinum acid proteinase
-
-
-
-
Penicillium cyclopium acid proteinase
-
-
-
-
Penicillium expansum acid proteinase
-
-
-
-
Penicillium janthinellum acid proteinase
-
-
-
-
Penicillium janthinellum aspartic proteinase
Penicillium roqueforti acid proteinase
-
-
-
-
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
CAS REGISTRY NUMBER
COMMENTARY
9074-08-2
-
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
Ac-(Ala)n-Lys-Nph-(Ala)m-amide + H2O
Ac-(Ala)n-Lys + Nph-(Ala)m-amide
-
-
-
?
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
-
-
?
Pro-Thr-Glu-Phe-(4-nitro)Phe-Arg-Leu + H2O
Pro-Thr-Glu-Phe + (4-nitro)Phe-Arg-Leu
-
-
-
?
trypsinogen + H2O
trypsin + propeptide Val(Asn)4-Lys-OH
substrate from Bos taurus, rapid activation
-
-
?
Trypsinogen + H2O
?
-
bovine, activation by cleavage of Lys6-Ile7
-
-
?
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
?
-
-
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
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Diazoacetyl-DL-norleucine methyl ester
i.e. DAN, active-site directed inhibitor
Leu-Gly-Leu
-
inhibits trypsinogen activation, activates cleavage of Leu-Tyr amide
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
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
-
investigation of the protonation state penicillopepsin in complex with phosphinate and phosphonate inhibitors
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Leu-Gly-Leu
-
inhibits trypsinogen activation, activates cleavage of Leu-Tyr amide
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
-
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
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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). PEPA2_PENJA
394
0
40840
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
amino acid sequence from Penicillium janthinellum enzyme
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
three-dimensional structure and comparison
additional information
three-dimensional structure and comparison
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
autoprocessing of the zymogen releasing the propeptide Val(Asn)4-Lys
glycoprotein
-
PencillopepsinJT2, glycosylated form of the active enzyme
proteolytic modification
proteolytic modification
autoprocessing of the zymogen
proteolytic modification
autoprocessing of the zymogen releasing the propeptide Val(Asn)4-Lys-OH
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
penicillopepsin-JT2, DNA and amino acid sequence determination and analysis
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-JT3, DNA and amino acid sequence determination and analysis
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
design of inhibitors with enhanced potency against proteolytic enzymes has many applications for treatment of human diseases
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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
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
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
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
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
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
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
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
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
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
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
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
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)
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
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 duponti K1014, Penicillium janthinellum, Penicillium janthinellum (P78735), Penicillium janthinellum (Q9HEZ3), Penicillium roqueforti
-
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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