BRENDA - Enzyme Database show
show all sequences of 3.4.23.20

Penicillopepsin

Hofmann, T.; Handbook of Proteolytic Enzymes (Barrett, J. ; Rawlings, N. D. ; Woessner, J. F. , eds. ) 1, 99-104 (2004)
No PubMed abstract available

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
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
Penicillium janthinellum
Crystallization (Commentary)
Crystallization
Organism
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
Penicillium janthinellum
Engineering
Amino acid exchange
Commentary
Organism
T219A
site-directed mutagenesis, comparison of substrate binding to the wild-type enzyme
Penicillium janthinellum
T219G
site-directed mutagenesis, comparison of substrate binding to the wild-type enzyme
Penicillium janthinellum
T219S
site-directed mutagenesis, comparison of substrate binding to the wild-type enzyme
Penicillium janthinellum
T219V
site-directed mutagenesis, comparison of substrate binding to the wild-type enzyme
Penicillium janthinellum
Inhibitors
Inhibitors
Commentary
Organism
Structure
Diazoacetyl-DL-norleucine methyl ester
i.e. DAN, active-site directed inhibitor
Penicillium camemberti
Diazoacetyl-DL-norleucine methyl ester
i.e. DAN, active-site directed inhibitor, inactivation, also by related compounds
Penicillium duponti
Diazoacetyl-DL-norleucine methyl ester
i.e. DAN, active-site directed inhibitor
Penicillium janthinellum
isovaleryl-Val-statine-ethoxy
pepstatin analogue
Penicillium janthinellum
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
substrate binding subsite kinetics
Penicillium janthinellum
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
33400
-
x * 33400
Penicillium roqueforti
33422
-
x * 33422, amino acid sequence calculation
Penicillium janthinellum
33500
-
x * 33500
Penicillium camemberti
33800
-
x * 33800
Penicillium janthinellum
41590
-
x * 41590
Penicillium duponti
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Penicillium camemberti
-
-
-
Penicillium duponti
-
thermophilic fungus
-
Penicillium duponti K1014
-
thermophilic fungus
-
Penicillium janthinellum
P78735
precursor; penicillopepsin-JT2
-
Penicillium janthinellum
-
isozymes penicillopepsin-JT1 and penicillopepsin-JT3
-
Penicillium janthinellum
Q9HEZ3
precursor; penicillopepsin-JT3
-
Penicillium roqueforti
-
-
-
Posttranslational Modification
Posttranslational Modification
Commentary
Organism
glycoprotein
highly glycosylated enzyme
Penicillium duponti
glycoprotein
-
Penicillium janthinellum
proteolytic modification
autoprocessing of the zymogen; autoprocessing of the zymogen releasing the propeptide Val(Asn)4-Lys; autoprocessing of the zymogen releasing the propeptide Val(Asn)4-Lys-OH
Penicillium janthinellum
Purification (Commentary)
Commentary
Organism
-
Penicillium camemberti
-
Penicillium duponti
-
Penicillium roqueforti
penicillopepsin-JT1 to homogeneity; penicillopepsin-JT2
Penicillium janthinellum
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Ac-(Ala)n-Lys-Nph-(Ala)m-amide + H2O
-
668813
Penicillium janthinellum
Ac-(Ala)n-Lys + Nph-(Ala)m-amide
-
-
-
?
FVNQHLCGSHLVEALYLVCGERGFFYTPKA + H2O
i.e. insulin B chain, cleavage site specificity
668813
Penicillium janthinellum
FVNQHLCGSHLVEALYLVCG + ERGFFYTPKA
-
-
-
?
additional information
broad protein substrate specificity
668813
Penicillium duponti
?
-
-
-
-
additional information
broad protein substrate specificity
668813
Penicillium roqueforti
?
-
-
-
-
additional information
broad protein substrate specificity
668813
Penicillium camemberti
?
-
-
-
-
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
668813
Penicillium janthinellum
?
-
-
-
-
additional information
substrate binding specificity, cleavage site specificity, overview
668813
Penicillium janthinellum
?
-
-
-
-
additional information
broad protein substrate specificity
668813
Penicillium duponti K1014
?
-
-
-
-
trypsin inhibitor + H2O
substrate from Cucurbita maxima, specific cleavage of Leu7-Met8 bond at pH 3.3
668813
Penicillium camemberti
trypsin inhibitor fragments
-
-
-
?
trypsinogen + H2O
substrate from Bos taurus, rapid activation
668813
Penicillium janthinellum
trypsin + propeptide Val(Asn)4-Lys-OH
-
-
-
?
trypsinogen + H2O
rapid activation
668813
Penicillium duponti
trypsin + Val(Asn)4-Lys
-
-
-
?
trypsinogen + H2O
rapid activation
668813
Penicillium roqueforti
trypsin + Val(Asn)4-Lys
-
-
-
?
trypsinogen + H2O
rapid activation
668813
Penicillium camemberti
trypsin + Val(Asn)4-Lys
-
-
-
?
trypsinogen + H2O
rapid activation
668813
Penicillium duponti K1014
trypsin + Val(Asn)4-Lys
-
-
-
?
Subunits
Subunits
Commentary
Organism
?
x * 33500
Penicillium camemberti
?
x * 41590
Penicillium duponti
?
x * 33422, amino acid sequence calculation; x * 33800
Penicillium janthinellum
?
x * 33400
Penicillium roqueforti
More
three-dimensional structure and comparison
Penicillium janthinellum
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
420
-
Trypsinogen
-
Penicillium janthinellum
pI Value
Organism
Commentary
pI Value Maximum
pI Value
Penicillium janthinellum
below, penicillopepsin-JT1
-
3
Penicillium duponti
-
-
3.3
Cloned(Commentary) (protein specific)
Commentary
Organism
penicillopepsin-JT1, DNA and amino acid sequence determination and analysis
Penicillium janthinellum
penicillopepsin-JT2, DNA and amino acid sequence determination and analysis
Penicillium janthinellum
penicillopepsin-JT3, DNA and amino acid sequence determination and analysis
Penicillium janthinellum
Crystallization (Commentary) (protein specific)
Crystallization
Organism
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
Penicillium janthinellum
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
T219A
site-directed mutagenesis, comparison of substrate binding to the wild-type enzyme
Penicillium janthinellum
T219G
site-directed mutagenesis, comparison of substrate binding to the wild-type enzyme
Penicillium janthinellum
T219S
site-directed mutagenesis, comparison of substrate binding to the wild-type enzyme
Penicillium janthinellum
T219V
site-directed mutagenesis, comparison of substrate binding to the wild-type enzyme
Penicillium janthinellum
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
Diazoacetyl-DL-norleucine methyl ester
i.e. DAN, active-site directed inhibitor
Penicillium camemberti
Diazoacetyl-DL-norleucine methyl ester
i.e. DAN, active-site directed inhibitor, inactivation, also by related compounds
Penicillium duponti
Diazoacetyl-DL-norleucine methyl ester
i.e. DAN, active-site directed inhibitor
Penicillium janthinellum
isovaleryl-Val-statine-ethoxy
pepstatin analogue
Penicillium janthinellum
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
substrate binding subsite kinetics
Penicillium janthinellum
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
33400
-
x * 33400
Penicillium roqueforti
33422
-
x * 33422, amino acid sequence calculation
Penicillium janthinellum
33500
-
x * 33500
Penicillium camemberti
33800
-
x * 33800
Penicillium janthinellum
41590
-
x * 41590
Penicillium duponti
Posttranslational Modification (protein specific)
Posttranslational Modification
Commentary
Organism
glycoprotein
highly glycosylated enzyme
Penicillium duponti
glycoprotein
-
Penicillium janthinellum
proteolytic modification
autoprocessing of the zymogen releasing the propeptide Val(Asn)4-Lys-OH
Penicillium janthinellum
proteolytic modification
autoprocessing of the zymogen releasing the propeptide Val(Asn)4-Lys
Penicillium janthinellum
proteolytic modification
autoprocessing of the zymogen
Penicillium janthinellum
Purification (Commentary) (protein specific)
Commentary
Organism
-
Penicillium camemberti
-
Penicillium duponti
-
Penicillium roqueforti
penicillopepsin-JT1 to homogeneity
Penicillium janthinellum
penicillopepsin-JT2
Penicillium janthinellum
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Ac-(Ala)n-Lys-Nph-(Ala)m-amide + H2O
-
668813
Penicillium janthinellum
Ac-(Ala)n-Lys + Nph-(Ala)m-amide
-
-
-
?
FVNQHLCGSHLVEALYLVCGERGFFYTPKA + H2O
i.e. insulin B chain, cleavage site specificity
668813
Penicillium janthinellum
FVNQHLCGSHLVEALYLVCG + ERGFFYTPKA
-
-
-
?
additional information
broad protein substrate specificity
668813
Penicillium duponti
?
-
-
-
-
additional information
broad protein substrate specificity
668813
Penicillium roqueforti
?
-
-
-
-
additional information
broad protein substrate specificity
668813
Penicillium camemberti
?
-
-
-
-
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
668813
Penicillium janthinellum
?
-
-
-
-
additional information
substrate binding specificity, cleavage site specificity, overview
668813
Penicillium janthinellum
?
-
-
-
-
additional information
broad protein substrate specificity
668813
Penicillium duponti K1014
?
-
-
-
-
trypsin inhibitor + H2O
substrate from Cucurbita maxima, specific cleavage of Leu7-Met8 bond at pH 3.3
668813
Penicillium camemberti
trypsin inhibitor fragments
-
-
-
?
trypsinogen + H2O
substrate from Bos taurus, rapid activation
668813
Penicillium janthinellum
trypsin + propeptide Val(Asn)4-Lys-OH
-
-
-
?
trypsinogen + H2O
rapid activation
668813
Penicillium duponti
trypsin + Val(Asn)4-Lys
-
-
-
?
trypsinogen + H2O
rapid activation
668813
Penicillium roqueforti
trypsin + Val(Asn)4-Lys
-
-
-
?
trypsinogen + H2O
rapid activation
668813
Penicillium camemberti
trypsin + Val(Asn)4-Lys
-
-
-
?
trypsinogen + H2O
rapid activation
668813
Penicillium duponti K1014
trypsin + Val(Asn)4-Lys
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 33500
Penicillium camemberti
?
x * 41590
Penicillium duponti
?
x * 33422, amino acid sequence calculation
Penicillium janthinellum
?
x * 33800
Penicillium janthinellum
?
x * 33400
Penicillium roqueforti
More
three-dimensional structure and comparison
Penicillium janthinellum
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
420
-
Trypsinogen
-
Penicillium janthinellum
pI Value (protein specific)
Organism
Commentary
pI Value Maximum
pI Value
Penicillium janthinellum
below, penicillopepsin-JT1
-
3
Penicillium duponti
-
-
3.3
Other publictions for EC 3.4.23.20
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
670005
Vidossich
Binding of phosphinate and pho ...
Penicillium janthinellum
J. Phys. Chem. B
110
1437-1442
2006
-
-
-
-
-
-
2
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
668813
Hofmann
-
Penicillopepsin ...
Penicillium camemberti, Penicillium duponti, Penicillium duponti K1014, Penicillium janthinellum, Penicillium roqueforti
Handbook of Proteolytic Enzymes (Barrett, J. ; Rawlings, N. D. ; Woessner, J. F. , eds. )
1
99-104
2004
-
-
1
1
4
-
4
1
-
-
5
-
-
7
-
3
4
-
-
-
-
-
16
5
-
-
-
1
-
-
-
-
-
2
-
-
-
3
-
1
4
-
-
4
-
1
-
-
5
-
-
-
5
5
-
-
-
-
16
6
-
-
-
1
-
-
-
2
-
-
-
-
-
-
653829
Cao
Penicillopepsin-JT2, a recombi ...
Penicillium janthinellum, Penicillium janthinellum NRRL 905
Protein Sci.
9
991-1001
2000
-
-
1
-
4
-
1
47
-
-
1
-
-
5
-
1
1
-
-
-
-
-
15
-
-
-
-
47
-
-
-
-
5
-
-
-
-
1
-
-
4
-
-
1
5
47
-
-
1
-
-
-
1
1
-
-
-
-
15
-
-
-
-
47
-
-
-
-
-
-
-
-
-
-
649272
Fraser
Overcoming the unfavourable en ...
Penicillium sp.
Adv. Exp. Med. Biol.
436
355-359
1998
-
-
-
1
-
-
3
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
1
-
-
-
3
3
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
649841
Khan
Lowering the entropic barrier ...
Penicillium janthinellum
Biochemistry
37
16839-16845
1998
-
1
-
1
-
-
2
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
1
-
-
1
-
-
-
2
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
30601
James
Crystallographic analysis of t ...
Penicillium janthinellum
Biochemistry
31
3872-3886
1992
-
-
-
1
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
30602
Fraser
Crystallographic analysis of t ...
Penicillium janthinellum
Biochemistry
31
5201-5214
1992
-
-
-
1
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
30588
Hofmann
Effect of secondary substrate ...
Penicillium janthinellum
Biochemistry
27
1140-1146
1988
-
-
-
-
-
-
-
7
-
-
-
-
-
1
-
-
-
-
-
-
-
-
6
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
7
-
-
-
-
-
-
-
-
-
-
-
-
6
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
30589
Dunn
A systematic series of synthet ...
Penicillium janthinellum
Biochem. J.
237
899-906
1986
-
-
-
-
-
-
-
2
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
30597
Blum
Penicillopepsin, the aspartic ...
Penicillium janthinellum
Biochem. Soc. Trans.
13
1044-1046
1985
-
-
-
-
-
-
2
-
1
-
-
-
-
2
-
-
-
-
-
-
-
-
3
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
1
-
-
-
-
-
-
-
-
-
-
-
3
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
30598
James
Stereochemical analysis of pep ...
Penicillium janthinellum
Biochemistry
24
3701-3713
1985
-
-
-
1
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
30599
Hofmann
Effect of pH on the activities ...
Penicillium janthinellum
Biochemistry
23
635-643
1984
-
-
-
-
-
-
-
4
-
-
-
-
-
2
-
-
-
-
-
-
-
-
3
-
-
-
-
5
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
3
-
-
-
-
5
-
-
-
-
-
-
-
-
-
-
30600
James
Structure and refinement of pe ...
Penicillium janthinellum
J. Mol. Biol.
163
299-361
1983
-
-
-
1
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
30603
Houmard
Further characterization of th ...
Penicillium roqueforti
Biochimie
61
979-982
1979
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
30587
Hsu
Penicillopepsin from Penicilli ...
Penicillium janthinellum
Nature
266
140-145
1977
-
-
-
1
-
-
-
-
-
-
1
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
30590
James
Mechanism of acid protease cat ...
Penicillium janthinellum
Nature
267
808-813
1977
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
30592
Wang
Acyl and amino intermediates i ...
Penicillium janthinellum
Can. J. Biochem.
55
286-294
1977
-
-
-
-
-
-
1
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
30585
Hofmann
Penicillopepsin ...
Penicillium janthinellum
Methods Enzymol.
45
434-452
1976
1
-
-
-
-
-
9
1
1
-
2
-
-
1
-
-
1
-
-
-
1
1
4
-
-
-
2
1
3
-
4
-
-
-
-
1
-
-
-
-
-
-
-
9
-
1
1
-
2
-
-
-
-
1
-
-
1
1
4
-
-
-
2
1
3
-
4
-
-
-
-
-
-
-
30586
Emi
Purification and properties of ...
Penicillium duponti, Penicillium duponti K 1014
Biochemistry
15
842-848
1976
-
-
-
-
-
-
5
-
-
-
1
-
-
4
-
1
1
-
-
-
1
-
6
-
2
-
2
-
2
-
4
-
-
-
-
-
-
-
-
-
-
-
-
5
-
-
-
-
1
-
-
-
1
1
-
-
1
-
6
-
2
-
2
-
2
-
4
-
-
-
-
-
-
-
30593
Hsu
The crystal structure of penic ...
Penicillium janthinellum
Biochem. Biophys. Res. Commun.
72
363-368
1976
-
-
-
1
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
30594
Mabrouk
-
A rennin-like enzyme from Peni ...
Penicillium expansum
Agric. Biol. Chem.
40
419-420
1976
1
-
-
-
-
-
4
-
-
2
-
-
-
1
-
-
1
-
-
-
-
-
1
-
1
-
-
-
2
-
-
-
-
-
-
1
-
-
-
-
-
-
-
4
-
-
-
2
-
-
-
-
-
1
-
-
-
-
1
-
1
-
-
-
2
-
-
-
-
-
-
-
-
-
30604
Gripon
Inactivation of Penicillium ro ...
Penicillium roqueforti
Biochimie
58
747-749
1976
-
-
-
-
-
-
4
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
30591
Mains
The inactivation of penicillop ...
Penicillium janthinellum
Can. J. Biochem.
52
1018-1023
1974
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
30595
Hashimoto
Some properties of acid protea ...
Penicillium duponti, Penicillium duponti K 1014
Appl. Microbiol.
25
578-583
1973
1
-
-
-
-
-
4
-
-
-
1
-
-
4
-
-
-
-
-
-
-
-
2
-
3
-
4
-
1
-
3
-
-
-
-
1
-
-
-
-
-
-
-
4
-
-
-
-
1
-
-
-
-
-
-
-
-
-
2
-
3
-
4
-
1
-
3
-
-
-
-
-
-
-
30596
Hashimoto
Production and purification of ...
Penicillium duponti, Penicillium duponti K 1014
Appl. Microbiol.
25
584-588
1973
-
-
-
-
-
-
-
-
-
-
-
-
-
4
-
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-