Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

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

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.23.20 penicillopepsin-JT1, DNA and amino acid sequence determination and analysis Penicillium janthinellum
3.4.23.20 penicillopepsin-JT2, DNA and amino acid sequence determination and analysis Penicillium janthinellum
3.4.23.20 penicillopepsin-JT3, DNA and amino acid sequence determination and analysis Penicillium janthinellum

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.4.23.20 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

Protein Variants

EC Number Protein Variants Comment Organism
3.4.23.20 T219A site-directed mutagenesis, comparison of substrate binding to the wild-type enzyme Penicillium janthinellum
3.4.23.20 T219G site-directed mutagenesis, comparison of substrate binding to the wild-type enzyme Penicillium janthinellum
3.4.23.20 T219S site-directed mutagenesis, comparison of substrate binding to the wild-type enzyme Penicillium janthinellum
3.4.23.20 T219V site-directed mutagenesis, comparison of substrate binding to the wild-type enzyme Penicillium janthinellum

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.23.20 Diazoacetyl-DL-norleucine methyl ester i.e. DAN, active-site directed inhibitor Penicillium camemberti
3.4.23.20 Diazoacetyl-DL-norleucine methyl ester i.e. DAN, active-site directed inhibitor, inactivation, also by related compounds Penicillium duponti
3.4.23.20 Diazoacetyl-DL-norleucine methyl ester i.e. DAN, active-site directed inhibitor Penicillium janthinellum
3.4.23.20 isovaleryl-Val-statine-ethoxy pepstatin analogue Penicillium janthinellum

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.4.23.20 additional information
-
additional information substrate binding subsite kinetics Penicillium janthinellum

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.4.23.20 33400
-
x * 33400 Penicillium roqueforti
3.4.23.20 33422
-
x * 33422, amino acid sequence calculation Penicillium janthinellum
3.4.23.20 33500
-
x * 33500 Penicillium camemberti
3.4.23.20 33800
-
x * 33800 Penicillium janthinellum
3.4.23.20 41590
-
x * 41590 Penicillium duponti

Organism

EC Number Organism UniProt Comment Textmining
3.4.23.20 Penicillium camemberti
-
-
-
3.4.23.20 Penicillium duponti
-
thermophilic fungus
-
3.4.23.20 Penicillium duponti K1014
-
thermophilic fungus
-
3.4.23.20 Penicillium janthinellum
-
isozymes penicillopepsin-JT1 and penicillopepsin-JT3
-
3.4.23.20 Penicillium janthinellum P78735 precursor; penicillopepsin-JT2
-
3.4.23.20 Penicillium janthinellum Q9HEZ3 precursor; penicillopepsin-JT3
-
3.4.23.20 Penicillium roqueforti
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.4.23.20 glycoprotein
-
Penicillium janthinellum
3.4.23.20 glycoprotein highly glycosylated enzyme Penicillium duponti
3.4.23.20 proteolytic modification autoprocessing of the zymogen Penicillium janthinellum
3.4.23.20 proteolytic modification autoprocessing of the zymogen releasing the propeptide Val(Asn)4-Lys Penicillium janthinellum
3.4.23.20 proteolytic modification autoprocessing of the zymogen releasing the propeptide Val(Asn)4-Lys-OH Penicillium janthinellum

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.23.20
-
Penicillium duponti
3.4.23.20
-
Penicillium roqueforti
3.4.23.20
-
Penicillium camemberti
3.4.23.20 penicillopepsin-JT1 to homogeneity Penicillium janthinellum
3.4.23.20 penicillopepsin-JT2 Penicillium janthinellum

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.23.20 Ac-(Ala)n-Lys-Nph-(Ala)m-amide + H2O
-
Penicillium janthinellum Ac-(Ala)n-Lys + Nph-(Ala)m-amide
-
?
3.4.23.20 FVNQHLCGSHLVEALYLVCGERGFFYTPKA + H2O i.e. insulin B chain, cleavage site specificity Penicillium janthinellum FVNQHLCGSHLVEALYLVCG + ERGFFYTPKA
-
?
3.4.23.20 additional information broad protein substrate specificity Penicillium duponti ?
-
?
3.4.23.20 additional information broad protein substrate specificity Penicillium roqueforti ?
-
?
3.4.23.20 additional information broad protein substrate specificity Penicillium camemberti ?
-
?
3.4.23.20 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 Penicillium janthinellum ?
-
?
3.4.23.20 additional information substrate binding specificity, cleavage site specificity, overview Penicillium janthinellum ?
-
?
3.4.23.20 additional information broad protein substrate specificity Penicillium duponti K1014 ?
-
?
3.4.23.20 trypsin inhibitor + H2O substrate from Cucurbita maxima, specific cleavage of Leu7-Met8 bond at pH 3.3 Penicillium camemberti trypsin inhibitor fragments
-
?
3.4.23.20 trypsinogen + H2O substrate from Bos taurus, rapid activation Penicillium janthinellum trypsin + propeptide Val(Asn)4-Lys-OH
-
?
3.4.23.20 trypsinogen + H2O rapid activation Penicillium duponti trypsin + Val(Asn)4-Lys
-
?
3.4.23.20 trypsinogen + H2O rapid activation Penicillium roqueforti trypsin + Val(Asn)4-Lys
-
?
3.4.23.20 trypsinogen + H2O rapid activation Penicillium camemberti trypsin + Val(Asn)4-Lys
-
?
3.4.23.20 trypsinogen + H2O rapid activation Penicillium duponti K1014 trypsin + Val(Asn)4-Lys
-
?

Subunits

EC Number Subunits Comment Organism
3.4.23.20 ? x * 33400 Penicillium roqueforti
3.4.23.20 ? x * 33422, amino acid sequence calculation Penicillium janthinellum
3.4.23.20 ? x * 33500 Penicillium camemberti
3.4.23.20 ? x * 33800 Penicillium janthinellum
3.4.23.20 ? x * 41590 Penicillium duponti
3.4.23.20 More three-dimensional structure and comparison Penicillium janthinellum

Synonyms

EC Number Synonyms Comment Organism
3.4.23.20 mold kinase
-
Penicillium janthinellum
3.4.23.20 More the enzyme belongs to the A1 peptidase family Penicillium janthinellum
3.4.23.20 penicillium kinase
-
Penicillium janthinellum
3.4.23.20 penicillopepsin-JT1
-
Penicillium janthinellum
3.4.23.20 penicillopepsin-JT2
-
Penicillium janthinellum
3.4.23.20 penicillopepsin-JT3
-
Penicillium janthinellum
3.4.23.20 Peptidase A
-
Penicillium janthinellum

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.4.23.20 420
-
Trypsinogen
-
Penicillium janthinellum

pI Value

EC Number Organism Comment pI Value Maximum pI Value
3.4.23.20 Penicillium janthinellum below, penicillopepsin-JT1
-
3
3.4.23.20 Penicillium duponti
-
-
3.3