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Literature summary for 3.4.23.20 extracted from
- Penicillopepsin (2004), Handbook of Proteolytic Enzymes (Barrett, J. ; Rawlings, N. D. ; Woessner, J. F. , eds. ), 1, 99-104.
No PubMed abstract available
Cloned(Commentary)
| Cloned (Comment) | 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)
| Crystallization (Comment) | 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 |
Protein Variants
| Protein Variants | Comment | 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 | Comment | 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 | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | substrate binding subsite kinetics | Penicillium janthinellum |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | 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 | UniProt | Comment | Textmining |
|---|---|---|---|
| Penicillium camemberti | - |
- |
- |
| Penicillium duponti | - |
thermophilic fungus | - |
| Penicillium duponti K1014 | - |
thermophilic fungus | - |
| Penicillium janthinellum | - |
isozymes penicillopepsin-JT1 and penicillopepsin-JT3 | - |
| Penicillium janthinellum | P78735 | precursor; penicillopepsin-JT2 | - |
| Penicillium janthinellum | Q9HEZ3 | precursor; penicillopepsin-JT3 | - |
| Penicillium roqueforti | - |
- |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| glycoprotein | - |
Penicillium janthinellum |
| glycoprotein | highly glycosylated enzyme | Penicillium duponti |
| proteolytic modification | autoprocessing of the zymogen | Penicillium janthinellum |
| proteolytic modification | autoprocessing of the zymogen releasing the propeptide Val(Asn)4-Lys | Penicillium janthinellum |
| proteolytic modification | autoprocessing of the zymogen releasing the propeptide Val(Asn)4-Lys-OH | Penicillium janthinellum |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Penicillium duponti |
- |
Penicillium roqueforti |
- |
Penicillium camemberti |
| penicillopepsin-JT1 to homogeneity | Penicillium janthinellum |
| penicillopepsin-JT2 | Penicillium janthinellum |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| Ac-(Ala)n-Lys-Nph-(Ala)m-amide + H2O | - |
Penicillium janthinellum | Ac-(Ala)n-Lys + Nph-(Ala)m-amide | - |
? | |
| FVNQHLCGSHLVEALYLVCGERGFFYTPKA + H2O | i.e. insulin B chain, cleavage site specificity | Penicillium janthinellum | FVNQHLCGSHLVEALYLVCG + ERGFFYTPKA | - |
? | |
| additional information | broad protein substrate specificity | Penicillium duponti | ? | - |
? | |
| additional information | broad protein substrate specificity | Penicillium roqueforti | ? | - |
? | |
| additional information | broad protein substrate specificity | 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 | Penicillium janthinellum | ? | - |
? | |
| additional information | substrate binding specificity, cleavage site specificity, overview | Penicillium janthinellum | ? | - |
? | |
| additional information | broad protein substrate specificity | Penicillium duponti K1014 | ? | - |
? | |
| trypsin inhibitor + H2O | substrate from Cucurbita maxima, specific cleavage of Leu7-Met8 bond at pH 3.3 | Penicillium camemberti | trypsin inhibitor fragments | - |
? | |
| trypsinogen + H2O | substrate from Bos taurus, rapid activation | Penicillium janthinellum | trypsin + propeptide Val(Asn)4-Lys-OH | - |
? | |
| trypsinogen + H2O | rapid activation | Penicillium duponti | trypsin + Val(Asn)4-Lys | - |
? | |
| trypsinogen + H2O | rapid activation | Penicillium roqueforti | trypsin + Val(Asn)4-Lys | - |
? | |
| trypsinogen + H2O | rapid activation | Penicillium camemberti | trypsin + Val(Asn)4-Lys | - |
? | |
| trypsinogen + H2O | rapid activation | Penicillium duponti K1014 | trypsin + Val(Asn)4-Lys | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 33400 | Penicillium roqueforti |
| ? | x * 33422, amino acid sequence calculation | Penicillium janthinellum |
| ? | x * 33500 | Penicillium camemberti |
| ? | x * 33800 | Penicillium janthinellum |
| ? | x * 41590 | Penicillium duponti |
| More | three-dimensional structure and comparison | Penicillium janthinellum |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| mold kinase | - |
Penicillium janthinellum |
| More | the enzyme belongs to the A1 peptidase family | Penicillium janthinellum |
| penicillium kinase | - |
Penicillium janthinellum |
| penicillopepsin-JT1 | - |
Penicillium janthinellum |
| penicillopepsin-JT2 | - |
Penicillium janthinellum |
| penicillopepsin-JT3 | - |
Penicillium janthinellum |
| Peptidase A | - |
Penicillium janthinellum |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 420 | - |
Trypsinogen | - |
Penicillium janthinellum | |
pI Value
| Organism | Comment | pI Value Maximum | pI Value |
|---|---|---|---|
| Penicillium janthinellum | below, penicillopepsin-JT1 | - |
3 |
| Penicillium duponti | - |
- |
3.3 |
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Release 2023.1 (January 2023)
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