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