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Literature summary for 3.4.24.39 extracted from
- Deuterolysin (2004), Handbook of Proteolytic Enzymes(Barrett,A. J. ,Rawlings,N. D. ,Woessner,J. F. ,Eds. )Academic Press, 1, 786-788.
No PubMed abstract available
Application
| Application | Comment | Organism |
|---|---|---|
| additional information | likely enables organisms to utilize substrates in their environment | Aspergillus sojae |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| recombinant NpII-O expressed from Saccharomyces cerevisiae as a secreted form and from Escherichia coli as a pro-NpII-O in the cells | Aspergillus sojae |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | mutant NpII-O forms | Aspergillus sojae |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| EDTA | only effective at acidic pH, reactivation by Zn2+, Co2+ and Mn2+ | Aspergillus sojae |  |
| metal chelator | - |
Aspergillus sojae | |
| additional information | not inhibited by DFP, sulfhydryl reagents, DAN and phosphoramidon | Aspergillus sojae |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Zn2+ | required for activity | Aspergillus sojae | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 19020 | - |
sequence analysis | Aspergillus sojae |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Aspergillus fumigatus | - |
- |
- |
| Aspergillus sojae | - |
- |
- |
| Penicillium camemberti | - |
- |
- |
| Penicillium roqueforti | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| to homogeneity | Aspergillus sojae |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| Albumin + H2O | low activity of the enzyme | Aspergillus sojae | ? | - |
? | |
| casein + H2O | low activity of the enzyme | Aspergillus sojae | ? | - |
? | |
| Gelatin + H2O | low activity of the enzyme | Aspergillus sojae | ? | - |
? | |
| Hemoglobin + H2O | low activity of the enzyme | Aspergillus sojae | ? | - |
? | |
| histone + H2O | high activity of the enzyme | Aspergillus sojae | ? | - |
? | |
| additional information | no cleavage of any disubstituted dipeptides | Aspergillus sojae | ? | - |
? | |
| Oxidized insulin B-chain + H2O | - |
Aspergillus sojae | ? | - |
? | |
| protamine + H2O | high activity of the enzyme | Aspergillus sojae | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| monomer | - |
Aspergillus sojae |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Neutral proteinase II | - |
Penicillium roqueforti |
| Neutral proteinase II | - |
Aspergillus sojae |
| Neutral proteinase II | - |
Aspergillus fumigatus |
| Neutral proteinase II | - |
Penicillium camemberti |
| NPII | - |
Penicillium roqueforti |
| NPII | - |
Aspergillus sojae |
| NPII | - |
Aspergillus fumigatus |
| NPII | - |
Penicillium camemberti |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 70 | 100 | most unstable after 10 min at ca. 65-75°C, but regains stability beyond this temperature | Aspergillus sojae |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 5.5 | 6 | on casein | Aspergillus sojae |
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Release 2023.1 (January 2023)
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