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Literature summary for 3.4.21.64 extracted from
- Molecular investigation on the interaction of spermine with proteinase K by multispectroscopic techniques and molecular simulation studies (2017), Int. J. Biol. Macromol., 94, 406-414 .
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| spermine | interaction of proteinase K with spermine, multispectroscopic study and molecular simulation, structure-function analysis, overview. The stability and enzyme activity of proteinase K-spermine complex are significantly enhanced as compared to the pure enzyme, secondary structure alteration of proteinase K with an increase in alpha-helicity and a decrease in beta-sheet of proteinase K upon spermine conjugation. Spermine interacts with proteinase K spontaneously at single binding site | Parengyodontium album |  |
General Stability
| General Stability | Organism |
|---|---|
| interaction of proteinase K with spermine, multispectroscopic study and molecular simulation, structure-function analysis, overview. The stability and enzyme activity of proteinase K-spermine complex are significantly enhanced as compared to the pure enzyme, secondary structure alteration of proteinase K with an increase in alpha-helicity and a decrease in beta-sheet of proteinase K upon spermine conjugation | Parengyodontium album |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | kinetics and thermodynamics | Parengyodontium album |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Parengyodontium album | P06873 | i.e. Tritirachium album or Engyodontium album | - |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| commercial preparation | - |
Parengyodontium album | - |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| monomer | proteinase K is a monomeric and globular protein with 279 amino acid residues | Parengyodontium album |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Proteinase K | - |
Parengyodontium album |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 35 | - |
assay at | Parengyodontium album |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8 | - |
assay at | Parengyodontium album |
General Information
| General Information | Comment | Organism |
|---|---|---|
| additional information | the catalytic triad and oxyanion hole of proteinase K are formed by Asp39, His69 and Ser224, and Asn161, respectively. Furthermore, two segments Asn99-Tyr104 and Ser132-Gly136 form substrate recognition site of proteinase K. Spermine quenches the intensity of proteinase K with static mechanism. Molecular docking using structure PDB ID 2ID8 | Parengyodontium album |
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Release 2023.1 (January 2023)
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