Literature summary extracted from
Petrotchenko, E.V.; Serpa, J.J.; Hardie, D.B.; Berjanskii, M.; Suriyamongkol, B.P.; Wishart, D.S.; Borchers, C.H.
Use of proteinase K nonspecific digestion for selective and comprehensive identification of interpeptide cross-links: application to prion proteins (2012), Mol. Cell. Proteomics, 11, M111.013524.
Application
EC Number |
Application |
Comment |
Organism |
---|
3.4.21.64 |
analysis |
nonspecific protease proteinase K can be used as an alternative to trypsin for cross-linking studies, digestion by proteinase K results in a family of related cross-linked peptides, all of which contained the same cross-linking sites, thus providing additional verification of the cross-linking results. Using proteinase K, the affinity-purifiable CID-cleavable and isotopically coded cross-linker cyanurbiotindipropionylsuccinimide and MALDI-MS cross-links are found for all of the possible cross-linking sites of native and oligomeric forms of prion protein substrates, overview. After digestion with proteinase K, the mass distribution of the crosslinked peptides is very suitable for MALDI-MS analysis |
Parengyodontium album |
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
3.4.21.64 |
Parengyodontium album |
P06873 |
- |
- |
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
3.4.21.64 |
additional information |
substrate synthesis: a synthetic gene corresponding to the Syrian hamster prion protein sequence 90-232 with a 23-residue N-terminal fusion tag containing His6 and a thrombin cleavage site (MGSSHHHHHHSSGLVPRGSHMLE) is specifically synthesized and expressedas substrate for the enzyme |
Parengyodontium album |
? |
- |
? |
|
3.4.21.64 |
prion protein + H2O |
specific cleavage, that does not occur at cross-linker-modified residues |
Parengyodontium album |
? |
- |
? |
|
Temperature Optimum [°C]
EC Number |
Temperature Optimum [°C] |
Temperature Optimum Maximum [°C] |
Comment |
Organism |
---|
3.4.21.64 |
37 |
- |
assay at |
Parengyodontium album |
pH Optimum
EC Number |
pH Optimum Minimum |
pH Optimum Maximum |
Comment |
Organism |
---|
3.4.21.64 |
8 |
8.5 |
assay at |
Parengyodontium album |
General Information
EC Number |
General Information |
Comment |
Organism |
---|
3.4.21.64 |
additional information |
nonspecific protease proteinase K can be used as an alternative to trypsin for cross-linking studies, digestion by proteinase K results in a family of related cross-linked peptides, all of which contained the same cross-linking sites, thus providing additional verification of the cross-linking results. Using proteinase K, the affinity-purifiable CID-cleavable and isotopically coded cross-linker cyanurbiotindipropionylsuccinimide and MALDI-MS cross-links are found for all of the possible cross-linking sites of native and oligomeric forms of prion protein substrates, overview. After digestion with proteinase K, the mass distribution of the crosslinked peptides is very suitable for MALDI-MS analysis, detailed overview of cross-links in prion proteins |
Parengyodontium album |