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Literature summary for 3.4.21.64 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.
    View publication on PubMedView publication on EuropePMC
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Application

Application Comment Organism
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

Organism UniProt Comment Textmining
Parengyodontium album P06873
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 ?
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 ?
prion protein + H2O specific cleavage, that does not occur at cross-linker-modified residues Parengyodontium album ?
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 ?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Parengyodontium album

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8 8.5 assay at Parengyodontium album

General Information

General Information Comment Organism
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