Proteinase K
Proteinase K | ||
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Existing structural data: s. UniProt entry |
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Cofactor | 2 Ca 2+ | |
Identifier | ||
External IDs |
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Enzyme classification | ||
EC, category | 3.4.21.64 , serine protease | |
MEROPS | S08.054 | |
Response type | proteolytic cleavage | |
Substrate | Keratin, peptide amides | |
Occurrence | ||
Parent taxon | Engyodontium album |
safety instructions | ||||||||
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CAS number |
39450-01-6 |
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Proteinase K is a proteinase from the hose fungi Engyodontium album (previously called Tritirachium album ) and Acremonium strictum , which belongs to the family of subtilisin- like serine proteases . The enzyme attacks peptide bonds both at the ends ( exopeptidase ) and inside ( endopeptidase ) of the proteins. Proteinase K is used to break down proteins in cell lysates and to release nucleic acids .
Application examples
- Isolation of genomic DNA from bacteria
- Isolation of DNA from cells or tissue for the polymerase chain reaction (PCR)
Individual evidence
- ↑ a b c data sheet Proteinase K from Tritirachium album at Sigma-Aldrich , accessed on July 29, 2017 ( PDF ).
- ↑ Engyodontium album (Tritirachium album). In: uniprot.org. Retrieved August 4, 2015 .
- ↑ UniProtKB - R4IR27 (ASES_SARSR) . In: UniProt . Retrieved September 3, 2019.