IUBMB Enzyme Nomenclature


Accepted name: peptidase K

Reaction: Hydrolysis of keratin, and of other proteins with subtilisin-like specificity. Hydrolyses peptide amides

Other names: Tritirachium alkaline proteinase; Tritirachium album serine proteinase; proteinase K; Tritirachium album proteinase K; endopeptidase K

Comments: From the mold Tritirachium album Limber. A peptidase of family S8 (subtilisin family) containing two disulfide bridges and one free Cys near the active site His. Formerly included in EC

Links to other databases: BRENDA, EXPASY, KEGG, MEROPS, Metacyc, PDB, CAS registry number: 39450-01-6


1. Ebeling, W., Hennrich, N., Klockow, M., Metz, H., Orth, H.D. and Lang, H. Proteinase K from Tritirachium album Limber. Eur. J. Biochem. 47 (1974) 91-97. [PMID: 4373242]

2. Morihara, K. and Tsuzuki, H. Specificity of proteinase K from Tritirachium album Limber for synthetic peptides. Agric. Biol. Chem. 39 (1975) 1489-1492

3. Kraus, E., Klitz, H.H. and Fembert, U.F. The specificity of proteinase K against oxidized insulin B chain. Hoppe-Seyler's Z. Physiol. Chem. 357 (1976) 233-237. [PMID: 943367]

4. Jany, K.-D., Lederer, G. and Mayer, B. Amino acid sequence of proteinase K from the mold Tritirachium album Limber. FEBS Lett. 199 (1986) 139-144

5. Betzel, C., Teplyakov, A.V., Harutyunyan, E.H., Saenger, W. and Wilson, K.S. Thermitase and proteinase K: a comparison of the refined three-dimensional structures of the native enzymes. Protein Engineering 3 (1990) 161-172 [PMID: 2184432]

[EC created 1992 (EC created 1961 as EC, transferred 1972 to EC, modified 1986, part incorporated 1992)]

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