ExplorEnz: EC 3.4.21.64

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3.4.21.64

Accepted name:

peptidase K

Reaction:

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

Other name(s):

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 3.4.21.14

Links to other databases:

BRENDA, EXPASY, Gene, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 39450-01-6

References:

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. [DOI] [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. [DOI] [PMID: 2184432]

[EC 3.4.21.64 created 1992 (EC 3.4.21.14 created 1961 as EC 3.4.4.16, transferred 1972 to EC 3.4.21.14, modified 1986, part incorporated 1992)]