MetaCyc EC 3.4.21.64 -- peptidase K

Parent Class: EC-Numbers → 3 -- Hydrolases → 3.4 -- Acting on peptide bonds (peptide hydrolases) → 3.4.21 -- Serine endopeptidases

Synonyms: Tritirachium alkaline proteinase, Tritirachium album serine proteinase, proteinase K, Tritirachium album proteinase K, endopeptidase K

Unification Links: BRENDA:3.4.21.64, ENZYME:3.4.21.64, IUBMB-ExplorEnz:3.4.21.64

Supersedes EC number: 3.4.4.16

Reaction:
protein + H2O → 2 peptide + 2 H+

Summary:
This enzyme catalyzes hydrolysis of keratin, and of other proteins with subtilisin-like specificity. Hydrolyses peptide amides.

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

Citations: [Ebeling74, Morihara75, Kraus76, Jany86, Betzel90]

References

Betzel90: Betzel C, Teplyakov AV, Harutyunyan EH, Saenger W, Wilson KS (1990). "Thermitase and proteinase K: a comparison of the refined three-dimensional structures of the native enzymes." Protein Eng 3(3);161-72. PMID: 2184432

Ebeling74: Ebeling W, Hennrich N, Klockow M, Metz H, Orth HD, Lang H (1974). "Proteinase K from Tritirachium album Limber." Eur J Biochem 47(1);91-7. PMID: 4373242

Jany86: Jany, K.-D., Lederer, G., Mayer, B. (1986). "Amino acid sequence of proteinase K from the mold Tritirachium album Limber." FEBS Lett.

Kraus76: Kraus E, Kiltz HH, Femfert UF (1976). "The specificity of proteinase K against oxidized insulin B chain." Hoppe Seylers Z Physiol Chem 357(2);233-7. PMID: 943367

Morihara75: Morihara, K., Tsuzuki, H. (1975). "Specificity of proteinase K from Tritirachium album Limber for synthetic peptides." Agric. Biol. Chem.

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Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 46(D1):D633-D639 2018
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