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Peptidases and proteinases C

Formerly known as: Proteases


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Peptidases and proteinases hydrolyse peptide bonds, and can be simply divided on the basis of whether terminal peptide bonds are cleaved (exopeptidases and exoproteinases) at the amino terminus (aminopeptidases) or carboxy terminus (carboxypeptidases). Non-terminal peptide bonds are cleaved by endopeptidases and endoproteinases, which are divided into serine endopeptidases (EC 3.4.21.-), cysteine endopeptidases (EC 3.4.22.-), aspartate endopeptidases (EC 3.4.23.-), metalloendopeptidases (EC 3.4.24.-) and threonine endopeptidases (EC 3.4.25.-).

Since it is beyond the scope of the Guide to list all peptidase and proteinase activities, this summary focuses on selected enzymes of significant pharmacological interest that have ligands (mostly small-molecules) directed against them. For those interested in detailed background we recommend the MEROPS database [1] (with whom we collaborate) as an information resource [2].


Families that contain targets of relevance to immunopharmacology are highlighted in blue

Further reading

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NC-IUPHAR subcommittee and family contributors

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How to cite this family page

Database page citation:

Arnaud Chatonnet, David Fairlie, Christopher M. Overall, Neil Rawlings, Christopher Southan, Anthony J. Turner. Peptidases and proteinases. Accessed on 13/07/2024. IUPHAR/BPS Guide to PHARMACOLOGY,

Concise Guide to PHARMACOLOGY citation:

Alexander SPH, Fabbro D, Kelly E, Mathie A, Peters JA, Veale EL, Armstrong JF, Faccenda E, Harding SD, Pawson AJ, Sharman JL, Southan C, Davies JA; CGTP Collaborators. (2019) The Concise Guide to PHARMACOLOGY 2019/20: Enzymes. Br J Pharmacol. 176 Issue S1: S297-S396.