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Proteolytic enzymes catalyze the breaking of the carbon-nitrogen bonds between amino acids that are found in peptides and proteins. Most proteolytic enzymes are hydrolases, and hydrolysis of a peptide bond is a form of an acid-base reaction, in which a hydrogen ion (proton) is transferred. The terms “protease,” “proteinase,” and “proteolytic enzyme” are synonymous but strictly speaking can only be applied to peptidases that hydrolase bonds in proteins. Because there are many peptidases that act only on peptides, the term “peptidase” is recommended. Peptidases are included in subclass 3.4 of enzyme nomenclature (Barrett et al. 2004; Puente et al. 2003). There is a group of enzymes that break peptide bonds by a different mechanism: an asparagine residue is induced to cyclize to form a succinimide, which breaks the peptide bond and releases a peptide. These kinds of enzymes are known as asparagine peptide lyases (Rawlings et...
References
Abbenante G, Fairlie DP (2005) Protease inhibitors in the clinic. Med Chem 1:71–104
Barrett AJ, Rawlings ND, Woessner JF (2004) Handbook of proteolytic enzymes. Elsevier, London
Puente XS, Sanchez LM, Overall CM et al (2003) Human and mouse proteases: a comparative genomic approach. Nat Rev Genet 4:544–558
Rawlings ND, Barrett AJ (1993) Evolutionary families of peptidases. Biochem J 290:205–218
Rawlings ND, Barrett AJ, Bateman A (2011) Asparagine peptide lyases: a seventh catalytic type of proteolytic enzymes. J Biol Chem 286:38321–38328
Rawlings ND, Barrett AJ, Thomas PD, Huang X, Bateman A, Finn RD (2018) The MEROPS database of proteolytic enzymes, their substrates and inhibitors in 2017 and a comparison with peptidases in the PANTHER database. Nucleic Acids Res 46:D624–D632
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Rawlings, N.D. (2021). Nonviral Peptidases. In: Offermanns, S., Rosenthal, W. (eds) Encyclopedia of Molecular Pharmacology. Springer, Cham. https://doi.org/10.1007/978-3-030-21573-6_107-1
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DOI: https://doi.org/10.1007/978-3-030-21573-6_107-1
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