Advertisement

Peptidases: a view of classification and nomenclature

  • Alan J. Barrett
Chapter
Part of the MCBU Molecular and Cell Biology Updates book series (MCBU)

Abstract

It is beyond question that the results of research on proteolytic enzymes, or peptidases, are already benefiting mankind in many ways, and there is no doubt that research in this area has the potential to contribute still more in the future. One of the clearest indications of the general recognition of this promise is the vast annual expenditure of the pharmaceutical industry on exploring the involvement of peptidases in human health and disease.

Keywords

Enzyme Commission Peptidase Family Enzyme Commission Number Acyl Enzyme Prolyl Oligopeptidase 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

References

  1. 1.
    Barrett AJ (1986) An introduction to the proteinases. In: AJ Barrett, G Salvesen (eds): Proteinase Inhibitors. Elsevier Science Publishers, Amsterdam, 3–22Google Scholar
  2. 2.
    Barrett AJ (1998) Proteolytic enzymes: nomenclature and classification. In: RJ Beynon, JS Bond (eds): Proteolytic Enzymes —a Practical Approach. Oxford University Press, OxfordGoogle Scholar
  3. 3.
    Nomenclature Committee of the International Union of Biochemistry Molecular Biology (1992) Enzyme Nomenclature 1992. Academic Press, OrlandoGoogle Scholar
  4. 4.
    Rawlings ND, Barrett AJ (1993) Evolutionary families of peptidases. Biochem J. 290: 205–218PubMedGoogle Scholar
  5. 5.
    Rawlings ND, Barrett AJ (1994) Families of serine peptidases. Meth Enzymol. 244: 19–61PubMedCrossRefGoogle Scholar
  6. 6.
    Rawlings ND, Barrett AJ (1994) Families of cysteine peptidases. Meth Enzymol. 244: 461–486PubMedCrossRefGoogle Scholar
  7. 7.
    Rawlings ND, Barrett AJ (1995) Evolutionary families of metallopeptidases. Meth Enzymol. 248: 183–228PubMedCrossRefGoogle Scholar
  8. 8.
    Rawlings ND, Barrett AJ (1995) Families of aspartic peptidases, and those of unknown catalytic mechanism. Meth Enzymol. 248: 105–120PubMedCrossRefGoogle Scholar
  9. 9.
    Webb EC (1993) Enzyme nomenclature: a personal perspective. FASEB J. 7: 1192–1194PubMedGoogle Scholar
  10. 10.
    Seemüller E, Lupas A, Stock D, Löwe J, Huber R, Baumeister W (1995) Proteasome from Thermoplasma acidophilum: a threonine protease. Science. 268: 579–582PubMedCrossRefGoogle Scholar
  11. 11.
    Allaire M, Chernaia MM, Malcolm BA, James MNG (1994) Picornaviral 3C cysteine proteinases have a fold similar to chymotrypsin-like serine proteinases. Nature. 369: 72–76PubMedCrossRefGoogle Scholar
  12. 12.
    Rawlings ND, Barrett AJ (1990) Bone morphogenetic protein 1 is homologous in part with calcium-dependent serine proteinase. Biochem J. 266: 622–624PubMedGoogle Scholar
  13. 13.
    Rawlings ND, Barrett AJ (1999) MEROPS: the peptidase database. Nucleic Acids Res. 27: 325–331PubMedCrossRefGoogle Scholar

Copyright information

© Springer Basel AG 1999

Authors and Affiliations

  • Alan J. Barrett
    • 1
  1. 1.MRC Molecular Enzymology LaboratoryThe Babraham InstituteCambridgeUK

Personalised recommendations