PROSITE documentation PDOC00122
Serine carboxypeptidases, active sites


All known carboxypeptidases are either metallo carboxypeptidases or serine carboxypeptidases (EC and EC The catalytic activity of the serine carboxypeptidases, like that of the trypsin family serine proteases, is provided by a charge relay system involving an aspartic acid residue hydrogen-bonded to a histidine, which is itself hydrogen-bonded to a serine [1]. Proteins known to be serine carboxypeptidases are:

  • Barley and wheat serine carboxypeptidases I, II, and III [2].
  • Yeast carboxypeptidase Y (YSCY) (gene PRC1), a vacuolar protease involved in degrading small peptides.
  • Yeast KEX1 protease, involved in killer toxin and α-factor precursor processing.
  • Fission yeast sxa2, a probable carboxypeptidase involved in degrading or processing mating pheromones [3].
  • Penicillium janthinellum carboxypeptidase S1 [4].
  • Aspergullus niger carboxypeptidase pepF.
  • Aspergullus satoi carboxypeptidase cpdS.
  • Vertebrate protective protein / cathepsin A [5], a lysosomal protein which is not only a carboxypeptidase but also essential for the activity of both β-galactosidase and neuraminidase.
  • Mosquito vitellogenic carboxypeptidase (VCP) [6].
  • Naegleria fowleri virulence-related protein Nf314 [7].
  • Yeast hypothetical protein YBR139w.
  • Caenorhabditis elegans hypothetical proteins C08H9.1, F13D12.6, F32A5.3, F41C3.5 and K10B2.2.

This family also includes:

  • Sorghum (s)-hydroxymandelonitrile lyase (EC (hydroxynitrile lyase) (HNL) [8], an enzyme involved in plant cyanogenesis.

The sequences surrounding the active site serine and histidine residues are highly conserved in all these serine carboxypeptidases.


These proteins belong to family S10 in the classification of peptidases [9,E1].

Last update:

February 2003 / Patterns and text revised.


Technical section

PROSITE methods (with tools and information) covered by this documentation:

CARBOXYPEPT_SER_HIS, PS00560; Serine carboxypeptidases, histidine active site  (PATTERN)

CARBOXYPEPT_SER_SER, PS00131; Serine carboxypeptidases, serine active site  (PATTERN)


1AuthorsLiao D.I. Remington S.J.
TitleStructure of wheat serine carboxypeptidase II at 3.5-A resolution. A new class of serine proteinase.
SourceJ. Biol. Chem. 265:6528-6531(1990).
PubMed ID2324088

2AuthorsSorensen S.B. Svendsen I. Breddam K.
TitlePrimary structure of carboxypeptidase III from malted barley.
SourceCarlsberg Res. Commun. 54:193-202(1989).
PubMed ID2639682

3AuthorsImai Y. Yamamoto M.
TitleSchizosaccharomyces pombe sxa1+ and sxa2+ encode putative proteases involved in the mating response.
SourceMol. Cell. Biol. 12:1827-1834(1992).
PubMed ID1549128

4AuthorsSvendsen I. Hofmann T. Endrizzi J. Remington S.J. Breddam K.
TitleThe primary structure of carboxypeptidase S1 from Penicillium janthinellum.
SourceFEBS Lett. 333:39-43(1993).
PubMed ID8224168

5AuthorsGaljart N.J. Morreau H. Willemsen R. Gillemans N. Bonten E.J. d'Azzo A.
TitleHuman lysosomal protective protein has cathepsin A-like activity distinct from its protective function.
SourceJ. Biol. Chem. 266:14754-14762(1991).
PubMed ID1907282

6AuthorsCho W.L. Deitsch K.W. Raikhel A.S.
TitleAn extraovarian protein accumulated in mosquito oocytes is a carboxypeptidase activated in embryos.
SourceProc. Natl. Acad. Sci. U.S.A. 88:10821-10824(1991).
PubMed ID1961751

7AuthorsHu W.N. Kopachik W. Band R.N.
TitleCloning and characterization of transcripts showing virulence-related gene expression in Naegleria fowleri.
SourceInfect. Immun. 60:2418-2424(1992).
PubMed ID1587609

8AuthorsWajant H. Mundry K.W. Pfizenmaier K.
TitleMolecular cloning of hydroxynitrile lyase from Sorghum bicolor (L.). Homologies to serine carboxypeptidases.
SourcePlant Mol. Biol. 26:735-746(1994).
PubMed ID7948927

9AuthorsRawlings N.D. Barrett A.J.
TitleFamilies of serine peptidases.
SourceMethods Enzymol. 244:19-61(1994).
PubMed ID7845208


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