PDOC00122 [for PROSITE entry PS00131]
Serine carboxypeptidases, active sites
All known carboxypeptidases are either metallo carboxypeptidases or serine
22.214.171.124 and EC 126.96.36.199). 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 [
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
Fission yeast sxa2, a probable carboxypeptidase involved in degrading or
processing mating pheromones [
Penicillium janthinellum carboxypeptidase S1 [
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) [
Naegleria fowleri virulence-related protein Nf314 [
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
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
February 2003 / Patterns and text revised.
PROSITE methods (with tools and information) covered by this documentation:
PS00131; Serine carboxypeptidases, serine active site (PATTERN)
PS00560; Serine carboxypeptidases, histidine active site (PATTERN)
1 Authors Liao D.I. Remington S.J.
Title Structure of wheat serine carboxypeptidase II at 3.5-A resolution. A new class of serine proteinase.
Source J. Biol. Chem. 265:6528-6531(1990).
PubMed ID 2324088
2 Authors Sorensen S.B. Svendsen I. Breddam K.
Title Primary structure of carboxypeptidase III from malted barley.
Source Carlsberg Res. Commun. 54:193-202(1989).
PubMed ID 2639682
3 Authors Imai Y. Yamamoto M.
Title Schizosaccharomyces pombe sxa1+ and sxa2+ encode putative proteases involved in the mating response.
Source Mol. Cell. Biol. 12:1827-1834(1992).
PubMed ID 1549128
4 Authors Svendsen I. Hofmann T. Endrizzi J. Remington S.J. Breddam K.
Title The primary structure of carboxypeptidase S1 from Penicillium janthinellum.
Source FEBS Lett. 333:39-43(1993).
PubMed ID 8224168
5 Authors Galjart N.J. Morreau H. Willemsen R. Gillemans N. Bonten E.J. d'Azzo A.
Title Human lysosomal protective protein has cathepsin A-like activity distinct from its protective function.
Source J. Biol. Chem. 266:14754-14762(1991).
PubMed ID 1907282
6 Authors Cho W.L. Deitsch K.W. Raikhel A.S.
Title An extraovarian protein accumulated in mosquito oocytes is a carboxypeptidase activated in embryos.
Source Proc. Natl. Acad. Sci. U.S.A. 88:10821-10824(1991).
PubMed ID 1961751
7 Authors Hu W.N. Kopachik W. Band R.N.
Title Cloning and characterization of transcripts showing virulence-related gene expression in Naegleria fowleri.
Source Infect. Immun. 60:2418-2424(1992).
PubMed ID 1587609
8 Authors Wajant H. Mundry K.W. Pfizenmaier K.
Title Molecular cloning of hydroxynitrile lyase from Sorghum bicolor (L.). Homologies to serine carboxypeptidases.
Source Plant Mol. Biol. 26:735-746(1994).
PubMed ID 7948927
9 Authors Rawlings N.D. Barrett A.J.
Title Families of serine peptidases.
Source Methods Enzymol. 244:19-61(1994).
PubMed ID 7845208
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