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PROSITE documentation PDOC00122

Serine carboxypeptidases, active sites

Description:

All known carboxypeptidases are either metallo carboxypeptidases or serine carboxypeptidases (EC 3.4.16.5 and EC 3.4.16.6). 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 4.1.2.11) (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.

Note:

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)
Consensus pattern: [LIVF]-x(2)-[LIVSTA]-x-[IVPST]-x-[GSDNQL]-[SAGV]-[SG]-H-x-[IVAQ]-P-x(3)-[PSA]
H is the active site residue
Sequences known to belong to this class detected by the pattern: ALL
Other sequence(s) detected in Swiss-Prot: NONE.
• Retrieve an alignment of Swiss-Prot true positive hits:
  Clustal format, color, condensed view  / Clustal format, color  / Clustal format, plain text  / Fasta format
• Retrieve the sequence logo from the alignment
• Taxonomic tree view of all Swiss-Prot/TrEMBL entries matching PS00560
• Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS00560
• Scan Swiss-Prot/TrEMBL entries against PS00560
• view ligand binding statistics
Matching PDB structures: 1AC5 1BCR 1BCS 1CPY ... [ALL]
CARBOXYPEPT_SER_SER, PS00131; Serine carboxypeptidases, serine active site  (PATTERN)
Consensus pattern: [LIVM]-x-[GSTA]-E-S-Y-[AG]-[GS]
S is the active site residue
Sequences known to belong to this class detected by the pattern: ALL, except for HNL
Other sequence(s) detected in Swiss-Prot: 3.
• Retrieve an alignment of Swiss-Prot true positive hits:
  Clustal format, color, condensed view  / Clustal format, color  / Clustal format, plain text  / Fasta format
• Retrieve the sequence logo from the alignment
• Taxonomic tree view of all Swiss-Prot/TrEMBL entries matching PS00131
• Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS00131
• Scan Swiss-Prot/TrEMBL entries against PS00131
• view ligand binding statistics
Matching PDB structures: 1AC5 1BCR 1BCS 1IVY ... [ALL]

References:

1 AuthorsLiao 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
2 AuthorsSorensen S.B., Svendsen I., Breddam K.
TitlePrimary structure of carboxypeptidase III from malted barley.
SourceCarlsberg Res. Commun. 54:193-202(1989).
PubMed ID2639682
3 AuthorsImai 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
4 AuthorsSvendsen 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
5 AuthorsGaljart 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
6 AuthorsCho 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
7 AuthorsHu 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
8 AuthorsWajant 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
9 AuthorsRawlings N.D., Barrett A.J.
TitleFamilies of serine peptidases.
SourceMethods Enzymol. 244:19-61(1994).
PubMed ID7845208
E1
Sourcehttp://www.expasy.org/cgi-bin/lists?peptidas.txt

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