Family S10

Family

Summary Holotypes Alignment Tree Genomes Structure Literature H-seq M-seq Architecture

Summary for family S10

Family type peptidaseS10.001 - carboxypeptidase Y (Saccharomyces cerevisiae), MEROPS Accession MER0002010 (peptidase unit: 112-532)
Content of familyPeptidase family S10 contains only carboxypeptidases.
History Identifier created: Biochem.J. 290:205-218 (1993)
Catalytic typeSerine
Active site residuesS257 D449 H508 
Active siteThe residues of the catalytic triad in family S10 occur in the order Ser, Asp and His (Jung et al., 1998). There is a conserved Glu preceding the catalytic serine that is thought to be responsible for the acidic pH optimum of the carboxypeptidases.
Activities and specificitiesThe peptidase family differs from most other serine peptidase families (S53 being the exception) in that its peptidases are only active at acidic pH. The carboxypeptidases in family S10 show two main types of specificity. Some (e.g. carboxypeptidase C) show a preference for hydrophobic residues in positions P1 and P1". Carboxypeptidases of the second set (e.g. carboxypeptidase D) display a preference for the basic amino acids either side of the scissile bond, but are also able to cleave peptides with hydrophobic residues in these positions. It is notable that carboxypeptidases specific for hydrophobic or basic residues are also found among the metallocarboxypeptidases in family M14.
InhibitorsNatural inhibitors include a high affinity inhibitor of carboxypeptidase Y encoded by the TFSI gene of Saccharomyces cerevisiae . Antipain and chymostatin inhibit carboxypeptidase D (Bullock et al., 1996). The serine carboxypeptidases are also inhibited by DFP and PMSF.
Molecular structureThe peptidases of family S10 have what has been termed the alpha/beta hydrolase fold (Ollis et al., 1992). Family S10 peptidases contain 14 alpha helices and 11 mixed beta sheets; the six central beta strands are surrounded on either side by the 14 alpha helices. The catalytic triads of carboxypeptidase C, chymotrypsin and subtilisin can be superimposed, even though the folds are unrelated.
ClanSC
Basis of clan assignmentType family of clan SC.
Distribution of family Bacteria details  
Archaea details  
Protozoa details  
Fungi -  
Plants details  
Animals details  
Viruses -  
Biological functionsThe serine carboxypeptidases are synthesised as preproenzymes. Carboxypeptidases C have been implicated in having structural roles. Lysosomal carboxypeptidase A is essential for the correct assembly and function of the particle that contains beta-galactosidase and neuraminidase. Mutation in the this leads to genetic disorders such as galactosialidosis.
Pharmaceutical and biotech relevanceCarboxypeptidase Y (S10.001) is used in peptide sequencing.
Statistics for family S10Sequences:10248
Identifiers:87
Identifiers with PDB entries:7
Downloadable files Sequence library (FastA format)
Sequence alignment (FastA format)
Phylogenetic tree (Newick format)
Other databases CATH 3.40.50.1820
INTERPRO IPR000379
PANTHER PTHR11802
PFAM PF00450
SCOP 53499
Peptidases and Homologues MEROPS ID Structure
carboxypeptidase YS10.001Yes
serine carboxypeptidase AS10.002Yes
vitellogenic carboxypeptidase-like proteinS10.003-
serine carboxypeptidase CS10.004-
serine carboxypeptidase DS10.005Yes
Mername-AA083 peptidaseS10.006-
kex carboxypeptidaseS10.007Yes
carboxypeptidase OcpAS10.008-
serine carboxypeptidase III (plant)S10.009-
serine carboxypeptidase Z (Absidia zachae) and similarS10.010-
serine carboxypeptidase PS10.011-
Sxa2 carboxypeptidaseS10.012-
SCPEP1 peptidaseS10.013-
carboxypeptidase OS10.014-
BRS1 serine carboxypeptidaseS10.015-
carboxypeptidase OcpBS10.016-
OsBISCPL1-type putative carboxypeptidaseS10.017-
serine carboxypeptidase 46 (Oryza sativa)S10.018-
At1g33540 (Arabidopsis thaliana)S10.A01-
At3g12230 (Arabidopsis thaliana)S10.A02-
At1g73290 (Arabidopsis thaliana)S10.A03-
At1g73270 (Arabidopsis thaliana)S10.A04-
At1g73280 (Arabidopsis thaliana)S10.A05-
At1g73310 (Arabidopsis thaliana)S10.A06-
At5g36180 (Arabidopsis thaliana)S10.A07-
At2g22970 (Arabidopsis thaliana)S10.A08-
At2g22920 (Arabidopsis thaliana)S10.A09-
At3g25420 (Arabidopsis thaliana)S10.A10-
At4g12910 (Arabidopsis thaliana)S10.A11-
At2g23010 (Arabidopsis thaliana)S10.A12-
At2g23000 (Arabidopsis thaliana)S10.A13-
At2g22990 (Arabidopsis thaliana)S10.A14Yes
At3g10450 (Arabidopsis thaliana)S10.A15-
At1g73300 (Arabidopsis thaliana)S10.A16-
At3g12220 (Arabidopsis thaliana)S10.A17-
At5g09640 (Arabidopsis thaliana)S10.A18Yes
At3g12203 (Arabidopsis thaliana)S10.A19-
At3g17180 (Arabidopsis thaliana)S10.A20-
At5g42240 (Arabidopsis thaliana)-type peptidaseS10.A21-
At5g42230 (Arabidopsis thaliana)S10.A22-
At3g07990 (Arabidopsis thaliana)-type peptidaseS10.A23-
At1g28110 (Arabidopsis thaliana)-type peptidaseS10.A24-
At1g43780 (Arabidopsis thaliana)S10.A25-
At1g61130 (Arabidopsis thaliana)S10.A26-
At4g15100 (Arabidopsis thaliana)S10.A27-
At2g35770 (Arabidopsis thaliana)S10.A28-
At2g05850 (Arabidopsis thaliana)S10.A29-
At2g24010 (Arabidopsis thaliana)S10.A30-
At3g52010 (Arabidopsis thaliana)S10.A31-
At4g30810 (Arabidopsis thaliana)S10.A32-
At2g12480 (Arabidopsis thaliana)S10.A33-
At5g08260 (Arabidopsis thaliana)S10.A34-
At2g24000 (Arabidopsis thaliana)S10.A35-
At1g11080 (Arabidopsis thaliana)S10.A36-
At3g52000 (Arabidopsis thaliana)S10.A37-
At3g52020 (Arabidopsis thaliana)S10.A38-
At5g23210 (Arabidopsis thaliana)S10.A39-
At3g02110 (Arabidopsis thaliana)S10.A40-
At3g63470 (Arabidopsis thaliana)S10.A41-
At2g33530 (Arabidopsis thaliana)S10.A42-
At2g35780 (Arabidopsis thaliana)S10.A43Yes
At5g22980 (Arabidopsis thaliana)S10.A44-
At3g10410 (Arabidopsis thaliana)S10.A45-
At3g45010 (Arabidopsis thaliana)S10.A46-
At2g22960 (Arabidopsis thaliana)S10.A47-
At3g56540 (Arabidopsis thaliana)S10.A48-
putative serine carboxypeptidase (Saccharomyces cerevisiae)S10.A49-
CG31821 (Drosophila melanogaster)S10.A50-
CG31823 protein (Drosophila melanogaster)S10.A51-
CG32483 protein (Drosophila melanogaster)S10.A52-
CG3344 protein (Drosophila melanogaster)S10.A53-
Y40D12A.2 g.p. (Caenorhabditis elegans)S10.A54-
F13D12.6 g.p. (Caenorhabditis elegans)S10.A55-
C08H9.1 g.p. (Caenorhabditis elegans)S10.A56-
Y16B4A.2 g.p. unit 3 (Caenorhabditis elegans)S10.A57-
K10B2.2 g.p. (Caenorhabditis elegans)S10.A58-
F41C3.5 g.p. (Caenorhabditis elegans)S10.A59-
K10C2.1 g.p. (Caenorhabditis elegans)S10.A60-
Y32F6A.5 g.p. (Caenorhabditis elegans)S10.A61-
Y16B4A.2 g.p. (Caenorhabditis elegans)S10.A62-
F22E12.1 g.p. (Caenorhabditis elegans)S10.A63-
K10C2.1 g.p. (Caenorhabditis elegans)S10.A64-
F32A5.3 (Caenorhabditis elegans)S10.A65-
cpy1 g.p. (Schizosaccharomyces pombe)S10.A66-
kex1 g.p. (Schizosaccharomyces pombe)S10.A67-
DDB_G0280105 g.p. (Dictyostelium discoideum)S10.A68-
SCPL54 g.p. (Arabidopsis thaliana)S10.A69-
Family S10 non-peptidase homologuesnon-peptidase homologue-
Family S10 unassigned peptidasesunassigned-