Family S46


Summary Holotypes Alignment Tree Genomes Structure Literature

Summary for family S46

Family type peptidaseS46.001 - dipeptidyl-peptidase 7 (Porphyromonas gingivalis-type) (Porphyromonas gingivalis), MEROPS Accession MER0014366 (peptidase unit: 1-712)
Content of familyPeptidase family S46 contains dipeptidyl-peptidases from bacteria.
History Identifier created: MEROPS 5.7 (17 December 2001)
The only peptidases in the family to have been characterized are dipeptidyl-peptidase 7 (DPP-7; S46.001; Potempa et al., 2004) and DPP-11 (Ohara-Nemoto et al., 2011,Ohara-Nemoto et al., 2011,Sakamoto et al., 2015) from Porphyromonas gingivalis; and dipeptidyl peptidase BII (DPP BII, S46.003) from Pseudoxanthomonas mexicana (Suzuki et al., 2014.
Catalytic typeSerine
Active site residuesH89 D196 S648 
Active siteA catalytic triad (His, Asp, Ser) has been identified biochemically in DPP BII (Suzuki et al., 2014). From the crystal structure, the side chain of Arg673 in DPP-11 (S46.002) is essential in the S1 subsite for recognizing Asp or Glu (Sakamoto et al., 2015).
Activities and specificitiesDPP-7 is assayed with Ala-PheNHPhNO2 and is active over a broad pH range (6.5-9.0). Proteins, long peptides (such as the insulin B chain) and N-terminally blocked peptides are not cleaved.
InhibitorsDPP-7 is inhibited by the serine peptidase inhibitors DFP and 3,4-dichloroisocoumarin, but not by metal chelators such as EDTA or by cysteine peptidase inhibitors such as E-64 and iodoacetate. It is not inhibited by proteinase inhibitors such as serpins and alpha2-macroglobulin.
Molecular structureThe tertiary structures have been determined for DPP BII (Sakamoto et al., 2014)and DPP-11 (Sakamoto et al., 2015) and each shows a double beta-barrell fold characteristic of members of clan PA with a regulatory alpha-helical domain. DPP-7 is located on the cell surface and is predicted to have two N-terminal transmembrane domains. The purified form is truncated by cleavage at the Lys23Ala bond, which removes the first of the transmembrane domains.
Basis of clan assignmentFamily S46 is included in clan PA on the basis of comparisons of hidden Markov models derived from the MEROPS family alignments
Distribution of family Bacteria details  
Archaea -  
Protozoa -  
Fungi -  
Plants details  
Animals -  
Viruses -  
Biological functionsDPP-7 probably has a nutrional role, perhaps required for the further digestion of peptides generated by proteinases such as the gingipains (see family C25).
Statistics for family S46Sequences:1052
Identifiers with PDB entries:2
Downloadable files Sequence library (FastA format)
Sequence alignment (FastA format)
Phylogenetic tree (Newick format)
Peptidases and Homologues MEROPS ID Structure
dipeptidyl-peptidase 7 (Porphyromonas gingivalis-type)S46.001-
dipeptidyl-peptidase 11 (Porphyromonas gingivalis-type)S46.002Yes
dipeptidyl-peptidase BII (Pseudoxanthomonas mexicana)S46.003Yes
family S46 non-peptidase homologuesnon-peptidase homologue-
family S46 unassigned peptidasesunassigned-