Literature for peptidase M34.002: Pro-Pro endopeptidase 1 (Clostridium difficile-type)

Summary Alignment Sequences Sequence features Distribution Structure Literature Substrates

(Topics flags: S Structure, P Specificity. To select only the references relevant to a single topic, click the link above. See explanation.)

    2024
  1. Claushuis,B., Cordfunke,R.A., de Ru,A.H., van Angeren,J., Baumann,U., van Veelen,P.A., Wuhrer,M., Corver,J., Drijfhout,J.W. and Hensbergen,P.J.
    Non-prime- and prime-side profiling of Pro-Pro endopeptidase specificity using synthetic combinatorial peptide libraries and mass spectrometry
    FEBS J291, 3820-3838. PubMed  Europe PubMed DOI
  2. 2019
  3. Pichlo,C., Juetten,L., Wojtalla,F., Schacherl,M., Diaz,D. and Baumann,U.
    Molecular determinants of the mechanism and substrate specificity of Clostridium difficile proline-proline endopeptidase-1
    J Biol Chem294, 11525-11535. PubMed  Europe PubMed DOI  S
  4. 2017
  5. Corver,J., Cordo',V., van Leeuwen,H.C., Klychnikov,O.I. and Hensbergen,P.J.
    Covalent attachment and Pro-Pro endopeptidase (PPEP-1)-mediated release of Clostridium difficile cell surface proteins involved in adhesion
    Mol Microbiol105, 663-673. PubMed  Europe PubMed DOI
  6. 2016
  7. Oliveira Paiva,A.M., Friggen,A.H., Hossein-Javaheri,S. and Smits,W.K.
    The signal sequence of the abundant extracellular metalloprotease PPEP-1 can be used to secrete synthetic reporter proteins in Clostridium difficile
    ACS Synth Biol5, 1376-1382. PubMed  Europe PubMed DOI
  8. Rubino,J.T., Martinelli,M., Cantini,F., Castagnetti,A., Leuzzi,R., Banci,L. and Scarselli,M.
    Structural characterization of zinc-bound Zmp1, a zinc-dependent metalloprotease secreted by Clostridium difficile
    J Biol Inorg Chem21, 185-196. PubMed  Europe PubMed DOI
  9. 2015
  10. Hensbergen,P.J., Klychnikov,O.I., Bakker,D., Dragan,I., Kelly,M.L., Minton,N.P., Corver,J., Kuijper,E.J., Drijfhout,J.W. and van Leeuwen,H.C.
    Clostridium difficile secreted Pro-Pro endopeptidase PPEP-1 (ZMP1/CD2830) modulates adhesion through cleavage of the collagen binding protein CD2831
    FEBS Lett589, 3952-3958. PubMed  Europe PubMed DOI  P
  11. Schacherl,M., Pichlo,C., Neundorf,I. and Baumann,U.
    Structural basis of proline-proline peptide bond specificity of the metalloprotease Zmp1 implicated in motility of Clostridium difficile
    Structure23, 1632-1642. PubMed  Europe PubMed DOI  S
  12. 2014
  13. Hensbergen,P.J., Klychnikov,O.I., Bakker,D., van Winden,V.J., Ras,N., Kemp,A.C., Cordfunke,R.A., Dragan,I., Deelder,A.M., Kuijper,E.J., Corver,J., Drijfhout,J.W. and van Leeuwen,H.C.
    A novel secreted metalloprotease (CD2830) from Clostridium difficile cleaves specific proline sequences in LPXTG cell surface proteins
    Mol Cell Proteomics13, 1231-1244. PubMed  Europe PubMed DOI  P
  14. 2013
  15. Cafardi,V., Biagini,M., Martinelli,M., Leuzzi,R., Rubino,J.T., Cantini,F., Norais,N., Scarselli,M., Serruto,D. and Unnikrishnan,M.
    Identification of a novel zinc metalloprotease through a global analysis of Clostridium difficile extracellular proteins
    PLoS ONE8, e81306-e81306. PubMed  Europe PubMed DOI