Literature for peptidase M34.002: Pro-Pro endopeptidase 1 (Clostridium difficile-type)
(Topics flags: S Structure, P Specificity. To select only the references relevant to a single topic, click the link above. See explanation.)
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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 -
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 -
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 -
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 -
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 -
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 -
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 -
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 -
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
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