The Enzyme Database

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EC 3.4.24.89     
Accepted name: Pro-Pro endopeptidase
Reaction: The enzyme catalyses the hydrolytic cleavage of peptide bonds between two proline residues
Other name(s): metalloprotease CD2830
Comments: This metalloprotease, which is secreted by the bacterium Peptoclostridium difficile, contains zinc.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  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 One 8:e81306 (2013). [PMID: 24303041]
2.  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. Proteomics 13 (2014) 1231–1244. [PMID: 24623589]
3.  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 Lett. 589 (2015) 3952–3958. [PMID: 26522134]
[EC 3.4.24.89 created 2015]
 
 


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