IUBMB Enzyme Nomenclature

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, CAS registry number:

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 (2013) e81306. [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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