| Entry |
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| Name |
Pro-Pro endopeptidase;
metalloprotease CD2830
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| Class |
Hydrolases;
Acting on peptide bonds (peptidases);
Metalloendopeptidases
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| Reaction(IUBMB) |
The enzyme catalyses the hydrolytic cleavage of peptide bonds between two proline residues
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| Comment |
This metalloprotease, which is secreted by the bacterium Peptoclostridium difficile, contains zinc.
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| History |
EC 3.4.24.89 created 2015
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| Orthology |
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| Genes |
» show all
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| Reference |
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| Authors |
Cafardi V, Biagini M, Martinelli M, Leuzzi R, Rubino JT, Cantini F, Norais N, Scarselli M, Serruto D, Unnikrishnan M |
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| Title |
Identification of a novel zinc metalloprotease through a global analysis of Clostridium difficile extracellular proteins. |
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| Journal |
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| Sequence |
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| Reference |
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| Authors |
Hensbergen PJ, Klychnikov OI, Bakker D, van Winden VJ, Ras N, Kemp AC, Cordfunke RA, Dragan I, Deelder AM, Kuijper EJ, Corver J, Drijfhout JW, van Leeuwen HC |
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| Title |
A novel secreted metalloprotease (CD2830) from Clostridium difficile cleaves specific proline sequences in LPXTG cell surface proteins. |
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| Journal |
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| Sequence |
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| Reference |
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| Authors |
Hensbergen PJ, Klychnikov OI, Bakker D, Dragan I, Kelly ML, Minton NP, Corver J, Kuijper EJ, Drijfhout JW, van Leeuwen HC |
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| Title |
Clostridium difficile secreted Pro-Pro endopeptidase PPEP-1 (ZMP1/CD2830) modulates adhesion through cleavage of the collagen binding protein CD2831. |
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| Journal |
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| Sequence |
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| Other DBs |
| ExPASy - ENZYME nomenclature database: | 3.4.24.89 |
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