Entry |
|
Name |
Pro-Pro endopeptidase;
metalloprotease CD2830
|
Class |
Hydrolases;
Acting on peptide bonds (peptidases);
Metalloendopeptidases
|
Reaction(IUBMB) |
The enzyme catalyses the hydrolytic cleavage of peptide bonds between two proline residues
|
Comment |
This metalloprotease, which is secreted by the bacterium Peptoclostridium difficile, contains zinc.
|
History |
EC 3.4.24.89 created 2015
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Orthology |
|
Genes |
BMET: | BMMGA3_10250 BMMGA3_15165 |
BDA: | FSZ17_14335 FSZ17_21540 |
PARG: | PspKH34_19770(zmp1) |
ACAC: | EYQ97_02490 EYQ97_06835 |
» show all
|
Reference |
|
Authors |
Cafardi V, Biagini M, Martinelli M, Leuzzi R, Rubino JT, Cantini F, Norais N, Scarselli M, Serruto D, Unnikrishnan M |
Title |
Identification of a novel zinc metalloprotease through a global analysis of Clostridium difficile extracellular proteins. |
Journal |
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Sequence |
|
Reference |
|
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 |
Title |
A novel secreted metalloprotease (CD2830) from Clostridium difficile cleaves specific proline sequences in LPXTG cell surface proteins. |
Journal |
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Sequence |
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Reference |
|
Authors |
Hensbergen PJ, Klychnikov OI, Bakker D, Dragan I, Kelly ML, Minton NP, Corver J, Kuijper EJ, Drijfhout JW, van Leeuwen HC |
Title |
Clostridium difficile secreted Pro-Pro endopeptidase PPEP-1 (ZMP1/CD2830) modulates adhesion through cleavage of the collagen binding protein CD2831. |
Journal |
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Sequence |
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Other DBs |
ExPASy - ENZYME nomenclature database: | 3.4.24.89 |
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