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A metalloproteinase, or metalloprotease, is any protease enzyme whose catalytic mechanism involves a metal. An example is ADAM12 which plays a significant role in the fusion of muscle cells during embryo development, in a process known as myogenesis.
Thimet oligopeptidase is an enzyme that in humans is encoded by the THOP1 gene.
Nardilysin is a protein that in humans is encoded by the NRD1 gene.
Lys-N is a metalloendopeptidase found in the mushroom Grifola frondosa that cleaves proteins on the amino side of lysine residues.
Ecadotril is a neutral endopeptidase inhibitor ((NEP) EC 3.4.24.11) and determined by the presence of peptidase family M13 as a neutral endopeptidase inhibited by phosphoramidon. Ecadotril is the (S)-enantiomer of racecadotril. NEP-like enzymes include the endothelin-converting enzymes. The peptidase M13 family believed to activate or inactivate oligopeptide (pro)-hormones such as opioid peptides, neprilysin is another member of this group, in the case of the metallopeptidases and aspartic, the nucleophiles clan or family for example MA, is an activated water molecule. The peptidase domain for members of this family also contains a bacterial member and resembles that of thermolysin the predicted active site residues for members of this family and thermolysin occur in the motif HEXXH. Thermolysin complexed with the inhibitor (S)-thiorphan are isomeric thiol-containing inhibitors of endopeptidase EC 24-11 (also called "enkephalinase").
Astacins are a family of multidomain metalloendopeptidases which are either secreted or membrane-anchored. These metallopeptidases belong to the MEROPS peptidase family M12, subfamily M12A. The protein fold of the peptidase domain for members of this family resembles that of thermolysin, the type example for clan MA and the predicted active site residues for members of this family and thermolysin occur in the motif HEXXH.
IgA-specific metalloendopeptidase is an enzyme. This enzyme catalyses the following chemical reaction:
Peptidyl-Lys metalloendopeptidase is an enzyme. This enzyme catalyses the following chemical reaction
Coccolysin is an enzyme. This enzyme catalyses the following chemical reaction
Beta-lytic metalloendopeptidase is an enzyme. This enzyme catalyses the following chemical reaction
Peptidyl-Asp metalloendopeptidase is an enzyme. This enzyme catalyses the following chemical reaction
Atrolysin F is an enzyme. This enzyme catalyses the following chemical reaction
Horrilysin is an enzyme. This enzyme catalyses the following chemical reaction
Pitrilysin is an enzyme. This enzyme catalyses the following chemical reaction:
Nardilysin is an enzyme. This enzyme catalyses the following chemical reaction
Menoufia University is one of the regional universities in Egypt, established in 1976. The university is characterized by rapid establishment and wide fame. The university started with four colleges, then it expanded and established many of its affiliated colleges until it became comprising about 80000 students, 3000 faculty members and assistant staff. The main headquarters of the university is located in Shebin El Kom. At the present time, the university includes 13 colleges and one institute after the separation of the faculties of the university branch in Sadat City, which has become the University of Sadat City.
Astacin-like metalloendopeptidase is a protein that in humans is encoded by the ASTL gene.
Thimet oligopeptidases, also known as TOPs, are a type of M3 metallopeptidases. These enzymes can be found in animals and plants, showing distinctive functions. In animals and humans, they are involved in the degradation of peptides, such as bradykinin, neurotensin, angiotensin I, and Aβ peptide, helping to regulate physiological processes. In plants, their role is related to the degradation of targeting peptides and the immune response to pathogens through Salicylic Acid (SA)-dependent stress signaling. In Arabidopsis thaliana—recognized as a model plant for scientific studies—two thimet oligopeptidases, known as TOP1 and TOP2, have been identified as targets for salicylic acid binding in the plant. These TOP enzymes are key components to understand the SA-mediated signaling where interactions exist with different components and most of the pathways are unknown.
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References
- ↑ Glucksman MJ, Orlowski M, Roberts JL (April 1992). "Structural and functional studies of the metalloendopeptidase (EC 3.4.24.15) involved in degrading gonadotropin releasing hormone". Biophysical Journal. 62 (1): 119–122. Bibcode:1992BpJ....62..119G. doi:10.1016/S0006-3495(92)81798-8. PMC 1260504 . PMID 1318098.
