Meprin A (EC 3.4.24.18, endopeptidase-2, meprin-a, meprin, N-benzoyl-L-tyrosyl-p-aminobenzoic acid hydrolase, PABA-peptide hydrolase, PPH) is an enzyme that cleaves protein and peptide substrates preferentially on carboxyl side of hydrophobic residues.[1] This metalloprotease can be associated with inflammatory responses.[2] It can be found in the extracellular space where it can also form complex structures by joining its monomers together.[2]
| Meprin A | |
|---|---|
| Identifiers | |
| Symbol | Meprin |
| InterPro | IPR008294 |
| Membranome | 537 |
Meprin A is a dimer composed of the products transcribed from the following two genes:
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References
edit- ^ Sterchi EE, Stöcker W, Bond JS (October 2008). "Meprins, membrane-bound and secreted astacin metalloproteinases". Molecular Aspects of Medicine. 29 (5): 309–28. doi:10.1016/j.mam.2008.08.002. PMC 2650038. PMID 18783725.
- ^ a b Prox J, Arnold P, Becker-Pauly C (May 2015). "Meprin α and meprin β: procollagen proteinases in health and disease". Matrix Biology. 44: 7–13. doi:10.1016/j.matbio.2015.01.010. PMID 25617491.
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