Meprin A | |
---|---|
Identifiers | |
Symbol | Meprin |
InterPro | IPR008294 |
Membranome | 537 |
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. This metalloprotease can be associated with inflammatory responses. It can be found in the extracellular space where it can also form complex structures by joining its monomers together.
Meprin A is a dimer composed of the products transcribed from the following two genes:
|
|
References
- 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.
- ^ 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.
Proteases: metalloendopeptidases (EC 3.4.24) | |
---|---|
ADAM proteins | |
Matrix metalloproteinases | |
Other |
Enzymes | |
---|---|
Activity | |
Regulation | |
Classification | |
Kinetics | |
Types |
|
This biochemistry article is a stub. You can help Misplaced Pages by expanding it. |