Meprin A
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| Meprin A | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.24.18 | ||||||||
| CAS no. | Template:CAS | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
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| Meprin A | |||||||
|---|---|---|---|---|---|---|---|
| Identifiers | |||||||
| Symbol | Meprin | ||||||
| InterPro | IPR008294 | ||||||
| Membranome | 537 | ||||||
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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 is a dimer composed of the products transcribed from the following two genes:
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References
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- ^ Page Module:Citation/CS1/styles.css has no content.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 Page Module:Citation/CS1/styles.css has no content.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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