| Meprin A | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.24.18 | ||||||||
| CAS no. | 148938-24-3 | ||||||||
| 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 | ||||||||
| |||||||||
| 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. [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
- ^ 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.
.svg){kind=small} | This biochemistry article is a stub. You can help Wikipedia by expanding it. |
| Meprin A | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.24.18 | ||||||||
| CAS no. | 148938-24-3 | ||||||||
| 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 | ||||||||
| |||||||||
| 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. [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:
|
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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.
- ^ 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.
|
| This biochemistry article is a stub. You can help Wikipedia by expanding it. |