Meprin A: Difference between revisions
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{{Pfam_box | |||
| Symbol = Meprin | |||
| Name = Meprin A | |||
| image = | |||
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| InterPro= IPR008294 | |||
| SMART= | |||
| PROSITE = | |||
| SCOP = | |||
| TCDB = | |||
| OPM family= | |||
| OPM protein= | |||
| Pfam= | |||
| PDB= | |||
| Membranome family= 537 | |||
}} | |||
'''Meprin A''' ({{EC number|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.<ref name="pmid18783725">{{cite journal | vauthors = Sterchi EE, Stöcker W, Bond JS | title = Meprins, membrane-bound and secreted astacin metalloproteinases | journal = Mol. Aspects Med. | volume = 29 | issue = 5 | pages = 309–28 |date=October 2008 | pmid = 18783725 | pmc = 2650038 | doi = 10.1016/j.mam.2008.08.002 | url = | issn = }}</ref> | '''Meprin A''' ({{EC number|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.<ref name="pmid18783725">{{cite journal | vauthors = Sterchi EE, Stöcker W, Bond JS | title = Meprins, membrane-bound and secreted astacin metalloproteinases | journal = Mol. Aspects Med. | volume = 29 | issue = 5 | pages = 309–28 |date=October 2008 | pmid = 18783725 | pmc = 2650038 | doi = 10.1016/j.mam.2008.08.002 | url = | issn = }}</ref> | ||
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[[Category:EC 3.4.24]] | [[Category:EC 3.4.24]] | ||
[[Category:Single-pass transmembrane proteins]] | |||
Latest revision as of 08:59, 9 January 2019
| 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]
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". Mol. Aspects Med. 29 (5): 309–28. doi:10.1016/j.mam.2008.08.002. PMC 2650038. PMID 18783725.
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