![]() ![]() ![]() ![]() Also has dipeptidyl peptidase activity, exhibiting the ability to hydrolyze the prolyl bond two residues from the N-terminus of synthetic dipeptide substrates provided that the penultimate residue is proline, with a preference for Ala-Pro, Ile-Pro, Gly-Pro, Arg-Pro and Pro-Pro (PubMed: 10347120, 10593948, 16175601, 16223769, 16651416, 16410248, 17381073, 21314817, 24371721, 24717288). Both plasma membrane and soluble forms exhibit post-proline cleaving endopeptidase activity, with a marked preference for Ala/Ser-Gly-Pro-Ser/Asn/Ala consensus sequences, on substrate such as alpha-2-antiplasmin SERPINF2 and SPRY2 (PubMed: 14751930, 16223769, 16480718, 16410248, 17381073, 18095711, 21288888, 24371721). UniProtKB/Swiss-Prot Summary for FAP GeneĬell surface glycoprotein serine protease that participates in extracellular matrix degradation and involved in many cellular processes including tissue remodeling, fibrosis, wound healing, inflammation and tumor growth.
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