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One family of natural inhibitors called "serpins" (abbreviated from serine protease inhibitors) can form a covalent bond with the serine protease, inhibiting its function. The best-studied serpins are antithrombin and alpha 1-antitrypsin , studied for their role in coagulation / thrombosis and emphysema / A1AT , respectively.
Serpins are a superfamily of proteins with similar structures that were first identified for their protease inhibition activity and are found in all kingdoms of life. [1] [2] The acronym serpin was originally coined because the first serpins to be identified act on chymotrypsin-like serine proteases (serine protease inhibitors).
This gene encodes a member of the serine protease family. The encoded protein contains a serine protease domain, a transmembrane domain, an LDL receptor class A domain, and a scavenger receptor cysteine-rich domain. Serine proteases are known to be involved in a variety of biological processes, whose malfunction often leads to human diseases ...
Transmembrane protease, serine 2 is an enzyme that in humans is encoded by the TMPRSS2 gene. [5] [6] [7] It belongs to the TMPRSS family of proteins, whose members are transmembrane proteins which have a serine protease activity. [8]
Kallikreins are a subgroup of serine proteases, enzymes capable of cleaving peptide bonds in proteins. In humans, plasma kallikrein (encoded by KLKB1 gene) has no known paralogue, while tissue kallikrein-related peptidases (KLKs) encode a family of fifteen closely related serine proteases.
Only 1 viral member of the subtilisin family is known, a 56-kDa protease from herpes virus 1, which infects the channel catfish. [3] Sedolisins (serine-carboxyl peptidases) are proteolytic enzymes whose fold resembles that of subtilisin; however, they are considerably larger, with the mature catalytic domains containing approximately 375 amino ...
Glutamyl endopeptidase I is a family of extracellular bacterial serine proteases. The proteases within this family have been identified in species of Staphylococcus, Bacillus, and Streptomyces, among others. The two former are more closely related, while the Streptomyces-type is treated as a separate family, glutamyl endopeptidase II. [1]
14089 Ensembl ENSG00000078098 ENSMUSG00000000392 UniProt Q12884 P97321 RefSeq (mRNA) NM_001291807 NM_004460 NM_007986 RefSeq (protein) NP_001278736 NP_004451 NP_032012 Location (UCSC) Chr 2: 162.17 – 162.25 Mb Chr 2: 62.33 – 62.4 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Fibroblast activation protein alpha (FAP-alpha) also known as prolyl endopeptidase FAP is an enzyme that ...