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Serine proteases (or serine endopeptidases) are enzymes that cleave peptide bonds in proteins. Serine serves as the nucleophilic amino acid at the (enzyme's) active site. [1] They are found ubiquitously in both eukaryotes and prokaryotes. Serine proteases fall into two broad categories based on their structure: chymotrypsin-like (trypsin-like ...
Factor D is a serine protease present in blood and tissue in an active sequence but self-inhibited conformation. The only known natural substrate of Factor D is Factor B, and cleavage of the Arg 234-Lys 235 scissile bond in Factor B results in two Factor B fragments, Ba and Bb.
The venom of solenodons and some shrews like the northern short-tailed shrew consist of multiple copies of kallikrein 1 (KLK1) serine proteases. [3] KLK1 are very similar to serine protease found in venomous snakes like vipers, and have evolved in parallel from a common toxin precursor, [4] which cause hypotensive effects in vivo. [5]
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 ...
7113 50528 Ensembl ENSG00000184012 ENSMUSG00000000385 UniProt O15393 Q9JIQ8 RefSeq (mRNA) NM_001135099 NM_005656 NM_001382720 NM_015775 RefSeq (protein) NP_001128571 NP_005647 NP_001369649 NP_056590 Location (UCSC) Chr 21: 41.46 – 41.53 Mb Chr 16: 97.37 – 97.41 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Transmembrane protease, serine 2 is an enzyme that in humans is encoded ...
"Subtilisin" does not refer to a single protein, but to an entire clade under subtilases containing the classical subtilisins. The clade can be further divided into four groups: "true subtilisins" (containing the classical members), "high-alkaline subtilisins", "intracellular subtilisins", and "phylogenetically intermediate subtilisins" (PIS).
Serine (symbol Ser or S) [3] [4] is an α-amino acid that is used in the biosynthesis of proteins. It contains an α- amino group (which is in the protonated − NH + 3 form under biological conditions), a carboxyl group (which is in the deprotonated − COO −
Serine protease HTRA1 is an enzyme that in humans is encoded by the HTRA1 gene. [ 5 ] [ 6 ] The HTRA1 protein is composed of four distinct protein domains . They are from amino-terminus to carboxyl-terminus an Insulin-like growth factor binding domain, a kazal domain , a trypsin -like peptidase domain and a PDZ domain .