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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 ...
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 .
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 human protein Serine protease HTRA2, mitochondrial is 49kDa in size and composed of 458 amino acids. The peptide fragment of 1-31 amino acid is the mitochondrial transition sequence, fragment 32-133 amino acid is propertied, and 134-458 is the mature protein Serine protease HTRA2, mitochondrial, and its theoretical pI of this protein is 6. ...
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]
Serine protease 23 is an enzyme that in humans is encoded by the PRSS23 gene. [5] This gene encodes a member of the trypsin family of serine proteases. Mouse studies found a decrease of mRNA levels after ovulation was induced. This gene seems to be highly conserved in vertebrates and may be an important ovarian protease. [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 ...
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 ...