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Proteases are a class of enzymes that regulate much of what happens in the human body, both inside the cell and out, by cleaving peptide bonds in proteins.Through this activity, they govern the four essential cell functions: differentiation, motility, division and cell death — and activate important extracellular episodes, such as the biochemical cascade effect in blood clotting.
Ribbon diagram of a protease (TEV protease) complexed with its peptide substrate in black with catalytic residues in red.(. A protease (also called a peptidase, proteinase, or proteolytic enzyme) [1] is an enzyme that catalyzes proteolysis, breaking down proteins into smaller polypeptides or single amino acids, and spurring the formation of new protein products. [2]
Membrane-bound transcription factor site-2 protease, also known as S2P endopeptidase or site-2 protease (S2P), is an enzyme (EC 3.4.24.85) encoded by the MBTPS2 gene which liberates the N-terminal fragment of sterol regulatory element-binding protein (SREBP) transcription factors from membranes.
There are four groups of intramembrane proteases, distinguished by their catalytic mechanism: [5]. Metalloproteases: Site-2 protease (S2P) and S2P-like proteases [9]; Aspartyl proteases: this group includes presenilin, the active subunit of gamma secretase [10] [11] and signal peptide peptidases (SPPs) and SPP-like proteases, which are distantly related to presenilin but have opposite membrane ...
[2] In structure, the proteasome is a cylindrical complex containing a "core" of four stacked rings forming a central pore. Each ring is composed of seven individual proteins. The inner two rings are made of seven β subunits that contain three to seven protease active sites. These sites are located on the interior surface of the rings, so that ...
In molecular biology, elastase is an enzyme from the class of proteases (peptidases) that break down proteins, [1] specifically one that can break down elastin. In other words, the name only refers to the substrate specificity (i.e. what proteins it can digest), not to any kind of evolutionary grouping. [2]
Beta-secretase 1, also known as beta-site amyloid precursor protein cleaving enzyme 1, beta-site APP cleaving enzyme 1 (BACE1), membrane-associated aspartic protease 2, memapsin-2, aspartyl protease 2, and ASP2, is an enzyme that in humans is encoded by the BACE1 gene. [5] Expression of BACE1 is observed mainly in neurons and oligodendrocytes. [6]
PAR2 is activated by several different endogenous and exogenous proteases. It is activated by proteolytic cleavage of its extracellular amino terminus between arginine and serine. [13] The newly exposed N-terminus serves as tethered activation ligand, which binds a conserved region on extracellular loop 2 (ECL2) and activates the receptor. [5]