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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.
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.
Protein degradation is a major regulatory mechanism of gene expression [1] and contributes substantially to shaping mammalian proteomes. [2] Uncatalysed, the hydrolysis of peptide bonds is extremely slow, taking hundreds of years. Proteolysis is typically catalysed by cellular enzymes called proteases, but may also occur by intra-molecular ...
The active site consists of amino acid residues that form temporary bonds with the substrate, the binding site, and residues that catalyse a reaction of that substrate, the catalytic site. Although the active site occupies only ~10–20% of the volume of an enzyme, [ 1 ] : 19 it is the most important part as it directly catalyzes the chemical ...
The structure of chymotrypsin was solved by X-ray crystallography in the 1960s, showing the orientation of the catalytic triad in the active site. [8] Other proteases were sequenced and aligned to reveal a family of related proteases, [9] [10] [11] now called the S1 family.
Oxyanion hole of a serine protease (black) stabilises negative charge build-up on the transition state of the substrate (red) using hydrogen bonds from enzyme's backbone amides (blue). An oxyanion hole is a pocket in the active site of an enzyme that stabilizes transition state negative charge on a deprotonated oxygen or alkoxide. [1]
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 ...