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Cathepsin E is an enzyme (EC 3.4.23.34) that in humans is encoded by the CTSE gene. [5] [6] [7] The enzyme is also known as slow-moving proteinase, erythrocyte membrane aspartic proteinase, SMP, EMAP, non-pepsin proteinase, cathepsin D-like acid proteinase, cathepsin E-like acid proteinase, cathepsin D-type proteinase) is an enzyme. [8] [9] [10 ...
Cathepsin B may function as a beta-secretase 1, cleaving amyloid precursor protein to produce amyloid beta. [10] Overexpression of the encoded protein, which is a member of the peptidase C1 family, has been associated with esophageal adenocarcinoma and other tumors. [ 11 ]
The catalytic sites of cathepsin D include two critical aspartic residues (amino acid 33 and 231) located on the 14 kDa and 34kDa chains. [11] The ultimate form of mature cathepsin D is composed of 337 amino acid residues, 196 amino acid residues in the heavy chain and 141 in the light chain. These two chains are linked by the hydrophobic ...
The 3C-like protease (3CL pro) or main protease (M pro), formally known as C30 endopeptidase or 3-chymotrypsin-like protease, [2] is the main protease found in coronaviruses.It cleaves the coronavirus polyprotein at eleven conserved sites.
[3] [10] [9] Many papain-like protease enzymes function as monomers, though a few, such as cathepsin C (Dipeptidyl-peptidase I), are homotetramers. The mature monomer structure is characteristically divided into two lobes or subdomains, known as the L-domain ( N-terminal ) and the R-domain ( C-terminal ), where the active site is located ...
The PDBbind database is a comprehensive collection of experimentally measured binding affinity data (Kd, Ki, and IC50) for the protein-ligand complexes deposited in the Protein Data Bank (PDB). [ 1 ] [ 2 ] It thus provides a link between energetic and structural information of protein-ligand complexes, which is of great value to various studies ...
Serine protease, as released by mast cells, is an important diagnostic marker for type 1 hypersensitivity reactions e.g., anaphylaxis. More useful than histamine due to the longer half-life , meaning it remains in the system for a clinically useful length of time.
Cathepsin S is a protein that in humans is encoded by the CTSS gene. [5] Transcript variants utilizing alternative polyadenylation signals exist for this gene. [5]Cathepsin S is a member of the peptidase C1 family of cysteine cathepsins, a lysosomal cysteine protease that may participate in the degradation of antigenic proteins to peptides for presentation to the MHC class II.