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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.
162,041 structures in the PDB have a structure factor file. 11,242 structures have an NMR restraint file. 5,774 structures in the PDB have a chemical shifts file. 13,388 structures in the PDB have a 3DEM map file deposited in EM Data Bank. Most structures are determined by X-ray diffraction, but about 7% of structures are determined by protein ...
20788 Ensembl ENSG00000198911 ENSMUSG00000022463 UniProt Q12772 Q3U1N2 RefSeq (mRNA) NM_004599 NM_033218 RefSeq (protein) NP_004590 NP_150087 Location (UCSC) Chr 22: 41.83 – 41.91 Mb Chr 15: 82.03 – 82.09 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Sterol regulatory element-binding protein 2 (SREBP-2) also known as sterol regulatory element binding transcription factor 2 ...
Cathepsin B may enhance the activity of other proteases, including matrix metalloproteinase, urokinase (serine protease urokinase plasminogen activator), and cathepsin D, [16] [17] and thus it has an essential position for the proteolysis of extracellular matrix components, intercellular communication disruption, and reduced protease inhibitor expression.
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 alpha/beta hydrolase superfamily is a superfamily of hydrolytic enzymes of widely differing phylogenetic origin and catalytic function that share a common fold. [1] The core of each enzyme is an alpha/beta-sheet (rather than a barrel ), containing 8 beta strands connected by 6 alpha helices .
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 ...
[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 ...