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  2. Cathepsin E - Wikipedia

    en.wikipedia.org/wiki/Cathepsin_E

    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.

  3. Protein Data Bank - Wikipedia

    en.wikipedia.org/wiki/Protein_Data_Bank

    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 ...

  4. Sterol regulatory element-binding protein 2 - Wikipedia

    en.wikipedia.org/wiki/Sterol_regulatory_element...

    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 ...

  5. Cathepsin B - Wikipedia

    en.wikipedia.org/wiki/Cathepsin_B

    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.

  6. Cathepsin - Wikipedia

    en.wikipedia.org/wiki/Cathepsin

    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 ]

  7. Alpha/beta hydrolase superfamily - Wikipedia

    en.wikipedia.org/wiki/Alpha/beta_hydrolase_super...

    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 .

  8. Cathepsin D - Wikipedia

    en.wikipedia.org/wiki/Cathepsin_D

    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 ...

  9. Papain-like protease - Wikipedia

    en.wikipedia.org/wiki/Papain-like_protease

    [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 ...