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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.
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 .
As of February 2015, SCOPe 2.05 classified 71,000 of the 110,000 total PDB entries. [ 11 ] SCOP2 prototype was a beta version of Structural classification of proteins and classification system that aimed to more the evolutionary complexity inherent in protein structure evolution. [ 12 ]
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 ...
[1] [2] Cancer, Cathepsin D is a mitogen and "it attenuates the anti-tumor immune response of decaying chemokines to inhibit the function of dendritic cells". Cathepsins B and L are involved in matrix degradation and cell invasion. [3]
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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 ...