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The result of this sequential cascade is to bind ubiquitin to lysine residues on the protein substrate via an isopeptide bond, cysteine residues through a thioester bond; serine, threonine, and tyrosine residues through an ester bond; or the amino group of the protein's N-terminus via a peptide bond. [7] [8] [9] [10]
590 12038 Ensembl ENSG00000114200 ENSMUSG00000027792 UniProt P06276 Q03311 RefSeq (mRNA) NM_000055 NM_009738 RefSeq (protein) NP_000046 NP_033868 Location (UCSC) Chr 3: 165.77 – 165.84 Mb Chr 3: 73.54 – 73.62 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Butyrylcholinesterase (HGNC symbol BCHE ; EC 3.1.1.8), also known as BChE, BuChE, BuChase, pseudocholinesterase, or plasma ...
Cells will use this phosphatidylserine to enter cells via apoptotic mimicry. The structure of this lipid differs in plants and animals, regarding fatty acid composition. In addition, phosphatidylserine plays an important role in the human brain content, as it makes up 13–15% of the phospholipids in the human cerebral cortex.
In biochemistry, an esterase is a class of enzyme that splits esters into an acid and an alcohol in a chemical reaction with water called hydrolysis (and as such, it is a type of hydrolase). A wide range of different esterases exist that differ in their substrate specificity, their protein structure , and their biological function.
Protein primary structure is the linear sequence of amino acids in a peptide or protein. [1] By convention, the primary structure of a protein is reported starting from the amino-terminal (N) end to the carboxyl-terminal (C) end. Protein biosynthesis is most commonly performed by ribosomes in cells. Peptides can also be synthesized in the ...
Furthermore, the TetM protein is found to allow aminoacyl-tRNA molecules to bind to the ribosomal acceptor site, despite being concentrated with tetracyclines that would typically inhibit such actions. The TetM protein is regarded as a ribosomal protection protein, exhibiting GTPase activity that is dependent upon ribosomes.
Glycine is integral to the formation of alpha-helices in secondary protein structure due to the "flexibility" caused by such a small R group. Glycine is also an inhibitory neurotransmitter [ 9 ] – interference with its release within the spinal cord (such as during a Clostridium tetani infection) can cause spastic paralysis due to uninhibited ...
Retinal pigment epithelium-specific 65 kDa protein (also known as RPE65) is a retinoid isomerohydrolase enzyme of the vertebrate visual cycle. [5] [6] RPE65 is expressed in the retinal pigment epithelium (RPE, a layer of epithelial cells that nourish the photoreceptor cells) and is responsible for the conversion of all-trans-retinyl esters to 11-cis-retinol during phototransduction.