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Pentamidine is an antimicrobial medication used to treat African trypanosomiasis, leishmaniasis, Balamuthia infections, [2] babesiosis, and to prevent and treat pneumocystis pneumonia (PCP) in people with poor immune function. [1]
Phenethylamine is a potent agonist of the mouse, rat, and human trace amine-associated receptor 1 (TAAR1). [43] [2] β-PEA is also an odorant binding TAAR4 in mice thought to mediate predator avoidance. [44] Similarly to the case of amphetamine, phenethylamine shows enhanced locomotor stimulation, a psychostimulant-like effect, in TAAR1 ...
The nAChRs are thought to be hetero-pentamers composed of homologous subunits. The proposed structure for each subunit is a conserved N-terminal extracellular domain followed by three conserved transmembrane domains, a variable cytoplasmic loop, a fourth conserved transmembrane domain, and a short C-terminal extracellular region.
Furthermore, the preceding sequence Gln-Gly-Gln-Cys is conserved in both isozymes for both human and horse, which is consistent with Cys-302 being crucial to catalytic function. [2] As discovered by site-directed mutagenesis, glutamate-268 is a key component of liver acetaldehyde dehydrogenase and is also critical to catalytic activity. Since ...
Venenivibrio stagnispumantis gains energy by oxidizing hydrogen gas.. In biochemistry, chemosynthesis is the biological conversion of one or more carbon-containing molecules (usually carbon dioxide or methane) and nutrients into organic matter using the oxidation of inorganic compounds (e.g., hydrogen gas, hydrogen sulfide) or ferrous ions as a source of energy, rather than sunlight, as in ...
Humans have at least six slightly different alcohol dehydrogenases. Each is a dimer (i.e., consists of two polypeptides ), with each dimer containing two zinc ions Zn 2+ . One of those ions is crucial for the operation of the enzyme: It is located at the catalytic site and holds the hydroxyl group of the alcohol in place.
3-Methyl-2-pentanone (methyl sec-butyl ketone) is an aliphatic ketone and isomer of 2-hexanone. [2] References This page was last edited on 17 November 2024, at 23: ...
The structure of 40-42 kDa porphobilinogen deaminase, which is highly conserved amongst organisms, consists of three domains. [5] [6] Domains 1 and 2 are structurally very similar: each consisting of five beta-sheets and three alpha helices in humans. [7] Domain 3 is positioned between the other two and has a flattened beta-sheet geometry.