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Taurine (/ ˈ t ɔː r iː n /), or 2-aminoethanesulfonic acid, is a non-proteinogenic naturally occurring amino sulfonic acid that is widely distributed in animal tissues. [1] It is a major constituent of bile and can be found in the large intestine, and accounts for up to 0.1% of total human body weight.
Hypotaurine is a sulfinic acid that is an intermediate in the biosynthesis of taurine. Like taurine, it also acts as an endogenous neurotransmitter via action on the glycine receptors. [1] It is an osmolyte with antioxidant properties. [2] Hypotaurine is derived from cysteine (and homocysteine). In mammals, the biosynthesis of hypotaurine from ...
The synthesis of N-methyltaurine was reported as early as 1878, [4] with methylamine being reacted with the silver salt of 2-chloroethanesulfonic acid. An obvious modification for this reaction is the replacement of the silver salt of 2-chloroethanesulfonic acid by the sodium salt of 2-chloroethanesulfonic acid. [5]
In the decomposition of taurine, it has been shown that molecular oxygen is activated by Iron II, which lies in the coordinating complex of taurine dioxygenase. [2] Here the enzyme with conjunction of an Iron II and 2-oxoglutarate maintain non-covalent bonds by electrostatic interactions, and coordinate a nucleophilic attack from dioxygen on 2-oxoglutarate carbon number 2. [3]
In enzymology, a taurine dehydrogenase (EC 1.4.99.2) is an enzyme that catalyzes the chemical reaction.. taurine + H 2 O + acceptor sulfoacetaldehyde + NH 3 + reduced acceptor. The 3 substrates of this enzyme are taurine, H 2 O, and acceptor, whereas its 3 products are sulfoacetaldehyde, NH 3, and reduced acceptor.
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The Escherichia coli tauD gene is required for the utilization of taurine (2-aminoethanesulfonic acid) as a sulfur source and is expressed only under conditions of sulfate starvation. TauD is an alpha-ketoglutarate-dependent dioxygenase catalyzing the oxygenolytic release of sulfite from taurine. [ 1 ]
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