Search results
Results from the WOW.Com Content Network
Homocysteine thiolactone (HTL) is an organosulfur compound with the formula H 2 NCHC(O)SCH 2 CH 2. It is the thiolactone (intramolecular thioester ) of homocysteine . It is produced by methionyl-tRNA synthetase in an error-editing reaction that prevents translational incorporation of homocysteine into proteins .
Homocysteine can cyclize to give homocysteine thiolactone, a five-membered heterocycle. Because of this "self-looping" reaction, homocysteine-containing peptides tend to cleave themselves by reactions generating oxidative stress. [12] Homocysteine also acts as an allosteric antagonist at Dopamine D 2 receptors. [13]
The activation of the drug clopidogrel (top left) gives a thiolactone, which ring-opens. [3] Thiolactones are intermediates in the activation of some drugs. [4] In nature, the most common thiolactone is homocysteine thiolactone. It is produced from homocysteine. It may play a role in protein damage. [5]
Reaction 5 is catalyzed by cystathionine beta-synthase while reaction 6 is catalyzed by cystathionine gamma-lyase. The required homocysteine is synthesized from methionine in reactions 1, 2, and 3. The transsulfuration pathway is a metabolic pathway involving the interconversion of cysteine and homocysteine through the intermediate cystathionine .
Transmethylation is a biologically important organic chemical reaction in which a methyl group is transferred from one compound to another. An example of transmethylation is the recovery of methionine from homocysteine. In order to sustain sufficient reaction rates during metabolic stress, this reaction requires adequate levels of vitamin B 12 ...
Consequently, a thermochemical cycle with i steps can be defined as sequence of i reactions equivalent to water-splitting and satisfying equations (4), (5) and (10). The key point to remember in that case is that the process temperature T H can theoretically be arbitrary chosen (1000K as a reference in most of the past studies, for high ...
In humans it is encoded by the MTR gene (5-methyltetrahydrofolate-homocysteine methyltransferase). [5] [6] Methionine synthase forms part of the S-adenosylmethionine (SAMe) biosynthesis and regeneration cycle, [7] and is the enzyme responsible for linking the cycle to one-carbon metabolism via the folate cycle.
The structure of vitamin B 12 was the first low-molecular weight natural product determined by x-ray analysis rather than by chemical degradation. Thus, while the structure of this novel type of complex biomolecule was established, its chemistry remained essentially unknown; exploration of this chemistry became one of the tasks of the vitamin's chemical synthesis.