Abstract
Homocysteine thiolactone is a five-membered cyclic thioester of amino acid homocysteine. It is generated from homocysteine as a result of an error-editing reaction, principally, of methionyl-tRNA synthetase. An elevated level of homocysteine thiolactone is associated with cardiovascular diseases, strokes, atherosclerosis, neurological abnormalities, etc., presumably because it reacts to the side chain of protein lysine causing protein damage and autoimmune responses. It is not only an important metabolite but also a versatile building block for organic and bioorganic synthesis. This entry contains data on the homocysteine thiolactone formation, metabolism, toxicity mechanism in vivo, and the bioorganic chemistry applications as a powerful synthetic tool in polymer science, sustainable materials development, and probes.
Highlights
Homocysteine thiolactone (HTL), its and discovery in theory living of cells and the Hcy and cardiovascular diseases to intensive investigations of intensive its possible reactions with theory of arteriosclerosis andlead cardiovascular diseases lead to investigations of proteins (Figure its possible reactions with proteins (Figure 4)
It will lead to a lot of applications in many areas such as polymer synthesis, material science, and pharmacology
Biomolecules modification by HTL and its derivatives is a vast field of research because thiols are involved in almost all physiological processes
Summary
Homocysteine (Hcy) is a non-protein amino acid that is an important risk factor for arteriosclerosis, Alzheimer’s disease, cardiovascular disease, ischemic heart disease, stroke, cancer, diabetic retinopathy, and diseases of the central nervous system in humans [1,2,3,4,5,6,7,8,9,10,11,12]. Hcy takes part in many fundamental processes in the human organism It is formed in the methionine cycle as an intermediate by hydrolysis of S-adenosylhomocysteine to Hcy and adenosine (Figure 1). The first reaction is the vitamins-dependent remethylation by methionine synthase (MS). The N-5-methyl tetrahydrofolate can donate a methyl group to Hcy in a reaction catalyzed by the vitamin. The reaction presumably occurs in the liver, kidney, and lens, whereas the first vitamin-dependent route is found in all tissues. The cystathionine is further hydrolyzed to Cys and α-ketobutyrate by cystathionine γ-lyase (CSE) These two reactions are catalyzed by the vitamin B6 -dependent enzymes (CSE and CBS). These two reactions are catalyzed by the vitamin. The Hcy detoxification through the transsulfurathrough the transsulfuration pathway occurs in the liver, kidney, small intestine, and lens.
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