反硫化
半胱氨酸
胱硫醚β合酶
生物化学
化学
同型半胱氨酸
半胱氨酸代谢
转甲基
蛋氨酸
谷胱甘肽
丝氨酸
钼辅因子
胱硫醚γ裂解酶
硫代谢
辅酶A
分解代谢
蛋氨酸合酶
新陈代谢
辅因子
氨基酸
酶
还原酶
作者
Sebastián Carballal,Ruma Banerjee
出处
期刊:Elsevier eBooks
[Elsevier]
日期:2022-01-01
卷期号:: 423-450
被引量:10
标识
DOI:10.1016/b978-0-323-90219-9.00016-9
摘要
In mammals, cysteine can be obtained from the diet or via recycling of protein and glutathione (GSH). In addition, cysteine can be synthesized from serine and methionine-derived homocysteine through the transsulfuration pathway. This pathway intersects with the methionine cycle, which supports transmethylation reactions and forms homocysteine as a key intermediate. The transsulfuration pathway leads to the irreversible commitment of the sulfur group of homocysteine to cysteine synthesis by the action of cystathionine β-synthase (CBS) and γ-cystathionase (CSE). Cysteine is catabolized either by desulfuration or oxidation. The products of cysteine catabolism are taurine, pyruvate, H2S, sulfate, and thiosulfate. In addition, cysteine is used in protein synthesis and serves as a precursor and sulfur source for metabolites including GSH and coenzyme A (CoA). In proteins, reversible oxidation or covalent posttranslational modification of cysteines including sulfenylation, thiolation, disulfide formation, nitrosation, persulfidation, prenylation, and acylation, are postulated to be involved in redox-dependent signaling and/or regulation of protein function.
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