半胱氨酸
化学
氧化还原
残留物(化学)
二硫键
硫醇
氨基酸
亲核细胞
生物化学
半胱氨酸代谢
氨基酸残基
组合化学
生物物理学
催化作用
肽序列
生物
酶
有机化学
基因
标识
DOI:10.1016/j.freeradbiomed.2014.11.013
摘要
Cysteine is one of the least abundant amino acids, yet it is frequently found as a highly conserved residue within functional (regulatory, catalytic, or binding) sites in proteins. It is the unique chemistry of the thiol or thiolate group of cysteine that imparts to functional sites their specialized properties (e.g., nucleophilicity, high-affinity metal binding, and/or ability to form disulfide bonds). Highlighted in this review are some of the basic biophysical and biochemical properties of cysteine groups and the equations that apply to them, particularly with respect to pKa and redox potential. Also summarized are the types of low-molecular-weight thiols present in high concentrations in most cells, as well as the ways in which modifications of cysteinyl residues can impart or regulate molecular functions important to cellular processes, including signal transduction.
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