Wright H T
Dept. of Biochemistry and Molecular Biophysics, Virginia Commonwealth University, Richmond 23298-0614.
Crit Rev Biochem Mol Biol. 1991;26(1):1-52. doi: 10.3109/10409239109081719.
Some asparagine and glutamine residues in proteins undergo deamidation to aspartate and glutamate with rates that depend upon the sequence and higher-order structure of the protein. Functional groups within the protein can catalyze this reaction, acting as general acids, bases, or stabilizers of the transition state. Information from specific proteins that deamidate and analysis of protein sequence and structure data bases suggest that asparagine and glutamine lability has been a selective pressure in the evolution of protein sequence and folding. Asparagine and glutamine deamidation can affect protein structure and function in natural and engineered mutant sequences, and may play a role in the regulation of protein folding, protein breakdown, and aging.
蛋白质中的一些天冬酰胺和谷氨酰胺残基会发生脱酰胺反应，生成天冬氨酸和谷氨酸，其反应速率取决于蛋白质的序列和高级结构。蛋白质中的官能团可催化此反应，充当一般酸、碱或过渡态稳定剂。来自特定脱酰胺蛋白质的信息以及对蛋白质序列和结构数据库的分析表明，天冬酰胺和谷氨酰胺的不稳定性在蛋白质序列进化和折叠过程中一直是一种选择压力。天冬酰胺和谷氨酰胺脱酰胺可影响天然和工程突变序列中的蛋白质结构与功能，可能在蛋白质折叠、蛋白质降解及衰老调控中发挥作用。
