Nonenzymatic deamidation of asparaginyl and glutaminyl residues in proteins.
Nonenzymatic deamidation of asparaginyl and glutaminyl residues in proteins.
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DOI：
10.3109/10409239109081719
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发表时间：
1991
影响因子：
6.5
通讯作者：
H. Wright;D. Urry
中科院分区：
文献类型：
--
作者：
H. Wright;D. Urry
蛋白质中的一些天冬酰胺和谷氨酰胺残基经历脱酰胺化为天冬氨酸和谷氨酸，其速率取决于蛋白质的序列和高级结构。蛋白质内的官能团可以催化该反应，充当一般的酸、碱或过渡态的稳定剂。通过对脱酰胺蛋白质的研究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是蛋白质序列和折叠进化中的一种选择压力。天冬酰胺和谷氨酰胺脱酰胺可以影响天然和工程突变序列中的蛋白质结构和功能，并且可以在蛋白质折叠、蛋白质分解和老化的调节中发挥作用。
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.