期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1971
卷号：68
期号：10
页码：2559-2563
DOI：10.1073/pnas.68.10.2559
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：Proteolytic degradation of the Escherichia coli DNA ligase-adenylate intermediate releases adenosine 5'-monophosphate linked to the {varepsilon}-amino group of lysine by a phosphoamide bond. Measurements of the rate of hydroxylaminolysis of the ligase-adenylate provide further support for a phosphoamide linkage in the native enzyme. Lysine ({varepsilon}-amino)-linked adenosine monophosphoramidate has also been isolated from the T4 phage-induced ligase-adenylate intermediate. These results indicate that an initial step of the DNA ligase reaction consists of the nucleophilic attack of the {varepsilon}-amino group of a lysine residue of the enzyme on the adenylyl phosphorus of DPN or ATP that leads to the formation of enzyme-bound lysine ({varepsilon}amino)-linked adenosine monophosphoramidate.
关键词：nucleotidyl group transfer ; covalent catalysis ; phosphoamides ; T4 phage ; E. coli
