Structure of the DNA Ligase-Adenylate Intermediate: Lysine (ɛ -amino)-Linked Adenosine Monophosphoramidate
Abstract
Proteolytic degradation of the Escherichia coli DNA ligase-adenylate intermediate releases adenosine 5‧-monophosphate linked to the ɛ-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 (ɛ-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 ɛ-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 (ɛamino)-linked adenosine monophosphoramidate.
- Publication:
-
Proceedings of the National Academy of Science
- Pub Date:
- October 1971
- DOI:
- 10.1073/pnas.68.10.2559
- Bibcode:
- 1971PNAS...68.2559G