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. 1971 Oct;68(10):2559–2563. doi: 10.1073/pnas.68.10.2559

Structure of the DNA Ligase-Adenylate Intermediate: Lysine (ε-amino)-Linked Adenosine Monophosphoramidate*

Richard I Gumport 1,†, I R Lehman 1
PMCID: PMC389468  PMID: 4944632

Abstract

Proteolytic degradation of the Escherichia coli DNA ligase-adenylate intermediate releases adenosine 5′-monophosphate linked to the ε-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 (ε-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 ε-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 (εamino)-linked adenosine monophosphoramidate.

Keywords: nucleotidyl group transfer, covalent catalysis, phosphoamides, T4 phage, E. coli

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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