Modification of Escherichia coli DNA ligase by cleavage with trypsin.


Journal Article

Limited treatment of Escherichia coli DNA ligase with trypsin results in rapid loss of DNA joining activity. However, the ability to react with DPN to form the covalent enzyme-AMP intermediate is unaffected. The cleaved enzyme is also unable to catalyze the formation of DNA-adenylate, the second covalent intermediate in the ligase-catalyzed reaction. These findings demonstrate that portions of the DNA ligase molecule that are required for phosphodiester bond formation are not required for at least one of the partial reactions catalyzed by this enzyme.

Full Text

Duke Authors

Cited Authors

  • Panasenko, SM; Modrich, P; Lehman, IR

Published Date

  • June 10, 1976

Published In

Volume / Issue

  • 251 / 11

Start / End Page

  • 3432 - 3435

PubMed ID

  • 179997

Pubmed Central ID

  • 179997

International Standard Serial Number (ISSN)

  • 0021-9258


  • eng

Conference Location

  • United States