Modification of Escherichia coli DNA ligase by cleavage with trypsin.
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.
D004926:Escherichia coli / Q000201:enzymology*; D009243:NAD; D009537:Nicotinamide Mononucleotide; D010446:Peptide Fragments / Q000378:metabolism; D011118:Polynucleotide Ligases / Q000378:metabolism; D014357:Trypsin
D010446:Peptide Fragments; D009243:NAD; D009537:Nicotinamide Mononucleotide; D014357:Trypsin; D011118:Polynucleotide Ligases