Modification of Escherichia coli DNA ligase by cleavage with trypsin

Autor:	I. R. Lehman, S M Panasenko, Paul Modrich
Rok vydání:	1976
Předmět:	chemistry.chemical_classification DNA ligase Cell Biology Trypsin Cleavage (embryo) Biochemistry chemistry.chemical_compound Enzyme chemistry Covalent bond Phosphodiester bond medicine Molecule Molecular Biology DNA medicine.drug
Zdroj:	Scopus-Elsevier
ISSN:	0021-9258
DOI:	10.1016/s0021-9258(17)33456-7
Popis:	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.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b176cc4cdba4fcd74dfdb42cff7a5a8a https://doi.org/10.1016/s0021-9258(17)33456-7 Zobrazit plný text záznamu