ATP-dependent DNA ligase from bacteriophage T7: Difference between revisions

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William Guthrie, Jeremy A. Hammett, Hunter Douglas, Jaime Prilusky

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	==Overview (General Function)==		==Overview (General Function)==

	ATP-dependent DNA ligase from bacteriophage T7 (Caudovirales Podoviridae) is used to catalyze a phosphodiester bond between single-strand nicks in double-stranded DNA. This occurs in replication (connecting okazaki fragments), DNA repair (excision repair), and recombination. DNA ligases require either ATP (eukaryotes and viruses) or NAD+ (prokaryotes) as a cofactor. All ligases require a divalent cation for function. Bacteriophage T7 DNA ligase uses Magnesium in vivo. A range of pH 7.2-7.7 is ideal for enzymatic activity. T7 ligase has a molecular weight of 41 kDa.		ATP-dependent DNA ligase from bacteriophage T7 (Caudovirales Podoviridae) is used to catalyze a phosphodiester bond between single-strand nicks in double-stranded DNA. This occurs in replication (connecting okazaki fragments)<ref name="Berg">Berg, Jeremy M, Stryer, Lubert, Tymoczko, John L. ''Biochemistry.'' Sixth edition. New York: W.H. Freeman and Company, 2007: 796. Print.</ref>, DNA repair (excision repair), and recombination. DNA ligases require either ATP (eukaryotes and viruses) or NAD+ (prokaryotes) as a cofactor. All ligases require a divalent cation for function. Bacteriophage T7 DNA ligase uses Magnesium in vivo. A range of pH 7.2-7.7 is ideal for enzymatic activity. T7 ligase has a molecular weight of 41 kDa.