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Literature summary extracted from

  • Lindahl, T.; Barnes, D.E.
    Mammalian DNA ligases (1992), Annu. Rev. Biochem., 61, 251-281.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
6.5.1.1 bovine serum albumin stimulates Mammalia
6.5.1.1 additional information human fibroblast line GM1492, but not several related fibroblast lines, expresses substantial amounts of a heat-stable protease-sensitive factor, which stimulates calf thymus DNA ligase I Mammalia
6.5.1.1 phosphate DNA ligase I is a phosphoprotein, dephosphorylation causes drastic reduction in enzyme activity Mammalia

Cloned(Commentary)

EC Number Cloned (Comment) Organism
6.5.1.1
-
 Drosophila melanogaster
6.5.1.1
-
 Saccharomyces cerevisiae
6.5.1.1
-
 Schizosaccharomyces pombe
6.5.1.1 amino acid sequence of human DNA ligase I and enzyme from Schizosaccharomyces pombe are virtually identical in the region of the active site, although the two enzymes show only 44% overall identity. The sequence of DNA ligase II appears to be quite different from that of DNA ligase I Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
6.5.1.1 R771W Arg771-Trp mutation in DNA ligase I of cell line 46BR defective in DNA ligase I accounts for the malfunctioning but partly active enzyme present in 46BR cells that allows cell proliferation Homo sapiens

General Stability

EC Number General Stability Organism
6.5.1.1 DNA ligase I is highly sensitive to partial proteolysis Mammalia
6.5.1.1 Tween 20, 0.2% or bovine serum albumin stabilizes Mammalia
6.5.1.1 very susceptible to proteolysis Drosophila melanogaster

Inhibitors

EC Number Inhibitors Comment Organism Structure
6.5.1.1 Arabinosyl-2-fluoro-ATP
-
 Mammalia
6.5.1.1 additional information dephosphorylation causes drastic reduction in enzyme activity Mammalia
6.5.1.1 additional information
-
 Rattus norvegicus
6.5.1.1 additional information
-
 Vaccinia virus
6.5.1.1 pyridoxal 5'-phosphate DNA ligase I Mammalia

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.5.1.1 0.0005 0.001 ATP DNA ligase I Mammalia
6.5.1.1 0.0016
-
 ATP
-
 Drosophila melanogaster
6.5.1.1 0.0016
-
 ATP
-
 Homo sapiens
6.5.1.1 0.01 0.1 ATP DNA ligase II Mammalia

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
6.5.1.1 nucleus
-
 Drosophila melanogaster 5634
-
6.5.1.1 nucleus
-
 Homo sapiens 5634
-
6.5.1.1 nucleus
-
 Bos taurus 5634
-
6.5.1.1 nucleus DNA ligase I, II and III. DNA ligase I is more firmly associated with the nucleus than DNA ligase I. DNA ligase III is associated with the condensed chromatin that is present from anaphase to telophase Mammalia 5634
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.5.1.1 Mg2+ required Mammalia
6.5.1.1 Mg2+ required Homo sapiens
6.5.1.1 Mg2+ required Rattus norvegicus
6.5.1.1 Mg2+ required Bos taurus
6.5.1.1 Mg2+ required Tequatrovirus T4

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
6.5.1.1 additional information
-
 DNA ligase I, and II have a markedly asymetric structure, gel filtration data lead to a gross overestimation of the MW Mammalia
6.5.1.1 46000
-
 1 * 46000 + 1 * 100000, DNA ligase III, SDS-PAGE. It cannot be concluded whether the 46000 MW peptide is an essential and integral part of DNA ligase III, or if it represents a separate protein that binds tentaciously to the 100000 MW DNA ligase component Mammalia
6.5.1.1 61000
-
 enzyme-adenylate complex Vaccinia virus
6.5.1.1 100000
-
 1 * 46000 + 1 * 100000, DNA ligase III, SDS-PAGE. It cannot be concluded whether the 46000 MW peptide is an essential and integral part of DNA ligase III, or if it represents a separate protein that binds tentaciously to the 100000 MW DNA ligase component Mammalia
6.5.1.1 102000
-
 sucrose density gradient centrifugation Mammalia
6.5.1.1 160000
-
-
 Ambystoma mexicanum
6.5.1.1 180000
-
-
 Xenopus laevis
6.5.1.1 180000
-
-
 Pleurodeles sp.

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.5.1.1 ATP + (deoxyribonucleotide)n + (deoxyribonucleotide)m Drosophila melanogaster
-
 ?
-
 ?
6.5.1.1 ATP + (deoxyribonucleotide)n + (deoxyribonucleotide)m Homo sapiens
-
 ?
-
 ?
6.5.1.1 ATP + (deoxyribonucleotide)n + (deoxyribonucleotide)m Saccharomyces cerevisiae
-
 ?
-
 ?
6.5.1.1 ATP + (deoxyribonucleotide)n + (deoxyribonucleotide)m Bos taurus
-
 ?
-
 ?
6.5.1.1 ATP + (deoxyribonucleotide)n + (deoxyribonucleotide)m Tequatrovirus T4
-
 ?
-
 ?
6.5.1.1 ATP + (deoxyribonucleotide)n + (deoxyribonucleotide)m Vaccinia virus nonessential for viral DNA replication and growth on several types of host cells. DNA ligase I participates in DNA base excision repair as a component of a multiprotein complex ?
-
 ?
6.5.1.1 ATP + (deoxyribonucleotide)n + (deoxyribonucleotide)m Mammalia DNA ligase I is the key enzyme for joining Okazaki fragments during lagging-strand DNA synthesis in mammalian cells and also for completion of DNA excision repair processes ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
6.5.1.1 Ambystoma mexicanum
-
 axolotl
-
6.5.1.1 Bos taurus
-
 calf
-
6.5.1.1 Bos taurus
-
 DNA ligase I, II
-
6.5.1.1 Drosophila melanogaster
-
 DNA ligase I and II
-
6.5.1.1 Homo sapiens
-
 DNA ligase I
-
6.5.1.1 Mammalia
-
 DNA ligase I, II, and III
-
6.5.1.1 Pleurodeles sp.
-
-
-
6.5.1.1 Rattus norvegicus
-
-
-
6.5.1.1 Saccharomyces cerevisiae
-
-
-
6.5.1.1 Schizosaccharomyces pombe
-
-
-
6.5.1.1 Tequatrovirus T4
-
-
-
6.5.1.1 Vaccinia virus
-
-
-
6.5.1.1 Xenopus laevis
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
6.5.1.1
-
 Bos taurus
6.5.1.1
-
 Pleurodeles sp.
6.5.1.1
-
 Ambystoma mexicanum
6.5.1.1 DNA ligase I, DNA ligase II partial Drosophila melanogaster
6.5.1.1 DNA ligase II Drosophila melanogaster

Reaction

EC Number Reaction Comment Organism Reaction ID
6.5.1.1 ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate mechanism: 1. formation of a covalent enzyme-adenylate complex, the ATP is cleaved to AMP and diphosphate with adenylyl residue linked by a phosphoramidate bond to the epsilon-amino group of a specific lysine residue at the active site of the protein, 2. the activated AMP residue of the DNA ligase-adenylate intermediate is transferred to the 5'-phosphate terminus of a single strand break in double-stranded DNA to generate a covalent DNA-AMP complex with a 5'-5' phosphoanhydride bond, 3. in the final step of DNA ligation, unadenylated DNA ligase is required for the generation of a phosphodiester bond and catalyzes displacement of the AMP residue through attack by adjacent 3'-hydroxyl group of the adenylylated site Mammalia
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining
6.5.1.1 egg 10fold lower activity in adult tissues than in eggs Xenopus laevis
-
6.5.1.1 egg unfertilized, high activity of DNA ligase Drosophila melanogaster
-
6.5.1.1 egg unfertilized, high activity of DNA ligase Xenopus laevis
-
6.5.1.1 egg unfertilized, high activity of DNA ligase Pleurodeles sp.
-
6.5.1.1 egg unfertilized, high activity of DNA ligase Ambystoma mexicanum
-
6.5.1.1 embryo
-
 Drosophila melanogaster
-
6.5.1.1 embryo
-
 Xenopus laevis
-
6.5.1.1 liver
-
 Rattus norvegicus
-
6.5.1.1 lymphoblast
-
 Mammalia
-
6.5.1.1 additional information DNA ligase I correlates well with changes in DNA replication during development, the level of DNA ligase II activity does not change significantly between different developmental stages Drosophila melanogaster
-
6.5.1.1 oocyte
-
 Xenopus laevis
-
6.5.1.1 thymus
-
 Bos taurus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.5.1.1 ATP + (deoxyribonucleotide)n + (deoxyribonucleotide)m DNA ligase I: performs blunt end ligation of DNA in presence of glycol, can ligate (rA)*poly(dT) hybrid substrate, unable to join oligo(rA)*poly(rU), unable to join oligo(dT)*poly(rA) Drosophila melanogaster AMP + diphosphate + (deoxyribonucleotide)n+m
-
 ?
6.5.1.1 ATP + (deoxyribonucleotide)n + (deoxyribonucleotide)m DNA ligase III: repairs single-strand breaks in DNA, but is unable to perform either blunt end ligation or AMP-dependent relaxation of supercoiled DNA. The enzyme can join both the oligo(dT)*poly(rA) and oligo(rA)*poly(dT) hybrid substrates Drosophila melanogaster AMP + diphosphate + (deoxyribonucleotide)n+m
-
 ?
6.5.1.1 ATP + (deoxyribonucleotide)n + (deoxyribonucleotide)m DNA ligase III: repairs single-strand breaks in DNA, but is unable to perform either blunt end ligation or AMP-dependent relaxation of supercoiled DNA. The enzyme can join both the oligo(dT)*poly(rA) and oligo(rA)*poly(dT) hybrid substrates Mammalia AMP + diphosphate + (deoxyribonucleotide)n+m
-
 ?
6.5.1.1 ATP + (deoxyribonucleotide)n + (deoxyribonucleotide)m DNA ligase III: repairs single-strand breaks in DNA, but is unable to perform either blunt end ligation or AMP-dependent relaxation of supercoiled DNA. The enzyme can join both the oligo(dT)*poly(rA) and oligo(rA)*poly(dT) hybrid substrates Homo sapiens AMP + diphosphate + (deoxyribonucleotide)n+m
-
 ?
6.5.1.1 ATP + (deoxyribonucleotide)n + (deoxyribonucleotide)m DNA ligase III: repairs single-strand breaks in DNA, but is unable to perform either blunt end ligation or AMP-dependent relaxation of supercoiled DNA. The enzyme can join both the oligo(dT)*poly(rA) and oligo(rA)*poly(dT) hybrid substrates Rattus norvegicus AMP + diphosphate + (deoxyribonucleotide)n+m
-
 ?
6.5.1.1 ATP + (deoxyribonucleotide)n + (deoxyribonucleotide)m DNA ligase III: repairs single-strand breaks in DNA, but is unable to perform either blunt end ligation or AMP-dependent relaxation of supercoiled DNA. The enzyme can join both the oligo(dT)*poly(rA) and oligo(rA)*poly(dT) hybrid substrates Saccharomyces cerevisiae AMP + diphosphate + (deoxyribonucleotide)n+m
-
 ?
6.5.1.1 ATP + (deoxyribonucleotide)n + (deoxyribonucleotide)m DNA ligase III: repairs single-strand breaks in DNA, but is unable to perform either blunt end ligation or AMP-dependent relaxation of supercoiled DNA. The enzyme can join both the oligo(dT)*poly(rA) and oligo(rA)*poly(dT) hybrid substrates Bos taurus AMP + diphosphate + (deoxyribonucleotide)n+m
-
 ?
6.5.1.1 ATP + (deoxyribonucleotide)n + (deoxyribonucleotide)m DNA ligase III: repairs single-strand breaks in DNA, but is unable to perform either blunt end ligation or AMP-dependent relaxation of supercoiled DNA. The enzyme can join both the oligo(dT)*poly(rA) and oligo(rA)*poly(dT) hybrid substrates Xenopus laevis AMP + diphosphate + (deoxyribonucleotide)n+m
-
 ?
6.5.1.1 ATP + (deoxyribonucleotide)n + (deoxyribonucleotide)m DNA ligase III: repairs single-strand breaks in DNA, but is unable to perform either blunt end ligation or AMP-dependent relaxation of supercoiled DNA. The enzyme can join both the oligo(dT)*poly(rA) and oligo(rA)*poly(dT) hybrid substrates Schizosaccharomyces pombe AMP + diphosphate + (deoxyribonucleotide)n+m
-
 ?
6.5.1.1 ATP + (deoxyribonucleotide)n + (deoxyribonucleotide)m DNA ligase III: repairs single-strand breaks in DNA, but is unable to perform either blunt end ligation or AMP-dependent relaxation of supercoiled DNA. The enzyme can join both the oligo(dT)*poly(rA) and oligo(rA)*poly(dT) hybrid substrates Tequatrovirus T4 AMP + diphosphate + (deoxyribonucleotide)n+m
-
 ?
6.5.1.1 ATP + (deoxyribonucleotide)n + (deoxyribonucleotide)m DNA ligase III: repairs single-strand breaks in DNA, but is unable to perform either blunt end ligation or AMP-dependent relaxation of supercoiled DNA. The enzyme can join both the oligo(dT)*poly(rA) and oligo(rA)*poly(dT) hybrid substrates Pleurodeles sp. AMP + diphosphate + (deoxyribonucleotide)n+m
-
 ?
6.5.1.1 ATP + (deoxyribonucleotide)n + (deoxyribonucleotide)m DNA ligase III: repairs single-strand breaks in DNA, but is unable to perform either blunt end ligation or AMP-dependent relaxation of supercoiled DNA. The enzyme can join both the oligo(dT)*poly(rA) and oligo(rA)*poly(dT) hybrid substrates Ambystoma mexicanum AMP + diphosphate + (deoxyribonucleotide)n+m
-
 ?
6.5.1.1 ATP + (deoxyribonucleotide)n + (deoxyribonucleotide)m DNA ligase III: repairs single-strand breaks in DNA, but is unable to perform either blunt end ligation or AMP-dependent relaxation of supercoiled DNA. The enzyme can join both the oligo(dT)*poly(rA) and oligo(rA)*poly(dT) hybrid substrates Vaccinia virus AMP + diphosphate + (deoxyribonucleotide)n+m
-
 ?
6.5.1.1 ATP + (deoxyribonucleotide)n + (deoxyribonucleotide)m catalyzes blunt end ligation of DNA, cannot join an oligo(dT)*poly(rA) hybrid substrate Xenopus laevis AMP + diphosphate + (deoxyribonucleotide)n+m
-
 ?
6.5.1.1 ATP + (deoxyribonucleotide)n + (deoxyribonucleotide)m joins restriction enzyme DNA fragments with staggered ends. Catalyzes blunt end ligation of DNA, this reaction is stimulated greatly by macromolecular crowding conditions. DNA ligase I is much more effective in blunt end joining than DNA ligase II and III, but is less efficient than T4 DNA ligase. DNA ligase acts at low efficiency as a topoisomerase, relaxing supercoiled DNA in an AMP-dependent reversal of the last step of the ligation reaction, joins oligo(dT) molecules hydrogen-bonded to poly(dA), is not able to ligate oligo(dT) with a poly(rA) complementary strand, can join oligo(rA) molecules hydrogen-bonded to poly(dT) Mammalia AMP + diphosphate + (deoxyribonucleotide)n+m
-
 ?
6.5.1.1 ATP + (deoxyribonucleotide)n + (deoxyribonucleotide)m ligation of strand interruptions in oligo(dT)*poly(dA) Vaccinia virus AMP + diphosphate + (deoxyribonucleotide)n+m
-
 ?
6.5.1.1 ATP + (deoxyribonucleotide)n + (deoxyribonucleotide)m ligates oligo(dT) with a poly(rA) complementary strand Tequatrovirus T4 AMP + diphosphate + (deoxyribonucleotide)n+m
-
 ?
6.5.1.1 ATP + (deoxyribonucleotide)n + (deoxyribonucleotide)m DNA ligase I: seals single-strand breaks in DNA Mammalia AMP + diphosphate + (deoxyribonucleotide)n+m
-
 ?
6.5.1.1 ATP + (deoxyribonucleotide)n + (deoxyribonucleotide)m DNA ligase II: can catalyze joining of an oligo(dT)*poly(rA) Drosophila melanogaster AMP + diphosphate + (deoxyribonucleotide)n+m
-
 ?
6.5.1.1 ATP + (deoxyribonucleotide)n + (deoxyribonucleotide)m
-
 Drosophila melanogaster ?
-
 ?
6.5.1.1 ATP + (deoxyribonucleotide)n + (deoxyribonucleotide)m
-
 Homo sapiens ?
-
 ?
6.5.1.1 ATP + (deoxyribonucleotide)n + (deoxyribonucleotide)m
-
 Saccharomyces cerevisiae ?
-
 ?
6.5.1.1 ATP + (deoxyribonucleotide)n + (deoxyribonucleotide)m
-
 Bos taurus ?
-
 ?
6.5.1.1 ATP + (deoxyribonucleotide)n + (deoxyribonucleotide)m
-
 Tequatrovirus T4 ?
-
 ?
6.5.1.1 ATP + (deoxyribonucleotide)n + (deoxyribonucleotide)m nonessential for viral DNA replication and growth on several types of host cells. DNA ligase I participates in DNA base excision repair as a component of a multiprotein complex Vaccinia virus ?
-
 ?
6.5.1.1 ATP + (deoxyribonucleotide)n + (deoxyribonucleotide)m DNA ligase I is the key enzyme for joining Okazaki fragments during lagging-strand DNA synthesis in mammalian cells and also for completion of DNA excision repair processes Mammalia ?
-
 ?
6.5.1.1 dATP + (deoxyribonucleotide)n + (deoxyribonucleotide)m
-
 Mammalia dAMP + diphosphate + (deoxyribonucleotide)n+m
-
 ?
6.5.1.1 dATP + (deoxyribonucleotide)n + (deoxyribonucleotide)m
-
 Tequatrovirus T4 dAMP + diphosphate + (deoxyribonucleotide)n+m
-
 ?
6.5.1.1 additional information DNA ligase I is induced upon cell proliferation, DNA ligase II, and III not Mammalia ?
-
 ?

Subunits

EC Number Subunits Comment Organism
6.5.1.1 ?
-
 Homo sapiens
6.5.1.1 ?
-
 Saccharomyces cerevisiae
6.5.1.1 ?
-
 Bos taurus
6.5.1.1 ?
-
 Schizosaccharomyces pombe
6.5.1.1 ? x * 83000-86000, SDS-PAGE Drosophila melanogaster
6.5.1.1 dimer 1 * 46000 + 1 * 100000, DNA ligase III, SDS-PAGE. It cannot be concluded whether the 46000 MW peptide is an essential and integral part of DNA ligase III, or if it represents a separate protein that binds tentaciously to the 100000 MW DNA ligase component Mammalia
6.5.1.1 monomer
-
 Drosophila melanogaster
6.5.1.1 monomer
-
 Saccharomyces cerevisiae
6.5.1.1 monomer
-
 Bos taurus
6.5.1.1 monomer
-
 Tequatrovirus T4
6.5.1.1 monomer 1 * 68000-72000, DNA ligase II, SDS-PAGE Mammalia
6.5.1.1 monomer 1 * 125000-130000, DNA ligase I, SDS-PAGE Mammalia

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
6.5.1.1 42
-
-
 Bos taurus
6.5.1.1 42
-
 rapid inactivation, DNA ligase II Mammalia