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Literature summary for 6.5.1.1 extracted from

  • Taylor, M.R.; Conrad, J.A.; Wahl, D.; OBrien, P.J.
    Kinetic mechanism of human DNA ligase I reveals magnesium-dependent changes in the rate-limiting step that compromise ligation efficiency (2011), J. Biol. Chem., 286, 23054-23062.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 6.5.1.1

Cloned(Commentary)

Cloned (Comment) Organism
the catalytic domain of human LIG1 (residues 232-919) is expressed in Escherichia coli Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
EDTA EDTA rapidly inactivates all LIG1-catalyzed reactions Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.012
-
 ATP at 30 mM Mg2+, pH and temperature not specified in the publication Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ LIG1 requires multiple Mg2+ ions for catalysis Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Ni-NTA column chromatography and Q-Sepharose column chromatography Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + (deoxyribonucleotide)n + (deoxyribonucleotide)m synthetic 28-mer oligonucleotide duplex that contains a nick with a 3'-hydroxyl and a 5'-phosphate, more than 95% of the nicked DNA is ligated within 2 s Homo sapiens AMP + diphosphate + (deoxyribonucleotide)m+n
-
 ?
additional information LIG1 catalyzes the ligation of single-strand breaks to complete DNA replication and repair. The energy of ATP is used to form a new phosphodiester bond in DNA via a reaction mechanism that involves three distinct chemical steps: enzyme adenylylation, adenylyl transfer to DNA, and nick sealing Homo sapiens ?
-
 ?

Synonyms

Synonyms Comment Organism
DNA ligase I
-
 Homo sapiens
LIG1
-
 Homo sapiens

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.74
-
 ATP at 30 mM Mg2+, pH and temperature not specified in the publication Homo sapiens

Cofactor

Cofactor Comment Organism Structure
ATP the efficiency of ligation falls from near 100% under optimal conditions with 1 mM Mg2+ and 10 mM ATP to 60% with 1 mM Mg2+ and 2 mM ATP Homo sapiens