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Literature summary extracted from

  • Teraoka, H.; Sawai, M.; Tsukada, K.
    Kinetic studies on the reaction catalyzed by DNA ligase from calf thymus (1983), Biochim. Biophys. Acta, 747, 117-122.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
6.5.1.1 spermidine 5 mM, increases the Km for nicked DNA, increases reaction velocity Bos taurus
6.5.1.1 spermine 0.5 mM, increases the Km for nicked DNA, increases reaction velocity Bos taurus

Inhibitors

EC Number Inhibitors Comment Organism Structure
6.5.1.1 dATP competitive with respect to ATP Bos taurus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.5.1.1 0.00011
-
DNA nicked DNA 5'-phosphoryl ends Bos taurus
6.5.1.1 0.002
-
ATP ATP Bos taurus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.5.1.1 Mg2+ required Bos taurus
6.5.1.1 Mg2+ optimal concentration: 10 mM Bos taurus

Organism

EC Number Organism UniProt Comment Textmining
6.5.1.1 Bos taurus
-
calf
-

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 uni-uni uni-bi ping-pong mechanism. The order of substrate addition and product release is as follows: ATP, diphosphate, nicked DNA, sealed DNA, 5'-AMP Bos taurus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
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
-
Bos taurus AMP + diphosphate + (deoxyribonucleotide)n+m
-
?
6.5.1.1 ATP + DNA
-
Bos taurus AMP + diphosphate + ?
-
?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
6.5.1.1 0.117
-
DNA
-
Bos taurus