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Literature summary extracted from

  • Lohman, G.J.; Chen, L.; Evans, T.C.
    Kinetic characterization of single strand break ligation in duplex DNA by T4 DNA ligase (2011), J. Biol. Chem., 286, 44187-44196.
    View publication on PubMedView publication on EuropePMC

Organism

EC Number Organism UniProt Comment Textmining
6.5.1.1 Tequatrovirus T4
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.5.1.1 ATP + (deoxyribonucleotide)n + (deoxyribonucleotide)m both adenylyl transfer and phosphodiester bond formation appear to be effectively irreversible under the reaction conditions tested. The rates of the slowest chemical steps for reaction of both phosphorylated substrate and adenylylated substrate are found to be 10times faster than the steady state turnover rates for each substrate, suggesting that the true rate-limiting step during turnover is release of the ligated product or a post-product release conformational change Tequatrovirus T4 AMP + diphosphate + (deoxyribonucleotide)n+m
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Synonyms

EC Number Synonyms Comment Organism
6.5.1.1 T4 DNA ligase
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 Tequatrovirus T4

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
6.5.1.1 16
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 assay at Tequatrovirus T4

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
6.5.1.1 additional information
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 additional information steady state experiments with a nicked substrate containing juxtaposed dC and 5'-phosphorylated dT deoxynucleotides yield kcat and kcat/Km values of 0.4/sec and 150/microM/sec, respectively. Under identical reaction conditions, turnover of an adenylylated version of this substrate yield kcat and kcat/Km values of 0.64/sec and 240 microM/sec Tequatrovirus T4

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
6.5.1.1 7.5
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 assay at Tequatrovirus T4