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Literature summary for 6.5.1.1 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
Search for more literature for 6.5.1.1

Organism

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

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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

Synonyms Comment Organism
T4 DNA ligase
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 Tequatrovirus T4

Temperature Optimum [°C]

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

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
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

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
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 assay at Tequatrovirus T4