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Literature summary for 6.5.1.1 extracted from

  • Tanabe, M.; Ishino, S.; Yohda, M.; Morikawa, K.; Ishino, Y.; Nishida, H.
    Structure-based mutational study of an archaeal DNA ligase towards improvement of ligation activity (2012), ChemBioChem, 13, 2575-2582.
    View publication on PubMed
Search for more literature for 6.5.1.1

Cloned(Commentary)

Cloned (Comment) Organism
overexpression of wild-type and mutant enzymes in Escherichia coli Pyrococcus furiosus

Crystallization (Commentary)

Crystallization (Comment) Organism
-
 Pyrococcus furiosus

Protein Variants

Protein Variants Comment Organism
D540A mutant exhibits notably enhanced nick-joining activity compared with that of the wild type enzyme, the mutant enzyme exhibits activity about twice as high as that of the wild type within 10 min Pyrococcus furiosus
D540A/Q547A/K554A/K558A the mutant enzyme exhibits activity about twice as high as that of the wild type within 10 min. The D540A ligation is almost the same as that of the D540A/Q547A/K554A/K558A mutant enzyme, thus implying that a single substitution for Asp540 might exert a more dominant effect than the substitutions of the other three polar and ionic residues at the C terminus Pyrococcus furiosus
D540K the mutant exhibits notably enhanced nick-joining activity compared with that of the wild type enzyme Pyrococcus furiosus
D540R the mutant exhibits notably enhanced nick-joining activity compared with that of the wild type enzyme Pyrococcus furiosus
D540S the mutant exhibits notably enhanced nick-joining activity compared with that of the wild type enzyme Pyrococcus furiosus
Q547A/K554A/K558A nick ligation activity of the mutant is slightly higher than that of the wild type enzyme Pyrococcus furiosus
R544A mutant R544A displays a notable reduction in nick-joining activity (less than 45% of the input substrate ligated) in comparison with that of mutant R544A/Q547A/K554A/K558A Pyrococcus furiosus
R544A/Q547A/K554A/K558A mutant enzyme exhibits low activity. Mutant R544A displays a notable reduction in nick-joining activity (less than 45% of the input substrate ligated) in comparison with that of mutant R544A/Q547A/K554A/K558A Pyrococcus furiosus

Organism

Organism UniProt Comment Textmining
Pyrococcus furiosus
-
-
-
Thermococcus sp.
-
-
-

Synonyms

Synonyms Comment Organism
DNA ligase
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 Thermococcus sp.
PfuLig
-
 Pyrococcus furiosus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
60
-
-
 Pyrococcus furiosus