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Literature summary 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

Cloned(Commentary)

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

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
6.5.1.1
-
 Pyrococcus furiosus

Protein Variants

EC Number Protein Variants Comment Organism
6.5.1.1 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
6.5.1.1 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
6.5.1.1 D540K the mutant exhibits notably enhanced nick-joining activity compared with that of the wild type enzyme Pyrococcus furiosus
6.5.1.1 D540R the mutant exhibits notably enhanced nick-joining activity compared with that of the wild type enzyme Pyrococcus furiosus
6.5.1.1 D540S the mutant exhibits notably enhanced nick-joining activity compared with that of the wild type enzyme Pyrococcus furiosus
6.5.1.1 Q547A/K554A/K558A nick ligation activity of the mutant is slightly higher than that of the wild type enzyme Pyrococcus furiosus
6.5.1.1 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
6.5.1.1 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

EC Number Organism UniProt Comment Textmining
6.5.1.1 Pyrococcus furiosus
-
-
-
6.5.1.1 Thermococcus sp.
-
-
-

Synonyms

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

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
6.5.1.1 60
-
-
 Pyrococcus furiosus