Highly efficient hyperthermophilic DNA ligase

Details Highly efficient hyperthermophilic DNA ligase Highly efficient hyperthermophilic DNA ligase

2011-07-19

2011-07-19

Hutson, Richard G (Department: 1652)

Chemistry: molecular biology and microbiology

Enzyme , proenzyme; compositions thereof; process for...

Transferase other than ribonuclease

C435S183000, C530S350000

Reexamination Certificate

active

07981653

ABSTRACT:
Disclosed is a modified hyperthermophilic DNA ligase having improved DNA binding ability and reactivity. The modified hyperthermophilic DNA ligase has an amino acid sequence corresponding to the amino acid sequence of a heat-resistant DNA ligase derived from a thermophilic bacterium, a hyperthermophilic bacterium, a thermophilic archaebacterium, or a hyperthermophilic archaebacterium, except with at least two of the charged amino acids in the C-terminal helix region each being substituted by alanine, threonine, or serine residues.

REFERENCES:
patent: 6576453 (2003-06-01), Barany et al.
Ngo et al., The Protein Folding Problem and Tertiary Structure Prediction, 1994, Merz et al. (ed.), Birkhauser, Boston, MA, pp. 433 and 492-495.
Nishida et al., Journal of Molecular Biology, vol. 360, No. 5, pp. 956-967, Jul. 2006.
Ishikawa, Kazuhiko, “Development of the World's Most Thermostable Enzyme (DNA Ligase) for Gene Diagnosis”, National Institute of Advanced Industrial Science and Technology, Sep. 10, 2003, 4 pages.

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