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Maiko Tanabe, Dr. Sonoko Ishino, Prof. Masafumi Yohda, Prof. Kosuke Morikawa, Prof. Yoshizumi Ishino and Dr. Hirokazu Nishida Structure-Based Mutational Study of an Archaeal DNA Ligase towards Improvement of Ligation Activity ChemBioChem 13

Version of Record online: 6 NOV 2012 | DOI: 10.1002/cbic.201200336

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Super mutant: We report a series of mutations in the domain boundary of Pyrococcus furiosus DNA ligase, and demonstrate that the replacement of Asp540 with a positively charged residue improved the ligation activity. The increased activity of the Asp540 mutant is attributed to efficient adenylylation and DNA binding.

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