| Literature DB >> 16614906 |
Yun Jae Kim1, Hyun Sook Lee, Seung Seob Bae, Jung Ho Jeon, Sung Hyun Yang, Jae Kyu Lim, Sung Gyun Kang, Suk-Tae Kwon, Jung-Hyun Lee.
Abstract
Genomic analysis of a hyperthermophilic archaeon, Thermococcus sp. NA1, revealed an ORF of 1689 bases encoding 562 amino acids that showed a high similarity to DNA ligases from other hyperthermophilic archaea. The ligase, which was designated TNA1_lig (Thermococcus sp. NA1 ligase), was cloned and expressed in Escherichia coli. The recombinant TNA1_lig was purified by metal affinity chromatography. The optimum ligase activity of the recombinant TNA1_lig occurred at 80 degrees C and pH 7.5. The enzyme was activated by MgCl2 and ZnCl2 but was inhibited by MnCl2 and NiCl2. Additionally, the enzyme was activated by either ATP or NAD+.Entities:
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Year: 2006 PMID: 16614906 DOI: 10.1007/s10529-005-6070-6
Source DB: PubMed Journal: Biotechnol Lett ISSN: 0141-5492 Impact factor: 2.461