EC 6.5.1.6 - DNA ligase (ATP or NAD+)

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IntEnz Enzyme Nomenclature
EC 6.5.1.6

Names

Accepted name:
DNA ligase (ATP or NAD+)
Systematic name:
poly(deoxyribonucleotide)-3'-hydroxyl:5'-phospho-poly(deoxyribonucleotide) ligase (ATP or NAD+)

Reactions

Comments:

The enzymes from the archaea Thermococcus fumicolans and Thermococcus onnurineus show high activity with either ATP or NAD+, and significantly lower activity with TTP, GTP, and CTP. The enzyme catalyses the ligation of DNA strands with 3'-hydroxyl and 5'-phosphate termini, forming a phosphodiester and sealing certain types of single-strand breaks in duplex DNA. Catalysis occurs by a three-step mechanism, starting with the activation of the enzyme by ATP or NAD+, forming a phosphoramide bond between adenylate and a lysine residue. The adenylate group is then transferred to the 5'-phosphate terminus of the substrate, forming the capped structure 5'-(5'-diphosphoadenosine)-[DNA]. Finally, the enzyme catalyses a nucleophilic attack of the 3'-OH terminus on the capped terminus, which results in formation of the phosphodiester bond and release of the adenylate. Different from EC 6.5.1.1, DNA ligase (ATP), EC 6.5.1.2, DNA ligase (NAD+) and EC 6.5.1.7, DNA ligase (ATP, ADP or GTP).

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
UniProtKB/Swiss-Prot:

References

  1. Rolland, J. L., Gueguen, Y., Persillon, C., Masson, J. M., Dietrich, J.
    Characterization of a thermophilic DNA ligase from the archaeon Thermococcus fumicolans.
    FEMS Microbiol. Lett. 236 : 267-273 (2004). [PMID: 15251207]
  2. Kim, Y. J., Lee, H. S., Bae, S. S., Jeon, J. H., Yang, S. H., Lim, J. K., Kang, S. G., Kwon, S. T., Lee, J. H.
    Cloning, expression, and characterization of a DNA ligase from a hyperthermophilic archaeon Thermococcus sp.
    Biotechnol. Lett. 28 : 401-407 (2006). [PMID: 16614906]

[EC 6.5.1.6 created 2014, modified 2016]