EC 6.5.1.2 - DNA ligase (NAD+)

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IntEnz Enzyme Nomenclature
EC 6.5.1.2

Names

Accepted name:
DNA ligase (NAD+)
Other names:
DNA joinase [ambiguous]
DNA ligase [ambiguous]
DNA repair enzyme [ambiguous]
DNA-joining enzyme [ambiguous]
deoxyribonucleate ligase [ambiguous]
deoxyribonucleic acid joinase [ambiguous]
deoxyribonucleic acid ligase [ambiguous]
deoxyribonucleic joinase [ambiguous]
deoxyribonucleic ligase [ambiguous]
deoxyribonucleic repair enzyme [ambiguous]
deoxyribonucleic-joining enzyme [ambiguous]
polydeoxyribonucleotide synthase (NAD+)
polynucleotide ligase [ambiguous]
polynucleotide ligase (nicotinamide adenine dinucleotide)
polynucleotide synthetase [ambiguous]
polynucleotide synthetase (nicotinamide adenine dinucleotide)
polynucleotide ligase (NAD+)
polydeoxyribonucleotide synthase (NAD+)
polynucleotide ligase (NAD+)
poly(deoxyribonucleotide):poly(deoxyribonucleotide) ligase (AMP-forming, NMN-forming)
Systematic name:
poly(deoxyribonucleotide)-3'-hydroxyl:5'-phospho-poly(deoxyribonucleotide) ligase (NAD+)

Reactions

Comments:

The enzyme, typically found in bacteria, 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 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. RNA can also act as substrate, to some extent. cf. EC 6.5.1.1, DNA ligase (ATP), EC 6.5.1.6, DNA ligase (ATP or 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
Protein domains and families: PROSITE:PDOC00809
Structural data: CSA , EC2PDB
Gene Ontology: GO:0003911
CAS Registry Number: 37259-52-2
UniProtKB/Swiss-Prot: (876) [show] [UniProt]

References

  1. Zimmerman, S.B., Little, J.W., Oshinsky, C.K. and Gellert, M.
    Enzymatic joining of DNA strands: a novel reaction of diphosphopyridine nucleotide.
    Proc. Natl. Acad. Sci. USA 57: 1841-1848 (1967). [PMID: 4291949]
  2. Little, J. W., Zimmerman, S. B., Oshinsky, C. K., Gellert, M.
    Enzymatic joining of DNA strands, II. An enzyme-adenylate intermediate in the dpn-dependent DNA ligase reaction.
    Proc. Natl. Acad. Sci. U.S.A. 58: 2004-2011 (1967). [PMID: 4295585]
  3. Modorich, P., Lehman, I. R.
    Deoxyribonucleic acid ligase. A steady state kinetic analysis of the reaction catalyzed by the enzyme from Escherichia coli.
    J. Biol. Chem. 248: 7502-7511 (1973). [PMID: 4355585]
  4. Modrich, P., Anraku, Y., Lehman, I. R.
    Deoxyribonucleic acid ligase. Isolation and physical characterization of the homogeneous enzyme from Escherichia coli.
    J. Biol. Chem. 248: 7495-7501 (1973). [PMID: 4355584]
  5. Uphoff, S., Reyes-Lamothe, R., Garza de Leon, F., Sherratt, D. J., Kapanidis, A. N.
    Single-molecule DNA repair in live bacteria.
    Proc. Natl. Acad. Sci. U.S.A. 110: 8063-8068 (2013). [PMID: 23630273]

[EC 6.5.1.2 created 1972, modified 1976, modified 2016]