ENZYME entry: EC 6.5.1.7

Accepted Name
DNA ligase (ATP, ADP or GTP).
Reaction catalysed
  • ATP + (deoxyribonucleotide)(n)-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)(m) <=> (deoxyribonucleotide)(n+m) + AMP + diphosphate
  • ADP + (deoxyribonucleotide)(n)-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)(m) <=> (deoxyribonucleotide)(n+m) + AMP + phosphate
  • GTP + (deoxyribonucleotide)(n)-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)(m) <=> (deoxyribonucleotide)(n+m) + GMP + diphosphate
Comment(s)
  • The enzymes from the archaea Hyperthermus butylicus and Sulfophobococcus zilligii are active with ATP, ADP or GTP.
  • They show no activity with NAD(+).
  • The enzyme catalyzes 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, ADP, or GTP, forming a phosphoramide bond between adenylate/guanylate and a lysine residue.
  • The nucleotide is then transferred to the 5'-phosphate terminus of the substrate, forming the capped structure 5'-(5'-diphosphoadenosine/guanosine)-(DNA).
  • Finally, the enzyme catalyzes a nucleophilic attack of the 3'-OH terminus on the capped terminus, which results in formation of the phosphodiester bond and release of the nucleotide.
  • Different from EC 6.5.1.1 and EC 6.5.1.6, which cannot utilize GTP.
Cross-references
BRENDA6.5.1.7
EC2PDB6.5.1.7
ExplorEnz6.5.1.7
PRIAM enzyme-specific profiles6.5.1.7
KEGG Ligand Database for Enzyme Nomenclature6.5.1.7
IUBMB Enzyme Nomenclature6.5.1.7
IntEnz6.5.1.7
MEDLINEFind literature relating to 6.5.1.7
MetaCyc6.5.1.7
UniProtKB/Swiss-Prot
A2BJX6, DNLI_HYPBU;  D2CJS7, DNLI_SULZI;  

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All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 6.5.1.-
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