| Accepted Name |
|---|
| DNA ligase (ATP or NAD(+))
|
| Reaction catalysed |
|---|
- ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m <=> (deoxyribonucleotide)n+m + AMP + diphosphate
- NAD(+) + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m <=> (deoxyribonucleotide)n+m + AMP + beta-nicotinamide D-nucleotide
|
| Comment(s) |
|---|
- 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 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 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 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 adenylate.
- Different from EC 6.5.1.1, EC 6.5.1.2 and EC 6.5.1.7.
|
| Cross-references |
|---|
| BRENDA | 6.5.1.6 |
| EC2PDB | 6.5.1.6 |
| ExplorEnz | 6.5.1.6 |
| PRIAM enzyme-specific profiles | 6.5.1.6 |
| KEGG Ligand Database for Enzyme Nomenclature | 6.5.1.6 |
| IUBMB Enzyme Nomenclature | 6.5.1.6 |
| IntEnz | 6.5.1.6 |
| MEDLINE | Find literature relating to 6.5.1.6 |
| MetaCyc | 6.5.1.6 |
| Rhea expert-curated reactions | 6.5.1.6 |
| UniProtKB/Swiss-Prot |
|
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