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 |
BRENDA | 6.5.1.7 |
EC2PDB | 6.5.1.7 |
ExplorEnz | 6.5.1.7 |
PRIAM enzyme-specific profiles | 6.5.1.7 |
KEGG Ligand Database for Enzyme Nomenclature | 6.5.1.7 |
IUBMB Enzyme Nomenclature | 6.5.1.7 |
IntEnz | 6.5.1.7 |
MEDLINE | Find literature relating to 6.5.1.7 |
MetaCyc | 6.5.1.7 |
Rhea expert-curated reactions | 6.5.1.7 |
UniProtKB/Swiss-Prot |
|
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