EC Number   |
Natural Substrates |
|---|
   6.5.1.1 | ATP + (deoxyribonucleotide)20 + (deoxyribonucleotide)20 |
sealing of a single nick in a 20mer DNA duplex, ADL is specific for nicked DNA and is not able to catalyze blunt end joining |
| 6.5.1.1 | ATP + (deoxyribonucleotide)n + (deoxyribonucleotide)m |
- |
| 6.5.1.1 | ATP + (deoxyribonucleotide)n + (deoxyribonucleotide)m |
ATP-dependent ligase LigB displays vigorous nick sealing activity in presence of NAD+ and ATP |
| 6.5.1.1 | ATP + (deoxyribonucleotide)n + (deoxyribonucleotide)m |
ATP-dependent ligase LigC displays weak nick joining activity and generates high levels of DNA adenylate intermediate |
| 6.5.1.1 | ATP + (deoxyribonucleotide)n + (deoxyribonucleotide)m |
ATP-dependent ligase LigD displays weak nick joining activity and generates high levels of DNA adenylate intermediate |
| 6.5.1.1 | ATP + (deoxyribonucleotide)n + (deoxyribonucleotide)m |
poly(ADP-ribose) polymerase-1 and XRCC1/DNA ligase III are involved in an alternative route for DNA double-strand breaks rejoining |
| 6.5.1.1 | ATP + (deoxyribonucleotide)n + (deoxyribonucleotide)m |
Agrobacterium LigD1 is composed of a central ligase domain fused to a C-terminal polymerase-like (POL) domain and an N-terminal 3'-phosphoesterase (PE) module. The LigD1 protein seals DNA nicks, albeit inefficiently. The LigD1 POL domain has no detectable polymerase activity. The PE domain catalyzes metal-dependent phosphodiesterase and phosphomonoesterase reactions at a primer-template with a 3'-terminal diribonucleotide to yield a primertemplate with a monoribonucleotide 3'-OH end. The PE domain also has a 3'-phosphatase activity on an all-DNA primer-template that yields a 3'-OH DNA end |
| 6.5.1.1 | ATP + (deoxyribonucleotide)n + (deoxyribonucleotide)m |
Agrobacterium LigD2 is composed of a central ligase domain fused to a C-terminal polymerase-like (POL) domain and an N-terminal 3'-phosphoesterase (PE) module. The LigD1 protein seals DNA nicks, albeit inefficiently. The LigD2 POL domain adds ribonucleotides or deoxyribonucleotides to a DNA primer-template, with rNTPs being the preferred substrates. The PE domain catalyzes metal-dependent phosphodiesterase and phosphomonoesterase reactions at a primer-template with a 3'-terminal diribonucleotide to yield a primer-template with a monoribonucleotide 3'-OH end. The PE domain also has a 3'-phosphatase activity on an all-DNA primer-template that yields a 3'-OH DNA end |
| 6.5.1.1 | ATP + (deoxyribonucleotide)n + (deoxyribonucleotide)m |
ATP-dependent DNA ligase LigA is non-essential for cell viability. Haloferax volcanii also encodes the NAD+-dependent DNA ligase LigN. As with LigA, LigN is also non-essential for cell viability. Simultaneous inactivation of both proteins is lethal, however, indicating that they share an essential function |
| 6.5.1.1 | ATP + (deoxyribonucleotide)n + (deoxyribonucleotide)m |
damaged DNA bases are repaired by base excision repair which can proceed via two pathways: short patch and long patch base excision repair. Inhibition of long patch base excision repair is mediated by the ligation activity of Lig III. Lowering the levels of XRCC1 and Lig III in HeLa cells decreases cellular repair capacity, but substantially increases Pol beta-dependent strand displacement DNA synthesis |
