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Information on EC 6.5.1.2 - DNA ligase (NAD+) and Organism(s) Escherichia coli and UniProt Accession P15042

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EC Tree
IUBMB 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).
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Escherichia coli
UNIPROT: P15042
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Word Map
The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
hide(Overall reactions are displayed. Show all >>)
Synonyms
nad(+)-dependent dna ligase, taq dna ligase, nad+-dependent dna ligase, tfi dna ligase, nad-dependent dna ligase, tth dna ligase, mimilig, wbm-liga, mtuliga, polynucleotide synthetase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
NAD+-dependent DNA ligase
-
beta-NAD+ -dependent DNA ligase
-
-
Deoxyribonucleate ligase
-
-
-
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Deoxyribonucleic acid joinase
-
-
-
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Deoxyribonucleic acid ligase
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-
-
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Deoxyribonucleic joinase
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-
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Deoxyribonucleic ligase
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-
-
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Deoxyribonucleic repair enzyme
-
-
-
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Deoxyribonucleic-joining enzyme
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-
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DNA joinase
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-
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DNA ligase
DNA ligase (NAD)
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-
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DNA repair enzyme
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-
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DNA-joining enzyme
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-
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Ligase, polynucleotide (nicotinamide adenine dinucleotide)
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-
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NAD(+)-dependent DNA ligase
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NAD-dependent DNA ligase
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Polydeoxyribonucleotide synthase (NAD+)
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Polydeoxyribonucleotide synthase [NAD+]
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Polynucleotide ligase
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-
-
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Polynucleotide synthetase
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-
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Polynucleotide synthetase (nicotinamide adenine dinucleotide)
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-
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Synthetase, polydeoxyribonucleotide (nicotinamide adenine dinucleotide)
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-
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Tfi DNA ligase
-
-
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Tth DNA ligase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + beta-nicotinamide D-nucleotide
show the reaction diagram
SYSTEMATIC NAME
IUBMB Comments
poly(deoxyribonucleotide)-3'-hydroxyl:5'-phospho-poly(deoxyribonucleotide) ligase (NAD+)
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).
CAS REGISTRY NUMBER
COMMENTARY hide
37259-52-2
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
NAD+ + (deoxyribonucleotide)n + (deoxyribonucleotide)m
AMP + beta-nicotinamide D-ribonucleotide + (deoxyribonucleotide)n+m
show the reaction diagram
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-
-
?
NAD+ + (deoxyribonucleotide)n + (deoxyribonucleotide)m
AMP + nicotinamide nucleotide + (deoxyribonucleotide)n+m
show the reaction diagram
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-
-
?
ATP + 5'-phosphate terminus of deoxyribonucleotides
?
show the reaction diagram
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-
-
-
?
ATP + nicked DNA
?
show the reaction diagram
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-
-
-
?
ATP + nicked DNA
AMP + diphosphate + ?
show the reaction diagram
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-
-
-
?
NAD+ + (deoxyribonucleotide)n + (deoxyribonucleotide)m
?
show the reaction diagram
NAD+ + (deoxyribonucleotide)n + (deoxyribonucleotide)m
AMP + beta-nicotinamide D-ribonucleotide + (deoxyribonucleotide)n+m
show the reaction diagram
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-
-
-
?
NAD+ + (deoxyribonucleotide)n + (deoxyribonucleotide)m
AMP + nicotinamide nucleotide + (deoxyribonucleotide)n+m
show the reaction diagram
NAD+ + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m
(deoxyribonucleotide)n+m + AMP + beta-nicotinamide D-nucleotide
show the reaction diagram
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-
-
-
?
NADH + (deoxyribonucleotide)n + (deoxyribonucleotide)m
?
show the reaction diagram
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NADH has a significantly higher Km as NAD+
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-
?
Thionicotinamide derivative of NAD+ + (deoxyribonucleotide)n + (deoxyribonucleotide)m
?
show the reaction diagram
-
significantly higher Km as NAD+
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?
additional information
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
NAD+ + (deoxyribonucleotide)n + (deoxyribonucleotide)m
?
show the reaction diagram
NAD+ + (deoxyribonucleotide)n + (deoxyribonucleotide)m
AMP + nicotinamide nucleotide + (deoxyribonucleotide)n+m
show the reaction diagram
NAD+ + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m
(deoxyribonucleotide)n+m + AMP + beta-nicotinamide D-nucleotide
show the reaction diagram
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
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60% as active as Mg2+ in activation as reported in one study, no activity in another
Co2+
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25% of the activity with Mg2+
KCl
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stimulation by 300 mM KCl, in 10% w/v polyethylene glycol 6000 solution or 150-300 mM KCl in 15% polyethylene glycol 6000 solution. Stimulation of intermolecular blunt end ligation by 150-250 mM KCl in 15% polyethylene glycol 600 solution
NaCl
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stimulation of intermolecular cohesive-end ligation by 200 mM NaCl, in 10% w/v polyethylene glycol 6000 solution, or 100-200 mM NaCl in 15% polyethylene glycol 6000 solution. Stimulation of intermolecular blunt end ligation by 100-150 mM NaCl in 15% polyethylene glycol 600 solution
Rb+
-
stimulates
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(2R,3S,4R,5R)-5-(6-amino-2-iodo-9H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl dihydrogen phosphate
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-
(3aR,5R,6R,6aS)-5-[6-amino-2-(methylsulfanyl)-9H-purin-9-yl]-6-hydroxy-2-sulfanyltetrahydro-2H-2lambda-5-furo[2,3-d][1,3,2]dioxaphosphol-2-one
-
-
(3S)-3-[4-amino-2-[(4-methylcyclohexyl)oxy]-5-oxopyrido[2,3-d]pyrimidin-8(5H)-yl]-4-hydroxycyclopentanecarboxamide
-
-
(3S)-3-[4-amino-2-[(4-methylcyclohexyl)oxy]-5-oxopyrido[2,3-d]pyrimidin-8(5H)-yl]-4-hydroxycyclopentanecarboxylic acid
-
-
(4-amino-2-[(2-methylcyclohexyl)oxy]-5-oxopyrido[2,3-d]pyrimidin-8(5H)-yl)acetonitrile
-
-
(4R)-N4-(6-chloro-2-methoxyacridin-9-yl)-N1,N1-diethylpentane-1,4-diamine
-
-
2,2'-([4-[(6-chloro-2-methoxyacridin-9-yl)amino]pentyl]imino)diethanol
-
-
2,4-diamino-5-oxo-5H-chromeno[2,3-b]pyridine-3-carbonitrile
-
powerful inhibitor, exhibits good inhibition at nanomolar concentrations
2,4-diamino-7-tert-butyl-4a,8a-dihydro-1,8-naphthyridine-3-carbonitrile
-
-
2-(butylsulfanyl)-5'-deoxyadenosine
-
-
2-(butylsulfanyl)adenosine
-
-
2-(cyclobutylmethoxy)-5'-deoxy-5'-fluoroadenosine
-
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2-(cyclopentyloxy)-3',5'-dideoxy-3'-[(3,5-dichlorophenyl)methyl]adenosine
-
-
2-(cyclopentyloxy)-3',5'-dideoxy-5'-fluoro-3'-(1H-triaziren-1-yl)adenosine
-
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2-(cyclopentyloxy)-5'-deoxy-5'-fluoroadenosine
-
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2-(cyclopentyloxy)-5'-deoxyadenosine
-
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2-(cyclopentyloxy)adenosine
-
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2-(cyclopentylsulfanyl)adenosine
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2-amino-5-(2-hydroxyethyl)-7-(trifluoromethyl)-1,8-naphthyridine-3-carboxamide
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2-amino-5-(2-methoxyethyl)-7-(trifluoromethyl)-1,8-naphthyridine-3-carboxamide
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2-amino-5-(aminomethyl)-7-(trifluoromethyl)-1,8-naphthyridine-3-carboxamide
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2-amino-5-methyl-7-(trifluoromethyl)-1,8-naphthyridine-3-carboxamide
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2-amino-5-oxo-5H-chromeno[2,3-b]pyridine-3-carboxamide
-
powerful inhibitor, exhibits good inhibition at nanomolar concentrations
2-amino-5-oxo-5H-[1]benzopyrano[2,3-b]pyridine-3-carboxamide
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2-amino-5-phenyl-7-(trifluoromethyl)-1,8-naphthyridine-3-carboxamide
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2-amino-5-[(3R)-3-aminopyrrolidin-1-yl]-6-bromo-7-(trifluoromethyl)-1,8-naphthyridine-3-carboxamide
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2-amino-5H-chromeno[2,3-b]pyridine-3-carboxamide
-
powerful inhibitor, exhibits good inhibition at nanomolar concentrations
2-amino-6-(2-phenylethyl)-7-(trifluoromethyl)-1,8-naphthyridine-3-carboxamide
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2-amino-6-(hydroxymethyl)-7-(trifluoromethyl)-1,8-naphthyridine-3-carboxamide
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2-amino-6-(propan-2-yl)-7-(trifluoromethyl)-1,8-naphthyridine-3-carboxamide
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2-amino-6-benzyl-7-(trifluoromethyl)-1,8-naphthyridine-3-carboxamide
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2-amino-6-benzyl-7-chloro-5-methyl-1,8-naphthyridine-3-carboxamide
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2-amino-6-bromo-5-(3-hydroxyazetidin-1-yl)-7-(trifluoromethyl)-1,8-naphthyridine-3-carboxamide
-
-
2-amino-6-bromo-5-(4-hydroxypiperidin-1-yl)-7-(trifluoromethyl)-1,8-naphthyridine-3-carboxamide
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2-amino-6-bromo-5-[(2-hydroxyethyl)(methyl)amino]-7-(trifluoromethyl)-1,8-naphthyridine-3-carboxamide
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2-amino-6-bromo-5-[(3R)-3-hydroxypyrrolidin-1-yl]-7-(trifluoromethyl)-1,8-naphthyridine-3-carboxamide
-
-
2-amino-6-bromo-7-(trifluoromethyl)-1,8-naphthyridine-3-carboxamide
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2-amino-6-bromo-7-cyclopentyl-1,8-naphthyridine-3-carboxamide
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2-amino-6-bromo-7-tert-butyl-1,8-naphthyridine-3-carboxamide
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2-amino-6-chloro-5-ethyl-1,8-naphthyridine-3-carboxamide
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2-amino-6-cyclopentyl-7-(trifluoromethyl)-1,8-naphthyridine-3-carboxamide
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2-amino-6-cyclopropyl-7-(trifluoromethyl)-1,8-naphthyridine-3-carboxamide
-
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2-amino-6-ethenyl-7-(trifluoromethyl)-1,8-naphthyridine-3-carboxamide
-
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2-amino-6-ethyl-7-(trifluoromethyl)-1,8-naphthyridine-3-carboxamide
-
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2-amino-6-methyl-7-(trifluoromethyl)-1,8-naphthyridine-3-carboxamide
-
-
2-amino-7,8-difluoro-5-oxo-5H-chromeno[2,3-b]pyridine-3-carboxamide
-
powerful inhibitor, exhibits good inhibition at nanomolar concentrations, worse inhibitor than 2-amino-7-fluoro-5-oxo-4a,10a-dihydro-5H-chromeno[2,3-b]pyridine-3-carboxamide
2-amino-7-(trifluoromethyl)-1,8-naphthyridine-3-carboxamide
-
-
2-amino-7-chloro-5-methyl-6-(prop-2-en-1-yl)-1,8-naphthyridine-3-carboxamide
-
-
2-amino-7-chloro-5-methyl-6-(pyridin-4-ylmethyl)-1,8-naphthyridine-3-carboxamide
-
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2-amino-7-fluoro-5-oxo-5H-chromeno[2,3-b]pyridine-3-carboxamide
-
powerful inhibitor, exhibits good inhibition at nanomolar concentrations, better inhibitor than 2-amino-7,8-difluoro-5-oxo-4a,10a-dihydro-5H-chromeno[2,3-b]pyridine-3-carboxamide
2-amino-7-[2-(benzyloxy)propan-2-yl]-6-bromo-1,8-naphthyridine-3-carboxamide
-
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2-iodo-AMP
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-
2-iodo-NAD+
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2-methylthio ADP
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2-methylthio-ATP
-
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2-phenyl-NAD+
-
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2-[(bicyclo[3.1.0]hexan-3-yl)oxy]-5'-deoxyadenosine
-
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2-[(decahydronaphthalen-2-yl)oxy]-5'-deoxyadenosine
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2-[(decahydronaphthalen-2-yl)oxy]adenosine
-
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3'-chloro-2-(cyclopentyloxy)-3',5'-dideoxyadenosine
-
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3'-chloro-2-(cyclopentyloxy)-3'-deoxyadenosine
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3'-chloro-3',5'-dideoxy-2-[(spiro[2.2]pentan-1-yl)methoxy]adenosine
-
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3-(4-amino-2-[(2-methylcyclohexyl)oxy]-5-oxopyrido[2,3-d]pyrimidin-8(5H)-yl)propanenitrile
-
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3-amino-6-[(6-chloro-2-methoxyacridin-9-yl)amino]heptan-1-ol
-
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3-chloro-9-[[5-(diethylammonio)pentan-2-yl]amino]-7-methoxyacridin-2-aminium
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3-chloro-N9-[5-(diethylamino)pentan-2-yl]-7-methoxyacridine-2,9-diamine
-
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3-[[[[(2R,3S,4R,5R)-5-(6-amino-2-iodo-9H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl]oxy](hydroxy)phosphoryl]carbamoyl]-1-[5-O-(hydroxyphosphinato)-beta-D-ribofuranosyl]pyridin-1-ium
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3-[[[[(2R,3S,4R,5R)-5-(6-amino-2-phenyl-9H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl]oxy](hydroxy)phosphoryl]carbamoyl]-1-[5-O-(hydroxyphosphinato)-beta-D-ribofuranosyl]pyridin-1-ium
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4-([4-amino-2-[(2-methylcyclohexyl)oxy]-5-oxopyrido[2,3-d]pyrimidin-8(5H)-yl]methyl)benzoic acid
-
-
4-amino-2-(1,4-dioxaspiro[4.5]dec-8-yloxy)-8-[(1R)-2-hydroxycyclopentyl]pyrido[2,3-d]pyrimidin-5(8H)-one
-
-
4-amino-2-(2-fluoroethoxy)-8-(2-hydroxyethyl)pyrido[2,3-d]pyrimidin-5(8H)-one
-
-
4-amino-2-(cyclopentylamino)-8-(2-hydroxyethyl)pyrido[2,3-d]pyrimidin-5(8H)-one
-
-
4-amino-2-(cyclopentyloxy)-8-(2-hydroxyethyl)pyrido[2,3-d]pyrimidin-5(8H)-one
-
-
4-amino-2-(cyclopentylsulfanyl)-8-(2-hydroxyethyl)pyrido[2,3-d]pyrimidin-5(8H)-one
-
-
4-amino-2-(cyclopentylsulfanyl)-8-[(1R)-2-hydroxycyclopentyl]pyrido[2,3-d]pyrimidin-5(8H)-one
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-
4-amino-2-[(1,3-difluoropropan-2-yl)oxy]-8-(2-hydroxyethyl)pyrido[2,3-d]pyrimidin-5(8H)-one
-
-
4-amino-2-[(2,4-dimethylcyclohexyl)oxy]-8-[(1R)-2-hydroxycyclopentyl]pyrido[2,3-d]pyrimidin-5(8H)-one
-
-
4-amino-2-[(2-methylcyclohexyl)oxy]-8-(1H-pyrazol-4-ylmethyl)pyrido[2,3-d]pyrimidin-5(8H)-one
-
-
4-amino-2-[(2-methylcyclohexyl)oxy]-8-[(1R,5R)-7-oxo-6-oxabicyclo[3.2.1]oct-4-yl]pyrido[2,3-d]pyrimidin-5(8H)-one
-
-
4-amino-2-[(4-chlorocyclohexyl)oxy]-8-[(1R)-2-hydroxycyclopentyl]pyrido[2,3-d]pyrimidin-5(8H)-one
-
-
4-amino-6-(1H-benzimidazol-2-yl)pyridazin-3(2H)-one
-
-
4-amino-8-(2,3-dihydroxypropyl)-2-[(2-methylcyclohexyl)oxy]pyrido[2,3-d]pyrimidin-5(8H)-one
-
-
4-amino-8-(2-hydroxyethyl)-2-(2-methylcyclohexyl)pyrido[2,3-d]pyrimidin-5(8H)-one
-
-
4-amino-8-(2-hydroxyethyl)-2-(4-methylcyclohexyl)pyrido[2,3-d]pyrimidin-5(8H)-one
-
-
4-amino-8-(2-hydroxyethyl)-2-(propan-2-yloxy)pyrido[2,3-d]pyrimidin-5(8H)-one
-
-
4-amino-8-(3-fluoro-2-hydroxypropyl)-2-[(2-methylcyclohexyl)oxy]pyrido[2,3-d]pyrimidin-5(8H)-one
-
-
4-amino-8-(cyclopent-3-en-1-ylmethyl)-2-[(2-methylcyclohexyl)oxy]pyrido[2,3-d]pyrimidin-5(8H)-one
-
-
4-amino-8-[(1R)-2-hydroxycyclopentyl]-2-[[4-(trifluoromethyl)cyclohexyl]oxy]pyrido[2,3-d]pyrimidin-5(8H)-one
-
-
4-amino-8-[(1S)-2,3-dihydroxycyclopentyl]-2-[(4-methylcyclohexyl)oxy]pyrido[2,3-d]pyrimidin-5(8H)-one
-
-
4-amino-8-[(1S,2S)-2-hydroxycyclopentyl]-2-[(4-methylcyclohexyl)oxy]pyrido[2,3-d]pyrimidin-5(8H)-one
-
-
4-amino-8-[(2R)-2-hydroxycyclohexyl]-2-[(2-methylcyclohexyl)oxy]pyrido[2,3-d]pyrimidin-5(8H)-one
-
-
4-amino-8-[(2R)-2-hydroxycyclopentyl]-2-[(4-methylcyclohexyl)oxy]pyrido[2,3-d]pyrimidin-5(8H)-one
-
-
4-amino-8-[(2S,5S)-2,5-dihydroxycyclopentyl]-2-[(4-methylcyclohexyl)oxy]pyrido[2,3-d]pyrimidin-5(8H)-one
-
-
4-amino-8-[(3,4-dihydroxycyclopentyl)methyl]-2-[(2-methylcyclohexyl)oxy]pyrido[2,3-d]pyrimidin-5(8H)-one
-
-
4-amino-8-[[(2R)-2-hydroxycyclopentyl]methyl]-2-[(2-methylcyclohexyl)oxy]pyrido[2,3-d]pyrimidin-5(8H)-one
-
-
4-amino-8-[[(4S)-4-hydroxytetrahydrofuran-3-yl]methyl]-2-[(2-methylcyclohexyl)oxy]pyrido[2,3-d]pyrimidin-5(8H)-one
-
-
5'-deoxy-2-(spiro[2.2]pent-1-ylmethoxy)adenosine
-
-
5'-deoxy-2-phenoxyadenosine
-
-
5'-deoxy-2-[(spiro[2.2]pentan-1-yl)methoxy]adenosine
-
-
5'-deoxy-2-[(trans-4-methylcyclohexyl)oxy]adenosine
-
-
5'-deoxy-2-[(tricyclo[3.3.1.1~3,7~]decan-2-yl)methoxy]adenosine
-
-
5'-deoxy-5'-fluoro-2-[(1,3-thiazol-2-yl)methoxy]adenosine
-
-
5'-deoxy-5'-fluoro-2-[(trans-4-methylcyclohexyl)oxy]adenosine
-
-
5'-deoxy-5'-fluoro-2-[[1-(hydroxymethyl)cyclopropyl]methoxy]adenosine
-
-
5,7-diamino-2-(2-methylpropyl)-4a,8a-dihydropyrido[2,3-d]pyrimidine-6-carbonitrile
-
-
5,7-diamino-2-(cyclohexylmethyl)-4a,8a-dihydropyrido[2,3-d]pyrimidine-6-carbonitrile
-
-
5,7-diamino-2-(propan-2-yl)-4a,8a-dihydropyrido[2,3-d]pyrimidine-6-carbonitrile
-
-
5,7-diamino-2-benzyl-4a,8a-dihydropyrido[2,3-d]pyrimidine-6-carbonitrile
-
-
5,7-diamino-2-cyclobutyl-4a,8a-dihydropyrido[2,3-d]pyrimidine-6-carbonitrile
-
-
5,7-diamino-2-cyclohexyl-4a,8a-dihydropyrido[2,3-d]pyrimidine-6-carbonitrile
-
-
5,7-diamino-2-cyclopentyl-4a,8a-dihydropyrido[2,3-d]pyrimidine-6-carbonitrile
-
-
5,7-diamino-2-cyclopropyl-4a,8a-dihydropyrido[2,3-d]pyrimidine-6-carbonitrile
-
-
5,7-diamino-2-methyl-4a,8a-dihydropyrido[2,3-d]pyrimidine-6-carbonitrile
-
-
5,7-diamino-2-phenyl-4a,8a-dihydropyrido[2,3-d]pyrimidine-6-carbonitrile
-
-
5,7-diamino-2-tert-butyl-4-(1,3-thiazol-2-yl)-4a,8a-dihydropyrido[2,3-d]pyrimidine-6-carbonitrile
-
-
5,7-diamino-2-tert-butyl-4-(1H-imidazol-1-yl)-4a,8a-dihydropyrido[2,3-d]pyrimidine-6-carbonitrile
-
-
5,7-diamino-2-tert-butyl-4-(3H-1,2,4-triazol-3-yl)-4a,8a-dihydropyrido[2,3-d]pyrimidine-6-carbonitrile
-
-
5,7-diamino-2-tert-butyl-4-(3H-pyrazol-3-yl)-4a,8a-dihydropyrido[2,3-d]pyrimidine-6-carbonitrile
-
-
5,7-diamino-2-tert-butyl-4-(4,5-dihydro-1,3-oxazol-2-yl)-4a,8a-dihydropyrido[2,3-d]pyrimidine-6-carbonitrile
-
-
5,7-diamino-2-tert-butyl-4-(4-cyanobutyl)-4a,8a-dihydropyrido[2,3-d]pyrimidine-6-carbonitrile
-
-
5,7-diamino-2-tert-butyl-4-(4-methyl-1H-imidazol-1-yl)-4a,8a-dihydropyrido[2,3-d]pyrimidine-6-carbonitrile
-
-
5,7-diamino-2-tert-butyl-4-(4H-1,2,3-triazol-4-yl)-4a,8a-dihydropyrido[2,3-d]pyrimidine-6-carbonitrile
-
-
5,7-diamino-2-tert-butyl-4-(5-cyanopentyl)-4a,8a-dihydropyrido[2,3-d]pyrimidine-6-carbonitrile
-
-
5,7-diamino-2-tert-butyl-4-(5-cyclohexylpentyl)-4a,8a-dihydropyrido[2,3-d]pyrimidine-6-carbonitrile
-
-
5,7-diamino-2-tert-butyl-4-(methylsulfanyl)-4a,8a-dihydropyrido[2,3-d]pyrimidine-6-carbonitrile
-
-
5,7-diamino-2-tert-butyl-4-(pyridin-2-yl)-4a,8a-dihydropyrido[2,3-d]pyrimidine-6-carbonitrile
-
-
5,7-diamino-2-tert-butyl-4-(pyridin-3-yl)-4a,8a-dihydropyrido[2,3-d]pyrimidine-6-carbonitrile
-
-
5,7-diamino-2-tert-butyl-4-(pyridin-4-yl)-4a,8a-dihydropyrido[2,3-d]pyrimidine-6-carbonitrile
-
-
5,7-diamino-2-tert-butyl-4-(pyrimidin-4-yl)-4a,8a-dihydropyrido[2,3-d]pyrimidine-6-carbonitrile
-
-
5,7-diamino-2-tert-butyl-4-(thiophen-2-yl)-4a,8a-dihydropyrido[2,3-d]pyrimidine-6-carbonitrile
-
-
5,7-diamino-2-tert-butyl-4-(thiophen-3-yl)-4a,8a-dihydropyrido[2,3-d]pyrimidine-6-carbonitrile
-
-
5,7-diamino-2-tert-butyl-4-cyclopentyl-4a,8a-dihydropyrido[2,3-d]pyrimidine-6-carbonitrile
-
-
5,7-diamino-2-tert-butyl-4-methyl-4a,8a-dihydropyrido[2,3-d]pyrimidine-6-carbonitrile
-
-
5,7-diamino-2-tert-butyl-4-phenyl-4a,8a-dihydropyrido[2,3-d]pyrimidine-6-carbonitrile
-
-
5,7-diamino-2-tert-butyl-4-propyl-4a,8a-dihydropyrido[2,3-d]pyrimidine-6-carbonitrile
-
-
5,7-diamino-2-tert-butyl-4-[4-(hydroxymethyl)-1,3-thiazol-2-yl]-4a,8a-dihydropyrido[2,3-d]pyrimidine-6-carbonitrile
-
-
5,7-diamino-2-tert-butyl-4-[4-(methoxymethyl)-1,3-thiazol-2-yl]-4a,8a-dihydropyrido[2,3-d]pyrimidine-6-carbonitrile
-
-
5,7-diamino-2-tert-butyl-4a,8a-dihydropyrido[2,3-d]pyrimidine-6-carbonitrile
-
-
5,7-diamino-4a,8a-dihydropyrido[2,3-d]pyrimidine-6-carbonitrile
-
-
5-(5,7-diamino-2-tert-butyl-6-cyano-4a,8a-dihydropyrido[2,3-d]pyrimidin-4-yl)thiophene-2-carboxylic acid
-
-
5-([4-amino-2-[(4-methylcyclohexyl)oxy]-5-oxopyrido[2,3-d]pyrimidin-8(5H)-yl]methyl)thiophene-2-carboxylic acid
-
-
6-chloro-2-methoxy-N-[4-(piperidin-1-yl)pentyl]acridin-9-amine
-
-
6-chloro-9-[[5-(diethylammonio)pentan-2-yl]amino]-2-methoxyacridinium
-
-
7-amino-2-tert-butyl-4-(1H-pyrrol-2-yl)-4a,8a-dihydropyrido[2,3-d]pyrimidine-6-carboxamide
-
-
7-methoxy-6-methylpteridine-2,4-diamine
-
-
ADP
-
inhibits adenylation reaction
AMP
-
inhibits adenylation reaction
ATP
-
inhibits adenylation reaction
cAMP
-
inhibits adenylation reaction
Chloroquine
doxorubicin
-
doxorubicin inhibits the ATP-dependent DNA ligase of bacteriophage T4 and the Escherichia coli NAD+-dependent ligase with a similar potency
ethyl 2-(5,7-diamino-2-tert-butyl-6-cyano-4a,8a-dihydropyrido[2,3-d]pyrimidin-4-yl)-1,3-thiazole-4-carboxylate
-
-
ethyl 2-(5,7-diamino-2-tert-butyl-6-cyano-4a,8a-dihydropyrido[2,3-d]pyrimidin-4-yl)-1,3-thiazole-5-carboxylate
-
-
hydroxychloroquine
-
specific inhibitor of the Escherichia coli enzyme
Mn2+
-
activation at 0.2-1.0 mM, inhibition at higher concentration
N'-(6-chloro-2-methoxyacridin-9-yl)-N,N-diethylbutane-1,4-diamine
-
-
N'-(6-chloro-2-methoxyacridin-9-yl)-N,N-dimethylbutane-1,4-diamine
-
-
N,N'-bis[4-((4-(diethylamino)-1-methylbutyl)amino)-quinoline-6-yl]sebacamide
-
powerful inhibitor, exhibits good inhibition at nanomolar concentrations
N,N'-bis[4-((4-(diethylamino)-1-methylbutyl)amino)-quinoline-8-yl]adipamide
-
powerful inhibitor, exhibits good inhibition at nanomolar concentrations
N,N-bis(4-aminobutyl)-N'-(6-chloro-2-methoxyacridin-9-yl)butane-1,4-diamine
-
-
N,N-bis(4-aminobutyl)-N'-(6-chloro-2-methoxyacridin-9-yl)pentane-1,5-diamine
-
-
N-(4-aminobutyl)-N-(3-aminopropyl)-N'-(6-chloro-2-methoxyacridin-9-yl)butane-1,4-diamine
-
-
N-(4-aminobutyl)-N-(3-aminopropyl)-N'-(6-chloro-2-methoxyacridin-9-yl)pentane-1,5-diamine
-
-
N-(4-aminobutyl)-N-[3-[(6-chloro-2-methoxyacridin-9-yl)amino]propyl]butane-1,4-diamine
-
-
N-(6-chloro-2-methoxyacridin-9-yl)butane-1,4-diamine
-
-
N1,N1-bis(2-chloroethyl)-N4-(6-chloro-2-methoxyacridin-9-yl)pentane-1,4-diamine
-
-
NAD+
-
inhibitory above 0.1 mM, activity is abolished at 0.5 mM
pyridochromanones
-
differently substituted compounds tested and all found to be inhibitory, competitive with NAD+, inhibitory in nano-molar rage without affecting human DNA-ligase (ATP-depentend) activity
-
Quinacrine
Rp-cAMPS
-
-
Sp-cAMPS
-
-
tert-butyl 3-(7-amino-3-bromo-6-carbamoyl-1,8-naphthyridin-2-yl)azetidine-1-carboxylate
-
-
additional information
-
not inhibited by cinchonidine, quinine, and N,N'-bis[4chloroquinolin-8-yl]succinamide
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Macromolecular solutes
-
blunt-end ligation in presence of high concentrations of macromolecular solutes, inactive in absence, e.g. polyethylene glycol 6000, bovine plasma albumin, or Ficoll 70
-
Rad51
-
Rad51 enhances Escherichia coli DNA ligase-catalyzed DNA ligation to produce multimers in an ADP-dependent manner
-
RecA
-
when incubated with linear double stranded DNA with 3' four-nucleotide overhangs and ATP, RecA greatly accelerates the end-joining to form multimers of the double stranded DNA catalyzed by NAD-dependent Escherichia coli DNA ligase
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000025 - 0.00056
5'-phosphate terminus of deoxyribonucleotides
-
-
-
0.00003 - 0.076
NAD+
0.00018 - 0.00204
nicked DNA
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0008 - 0.03
nicked DNA
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.12
(2R,3S,4R,5R)-5-(6-amino-2-iodo-9H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl dihydrogen phosphate
Escherichia coli
-
pH and temperature not specified in the publication
0.0015
(3aR,5R,6R,6aS)-5-[6-amino-2-(methylsulfanyl)-9H-purin-9-yl]-6-hydroxy-2-sulfanyltetrahydro-2H-2lambda-5-furo[2,3-d][1,3,2]dioxaphosphol-2-one
Escherichia coli
-
pH and temperature not specified in the publication
0.0000488
(3S)-3-[4-amino-2-[(4-methylcyclohexyl)oxy]-5-oxopyrido[2,3-d]pyrimidin-8(5H)-yl]-4-hydroxycyclopentanecarboxamide
Escherichia coli
-
pH and temperature not specified in the publication
0.000051
(3S)-3-[4-amino-2-[(4-methylcyclohexyl)oxy]-5-oxopyrido[2,3-d]pyrimidin-8(5H)-yl]-4-hydroxycyclopentanecarboxylic acid
Escherichia coli
-
pH and temperature not specified in the publication
0.00002
(4-amino-2-[(2-methylcyclohexyl)oxy]-5-oxopyrido[2,3-d]pyrimidin-8(5H)-yl)acetonitrile
Escherichia coli
-
pH and temperature not specified in the publication
0.12
(Rp)-3',5'-cyclic adenosine monophosphothiolate
Escherichia coli
-
37°C, pH 7.4, DNA ligation
0.0009
2,4-diamino-5-oxo-5H-chromeno[2,3-b]pyridine-3-carbonitrile
Escherichia coli
-
-
0.00023
2,4-diamino-7-tert-butyl-4a,8a-dihydro-1,8-naphthyridine-3-carbonitrile
Escherichia coli
-
at pH 7.4 and 20°C
0.00127
2-(butylsulfanyl)adenosine
0.000158 - 0.00016
2-(cyclobutylmethoxy)-5'-deoxy-5'-fluoroadenosine
0.00037
2-(cyclopentyloxy)-5'-deoxyadenosine
0.01
2-amino-5-(2-hydroxyethyl)-7-(trifluoromethyl)-1,8-naphthyridine-3-carboxamide
Escherichia coli
-
pH and temperature not specified in the publication
0.01
2-amino-5-(2-methoxyethyl)-7-(trifluoromethyl)-1,8-naphthyridine-3-carboxamide
Escherichia coli
-
pH and temperature not specified in the publication
0.0025
2-amino-5-(aminomethyl)-7-(trifluoromethyl)-1,8-naphthyridine-3-carboxamide
Escherichia coli
-
pH and temperature not specified in the publication
0.0005
2-amino-5-methyl-7-(trifluoromethyl)-1,8-naphthyridine-3-carboxamide
Escherichia coli
-
pH and temperature not specified in the publication
0.0001
2-amino-5-oxo-5H-chromeno[2,3-b]pyridine-3-carboxamide
Escherichia coli
-
-
0.0025
2-amino-5-phenyl-7-(trifluoromethyl)-1,8-naphthyridine-3-carboxamide
Escherichia coli
-
pH and temperature not specified in the publication
0.001
2-amino-5-[(3R)-3-aminopyrrolidin-1-yl]-6-bromo-7-(trifluoromethyl)-1,8-naphthyridine-3-carboxamide
Escherichia coli
-
pH and temperature not specified in the publication
0.001
2-amino-6-(2-phenylethyl)-7-(trifluoromethyl)-1,8-naphthyridine-3-carboxamide
Escherichia coli
-
value above, pH and temperature not specified in the publication
0.0005
2-amino-6-(hydroxymethyl)-7-(trifluoromethyl)-1,8-naphthyridine-3-carboxamide
Escherichia coli
-
pH and temperature not specified in the publication
0.0008
2-amino-6-(propan-2-yl)-7-(trifluoromethyl)-1,8-naphthyridine-3-carboxamide
Escherichia coli
-
pH and temperature not specified in the publication
0.0008
2-amino-6-benzyl-7-(trifluoromethyl)-1,8-naphthyridine-3-carboxamide
Escherichia coli
-
pH and temperature not specified in the publication
0.0005
2-amino-6-benzyl-7-chloro-5-methyl-1,8-naphthyridine-3-carboxamide
Escherichia coli
-
pH and temperature not specified in the publication
0.0005
2-amino-6-bromo-5-(3-hydroxyazetidin-1-yl)-7-(trifluoromethyl)-1,8-naphthyridine-3-carboxamide
Escherichia coli
-
pH and temperature not specified in the publication
0.0007
2-amino-6-bromo-5-(4-hydroxypiperidin-1-yl)-7-(trifluoromethyl)-1,8-naphthyridine-3-carboxamide
Escherichia coli
-
pH and temperature not specified in the publication
0.0007
2-amino-6-bromo-5-[(2-hydroxyethyl)(methyl)amino]-7-(trifluoromethyl)-1,8-naphthyridine-3-carboxamide
Escherichia coli
-
pH and temperature not specified in the publication
0.0007
2-amino-6-bromo-5-[(3R)-3-hydroxypyrrolidin-1-yl]-7-(trifluoromethyl)-1,8-naphthyridine-3-carboxamide
Escherichia coli
-
pH and temperature not specified in the publication
0.0003
2-amino-6-bromo-7-(trifluoromethyl)-1,8-naphthyridine-3-carboxamide
Escherichia coli
-
pH and temperature not specified in the publication
0.0005
2-amino-6-bromo-7-cyclopentyl-1,8-naphthyridine-3-carboxamide
Escherichia coli
-
pH and temperature not specified in the publication
0.0003
2-amino-6-bromo-7-tert-butyl-1,8-naphthyridine-3-carboxamide
Escherichia coli
-
pH and temperature not specified in the publication
0.008
2-amino-6-chloro-5-ethyl-1,8-naphthyridine-3-carboxamide
Escherichia coli
-
pH and temperature not specified in the publication
0.0025
2-amino-6-cyclopentyl-7-(trifluoromethyl)-1,8-naphthyridine-3-carboxamide
Escherichia coli
-
pH and temperature not specified in the publication
0.0004
2-amino-6-cyclopropyl-7-(trifluoromethyl)-1,8-naphthyridine-3-carboxamide
Escherichia coli
-
pH and temperature not specified in the publication
0.0004
2-amino-6-ethenyl-7-(trifluoromethyl)-1,8-naphthyridine-3-carboxamide
Escherichia coli
-
pH and temperature not specified in the publication
0.0006
2-amino-6-ethyl-7-(trifluoromethyl)-1,8-naphthyridine-3-carboxamide
Escherichia coli
-
pH and temperature not specified in the publication
0.0005
2-amino-6-methyl-7-(trifluoromethyl)-1,8-naphthyridine-3-carboxamide
Escherichia coli
-
pH and temperature not specified in the publication
0.00008
2-amino-7,8-difluoro-5-oxo-5H-chromeno[2,3-b]pyridine-3-carboxamide
Escherichia coli
-
-
0.0005
2-amino-7-(trifluoromethyl)-1,8-naphthyridine-3-carboxamide
Escherichia coli
-
pH and temperature not specified in the publication
0.0008
2-amino-7-chloro-5-methyl-6-(prop-2-en-1-yl)-1,8-naphthyridine-3-carboxamide
Escherichia coli
-
pH and temperature not specified in the publication
0.001
2-amino-7-chloro-5-methyl-6-(pyridin-4-ylmethyl)-1,8-naphthyridine-3-carboxamide
Escherichia coli
-
pH and temperature not specified in the publication
0.00004
2-amino-7-fluoro-5-oxo-5H-chromeno[2,3-b]pyridine-3-carboxamide
Escherichia coli
-
-
0.005
2-amino-7-[2-(benzyloxy)propan-2-yl]-6-bromo-1,8-naphthyridine-3-carboxamide
Escherichia coli
-
value above, pH and temperature not specified in the publication
0.0041
2-methylthio ADP
Escherichia coli
-
37°C, pH 7.4, DNA ligation
0.0011
2-methylthio ATP
Escherichia coli
-
37°C, pH 7.4, DNA ligation
0.000036
3-(4-amino-2-[(2-methylcyclohexyl)oxy]-5-oxopyrido[2,3-d]pyrimidin-8(5H)-yl)propanenitrile
Escherichia coli
-
pH and temperature not specified in the publication
0.138
3-[[[[(2R,3S,4R,5R)-5-(6-amino-2-iodo-9H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl]oxy](hydroxy)phosphoryl]carbamoyl]-1-[5-O-(hydroxyphosphinato)-beta-D-ribofuranosyl]pyridin-1-ium
Escherichia coli
-
pH and temperature not specified in the publication
0.000019
4-([4-amino-2-[(2-methylcyclohexyl)oxy]-5-oxopyrido[2,3-d]pyrimidin-8(5H)-yl]methyl)benzoic acid
Escherichia coli
-
pH and temperature not specified in the publication
0.00009
4-amino-2-(1,4-dioxaspiro[4.5]dec-8-yloxy)-8-[(1R)-2-hydroxycyclopentyl]pyrido[2,3-d]pyrimidin-5(8H)-one
Escherichia coli
-
pH and temperature not specified in the publication
0.00195
4-amino-2-(2-fluoroethoxy)-8-(2-hydroxyethyl)pyrido[2,3-d]pyrimidin-5(8H)-one
Escherichia coli
-
pH and temperature not specified in the publication
0.01
4-amino-2-(cyclopentylamino)-8-(2-hydroxyethyl)pyrido[2,3-d]pyrimidin-5(8H)-one
Escherichia coli
-
pH and temperature not specified in the publication
0.0051
4-amino-2-(cyclopentyloxy)-8-(2-hydroxyethyl)pyrido[2,3-d]pyrimidin-5(8H)-one
Escherichia coli
-
pH and temperature not specified in the publication
0.0035
4-amino-2-(cyclopentylsulfanyl)-8-(2-hydroxyethyl)pyrido[2,3-d]pyrimidin-5(8H)-one
Escherichia coli
-
pH and temperature not specified in the publication
0.000063
4-amino-2-(cyclopentylsulfanyl)-8-[(1R)-2-hydroxycyclopentyl]pyrido[2,3-d]pyrimidin-5(8H)-one
Escherichia coli
-
pH and temperature not specified in the publication
0.00031
4-amino-2-[(1,3-difluoropropan-2-yl)oxy]-8-(2-hydroxyethyl)pyrido[2,3-d]pyrimidin-5(8H)-one
Escherichia coli
-
pH and temperature not specified in the publication
0.00017
4-amino-2-[(2,4-dimethylcyclohexyl)oxy]-8-[(1R)-2-hydroxycyclopentyl]pyrido[2,3-d]pyrimidin-5(8H)-one
Escherichia coli
-
pH and temperature not specified in the publication
0.000036
4-amino-2-[(2-methylcyclohexyl)oxy]-8-(1H-pyrazol-4-ylmethyl)pyrido[2,3-d]pyrimidin-5(8H)-one
Escherichia coli
-
pH and temperature not specified in the publication
0.000028
4-amino-2-[(2-methylcyclohexyl)oxy]-8-[(1R,5R)-7-oxo-6-oxabicyclo[3.2.1]oct-4-yl]pyrido[2,3-d]pyrimidin-5(8H)-one
Escherichia coli
-
pH and temperature not specified in the publication
0.000041
4-amino-2-[(4-chlorocyclohexyl)oxy]-8-[(1R)-2-hydroxycyclopentyl]pyrido[2,3-d]pyrimidin-5(8H)-one
Escherichia coli
-
pH and temperature not specified in the publication
0.025
4-amino-6-(1H-benzimidazol-2-yl)pyridazin-3(2H)-one
Escherichia coli
-
value above, pH and temperature not specified in the publication
0.000079
4-amino-8-(2,3-dihydroxypropyl)-2-[(2-methylcyclohexyl)oxy]pyrido[2,3-d]pyrimidin-5(8H)-one
Escherichia coli
-
pH and temperature not specified in the publication
0.000057
4-amino-8-(2-hydroxyethyl)-2-(2-methylcyclohexyl)pyrido[2,3-d]pyrimidin-5(8H)-one
Escherichia coli
-
pH and temperature not specified in the publication
0.00042
4-amino-8-(2-hydroxyethyl)-2-(4-methylcyclohexyl)pyrido[2,3-d]pyrimidin-5(8H)-one
Escherichia coli
-
pH and temperature not specified in the publication
0.00106
4-amino-8-(2-hydroxyethyl)-2-(propan-2-yloxy)pyrido[2,3-d]pyrimidin-5(8H)-one
Escherichia coli
-
pH and temperature not specified in the publication
0.000028
4-amino-8-(3-fluoro-2-hydroxypropyl)-2-[(2-methylcyclohexyl)oxy]pyrido[2,3-d]pyrimidin-5(8H)-one
Escherichia coli
-
pH and temperature not specified in the publication
0.00002
4-amino-8-(cyclopent-3-en-1-ylmethyl)-2-[(2-methylcyclohexyl)oxy]pyrido[2,3-d]pyrimidin-5(8H)-one
Escherichia coli
-
pH and temperature not specified in the publication
0.00035
4-amino-8-[(1R)-2-hydroxycyclopentyl]-2-[[4-(trifluoromethyl)cyclohexyl]oxy]pyrido[2,3-d]pyrimidin-5(8H)-one
Escherichia coli
-
pH and temperature not specified in the publication
0.000225
4-amino-8-[(1S)-2,3-dihydroxycyclopentyl]-2-[(4-methylcyclohexyl)oxy]pyrido[2,3-d]pyrimidin-5(8H)-one
Escherichia coli
-
pH and temperature not specified in the publication
0.000039
4-amino-8-[(1S,2S)-2-hydroxycyclopentyl]-2-[(4-methylcyclohexyl)oxy]pyrido[2,3-d]pyrimidin-5(8H)-one
Escherichia coli
-
pH and temperature not specified in the publication
0.00011
4-amino-8-[(2R)-2-hydroxycyclohexyl]-2-[(2-methylcyclohexyl)oxy]pyrido[2,3-d]pyrimidin-5(8H)-one
Escherichia coli
-
pH and temperature not specified in the publication
0.00019
4-amino-8-[(2R)-2-hydroxycyclopentyl]-2-[(4-methylcyclohexyl)oxy]pyrido[2,3-d]pyrimidin-5(8H)-one
Escherichia coli
-
pH and temperature not specified in the publication
0.000076
4-amino-8-[(2S,5S)-2,5-dihydroxycyclopentyl]-2-[(4-methylcyclohexyl)oxy]pyrido[2,3-d]pyrimidin-5(8H)-one
Escherichia coli
-
pH and temperature not specified in the publication
0.000068
4-amino-8-[(3,4-dihydroxycyclopentyl)methyl]-2-[(2-methylcyclohexyl)oxy]pyrido[2,3-d]pyrimidin-5(8H)-one
Escherichia coli
-
pH and temperature not specified in the publication
0.00004
4-amino-8-[[(2R)-2-hydroxycyclopentyl]methyl]-2-[(2-methylcyclohexyl)oxy]pyrido[2,3-d]pyrimidin-5(8H)-one
Escherichia coli
-
pH and temperature not specified in the publication
0.000038
4-amino-8-[[(4S)-4-hydroxytetrahydrofuran-3-yl]methyl]-2-[(2-methylcyclohexyl)oxy]pyrido[2,3-d]pyrimidin-5(8H)-one
Escherichia coli
-
pH and temperature not specified in the publication
0.00018
5'-deoxy-2-(spiro[2.2]pent-1-ylmethoxy)adenosine
Escherichia coli
-
pH 7.5, 22°C
0.00018
5'-deoxy-2-[(spiro[2.2]pentan-1-yl)methoxy]adenosine
Escherichia coli
-
pH and temperature not specified in the publication
0.00032
5'-deoxy-2-[(trans-4-methylcyclohexyl)oxy]adenosine
Escherichia coli
-
pH and temperature not specified in the publication
0.00032
5'-deoxy-5'-fluoro-2-[(trans-4-methylcyclohexyl)oxy]adenosine
Escherichia coli
-
pH 7.5, 22°C
0.00049
5-([4-amino-2-[(4-methylcyclohexyl)oxy]-5-oxopyrido[2,3-d]pyrimidin-8(5H)-yl]methyl)thiophene-2-carboxylic acid
Escherichia coli
-
pH and temperature not specified in the publication
0.000077
7-amino-2-tert-butyl-4-(1H-pyrrol-2-yl)-4a,8a-dihydropyrido[2,3-d]pyrimidine-6-carboxamide
Escherichia coli
-
at pH 7.4 and 20°C
0.025
7-methoxy-6-methylpteridine-2,4-diamine
Escherichia coli
-
pH and temperature not specified in the publication
0.053
Chloroquine
Escherichia coli
-
-
0.063
hydroxychloroquine
Escherichia coli
-
-
0.0018
N,N'-bis[4-((4-(diethylamino)-1-methylbutyl)amino)-quinoline-6-yl]sebacamide
Escherichia coli
-
-
0.009
N,N'-bis[4-((4-(diethylamino)-1-methylbutyl)amino)-quinoline-8-yl]adipamide
Escherichia coli
-
-
0.0015
Quinacrine
Escherichia coli
-
-
0.0015
Sp-3',5'-cyclic adenosine monophosphothiolate
Escherichia coli
-
37°C, pH 7.4, DNA ligation
0.005
tert-butyl 3-(7-amino-3-bromo-6-carbamoyl-1,8-naphthyridin-2-yl)azetidine-1-carboxylate
Escherichia coli
-
value above, pH and temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5
-
NAD+/nicotinamide nucleotide exchange reaction
7.5 - 8
-
Tris-HCl buffer
8
-
sodium phosphate buffer
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.6 - 7.5
-
50% of maximal activity at pH 5.6 and 7.5, potassium phosphate buffer
6.5 - 9
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10 - 15
-
ligation of cohesive ends
20
-
mutant enzyme L15F has 20fold lower ligation activity in vitro than wild-type enzyme
42
-
mutant enzyme L15F has 60fold lower ligation activity in vitro than wild-type enzyme
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 37
-
activity at 20°C is lower than at 37°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
the enzyme repairs 3'-OH/5'-PO4 nicks in duplex DNA via reaction with NAD+ to form a covalent enzyme-(lysyl-Nzeta)-AMP intermediate, transfer of AMP to the nick 5'-PO4 to form an AppDNA intermediate (step 2), and attack of the nick 3'-OH on AppDNA to form a 3'-5' phosphodiester
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
73610
calculated from amino acid sequence
74000
-
1 * 74000, SDS-PAGE of denatured and reduced enzyme
76000
-
SDS-PAGE, recombinant protein
77000
-
sedimentation equilibrium ultracentrifugation
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
-
1 * 74000, SDS-PAGE of denatured and reduced enzyme
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion method at 22°C. 2.3 A crystal structure of Escherichia coli LigA bound to an adenylylated nick, which captures LigA in a state poised for strand closure and reveals the basis for nick recognition. LigA envelops the DNA within a protein clamp
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D450A
the helix-hairpin-helix domain mutant retains DNA relaxation function, concordant with the ability to effectively ligate nicks
D452A
mutant with 68% of wild type activity
D551A
E519A
G489A
the mutant retains 25% of wild type activity
G489D
mutant with 0.8% of wild type activity
G489V
mutant with 3.2% of wild type activity
G521A
the mutant is 50fold less active than wild type LigA
G521D
mutant with less than 0.1% of wild type function
G521V
mutant with less than 0.1% of wild type function
G553A
mutant with 38% of wild type activity
G553D
mutant with 2.6% of wild type activity
G553V
mutant with 0.9% of wild type activity
I384A
the mutant is defective for nick sealing, retaining 4% of wild type activity
K627A
mutant with 40% of wild type activity
K634A/K635A
mutant with 44% of wild type activity
K648A
mutant with 37% of wild type activity
K651A
mutant with 35% of wild type activity
N355A
mutant with 30% of wild type activity
Q330A
the mutation has no apparent effect on nick sealing acivity
Q386A
mutant with 30% of wild type activity
R333A
the oligonucleotide-binding domain mutation strongly suppresses DNA relaxation
R379A
the oligonucleotide-binding domain mutation strongly suppresses DNA relaxation
R487A
mutant with 6% of wild type activity
R510A
the helix-hairpin-helix domain mutant retains DNA relaxation function, concordant with the ability to effectively ligate nicks
R614A
mutant with 14% of wild type activity
V383A
the mutant is defective for nick sealing, retaining 4% of wild type activity
C408A
-
inactive, unable to complement DNA-ligase-deficient yeast
C411A
-
inactive, unable to complement DNA-ligase-deficient yeast
C426A
-
no effect in vivo, 7% of wild type activity
C432A
-
inactive, unable to complement DNA-ligase-deficient yeast
D117A
-
inactive in nick-joining, unable to complement DNA-ligase-deficient yeast
D117E
-
3% of ligase activity of wild-type enzyme, lethal mutation
D117N
-
less than 0.1% of ligase activity of wild-type enzyme, lethal mutation
D138A
-
37% of ligase activity of wild-type enzyme
D283A
-
57% of ligase activity of wild-type enzyme
D285E
-
4% of ligase activity of wild-type enzyme, lethal mutation
D285N
-
less than 0.1% of ligase activity of wild-type enzyme, lethal mutation
D32A
-
traces of nick joining activity
D32E
-
traces of nick joining activity
D32N
-
9% of nick joining activity, strongly reduced self-adenylation
D36A
-
traces of nick joining activity
D36E
-
4% of nick joining activity, strongly reduced self-adenylation
D36N
-
12% of nick joining activity, strongly reduced self-adenylation
DELTA1-38
DELTA1-592
-
fragment corresponding to BRCT domain binds to a wider range of substrates compared to full-length LigA
DELTA1-78
DELTA593-671
-
mutant lacking the BRCT domain, 3fold reduced in vitro ligation activity and reduced DNA binding
E10A
-
90% of nick joining activity
E113A
-
no effect in vivo, increased Km for NAD+, 40% of wild type activity
E143A
-
52% of ligase activity of wild-type enzyme
E173A
-
less than 0.1% of ligase activity of wild-type enzyme, lethal mutation
E173D
-
less than 0.1% of ligase activity of wild-type enzyme, lethal mutation
E173Q
-
less than 0.1% of ligase activity of wild-type enzyme, lethal mutation
E319A
-
no effect in vivo, 69% of wild type activity
G118A
-
less than 0.1% of ligase activity of wild-type enzyme, lethal mutation
G172A
-
36% of ligase activity of wild-type enzyme
G286A
-
14% of ligase activity of wild-type enzyme
H23A
-
10% of nick joining activity
H23Y
-
88% of nick joining activity
K115A
-
inactive in nick-joining, unable to complement DNA-ligase-deficient yeast
K115Q
-
less than 0.1% of ligase activity of wild-type enzyme, lethal mutation
K115R
-
less than 0.1% of ligase activity of wild-type enzyme, lethal mutation
K126A
-
inactive
K290A
-
13% of ligase activity of wild-type enzyme, lethal mutation
K314A [DV1]
-
accumulation of the DNA-adenylate intermediate, loss of function in vivo, strongly reduced activity
K314Q
-
less than 0.1% of ligase activity of wild-type enzyme, lethal mutation
K314R
-
5% of ligase activity of wild-type enzyme, lethal mutation
L119A
-
110% of ligase activity of wild-type enzyme
L15F
-
at 20°C mutant enzyme L15F has 20fold lower ligation activity in vitro, and its activity is reduced at 42°C, resulting in 60fold lower ligation activity than wild-type LigA
N198A
-
26% of ligase activity of wild-type enzyme
Q318A
-
no effect in vivo, 80% of wild type activity
R200A
-
less than 0.1% of ligase activity of wild-type enzyme, lethal mutation
R200K
-
less than 0.1% of ligase activity of wild-type enzyme, lethal mutation
R200Q
-
less than 0.1% of ligase activity of wild-type enzyme, lethal mutation
R208A
-
2% of ligase activity of wild-type enzyme, lethal mutation
R208K
-
1.2% of ligase activity of wild-type enzyme, lethal mutation
R208Q
-
less than 0.1% of ligase activity of wild-type enzyme, lethal mutation
R277A
R277K
-
5.6% of ligase activity of wild-type enzyme, themperature-sensitive mutation, rate of isolated sealing step is 4% of the activity of wild-type enzyme
R277Q
-
1.8% of ligase activity of wild-type enzyme, lethal mutation, rate of isolated sealing step is 10% of the activity of wild-type enzyme
V288A
-
74% of ligase activity of wild-type enzyme
Y225A
-
no effect in vivo, increased Km for NAD+, 25% of wild type activity
Y22A
-
traces of nick joining activity, strongly reduced self-adenylation
Y22S
-
9% of nick joining activity
Y35A
-
2% of nick joining activity, strongly reduced self-adenylation
Y35S
-
23% of nick joining activity
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
95
-
50% of activity lost within 5 min
additional information
-
thermal stability is increased by cofactor binding
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-agarose column chromatography
His-tag used for purification of recombinant enzymes
-
large scale
-
Ni-agarose column chromatography, and Superdex 200 gel filtration
-
recombinant protein from Escherichia coli GR501 using His-tag
-
recombinant protein using His-tag
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
capable of complementing DNA-ligase-deficient yeast, wild type and mutants expressed in Escherichia coli BL21(DE3)
-
expressed in Escherichia coli BL21 (DE3)
-
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli GR501, that contains a temperature sensitive mutation in ligA and is therefore unable to grow above 42°C, expression of protein enables Escherichia coli GR501 to grow at 44°C
-
ligase fragments and mutant
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
medicine
synthesis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Engler, M.J.; Richardson, C.C.
DNA ligases
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
15
3-29
1982
Bacillus subtilis, Escherichia coli, Salmonella enterica subsp. enterica serovar Typhimurium
-
Manually annotated by BRENDA team
Maunders, M.J.
DNA and RNA ligases (EC 6.5.1.1, EC 6.5.1.2, and EC 6.5.1.3)
Methods Mol. Biol.
16
213-230
1993
Bacillus subtilis, Escherichia coli, Thermus thermophilus, Salmonella enterica subsp. enterica serovar Typhimurium
Manually annotated by BRENDA team
Hayashi, K.; Nakazawa, M.; Ishizaki, Y.; Hiraoka, N.; Obayashi, A.
Stimulation of intermolecular ligation with E. coli DNA ligase by high concentrations of monovalent cations in polyethylene glycol solutions
Nucleic Acids Res.
13
7979-7992
1985
Escherichia coli
Manually annotated by BRENDA team
Zimmerman, S.B.; Pheiffer, B.H.
Macromolecular crowding allows blunt-end ligation by DNA ligases from rat liver or Escherichia coli
Proc. Natl. Acad. Sci. USA
80
5852-5856
1983
Escherichia coli
Manually annotated by BRENDA team
Higgins, N.P.; Cozzarelli, N.R.
DNA-joining enzymes: A review
Methods Enzymol.
68
50-71
1979
Escherichia coli
Manually annotated by BRENDA team
Panasenko, S.M.; Alazard, R.J.; Lehman, I.R.
A simple, three-step procedure for the large scale purification of DNA ligase from a hybrid lysogen constructed in vitro
J. Biol. Chem.
253
4590-4592
1978
Escherichia coli
Manually annotated by BRENDA team
Modrich, P.; Anraku, Y.; Lehman, I.R.
Deoxyribonucleic acid ligase. Isolation and physical characterization of the homogenous enzyme from Escherichia coli
J. Biol. Chem.
248
7475-7501
1973
Escherichia coli
-
Manually annotated by BRENDA team
Georlette, D.; Jonsson, Z.O.; Van Petegem, F.; Chessa, J.P.; Van Beeumen, J.; Hubscher, U.; Gerday, C.
A DNA ligase from the psychrophile Pseudoalteromonas haloplanktis gives insights into the adaptation of proteins to low temperatures
Eur. J. Biochem.
267
3502-3512
2000
Escherichia coli, Thermus scotoductus, Pseudoalteromonas haloplanktis (Q9RBF2)
Manually annotated by BRENDA team
Lim, J.H.; Choi, J.; Han, S.J.; Kim, S.H.; Hwang, H.Z.; Jin, D.K.; Ahn, B.Y.; Han, Y.S.
Molecular cloning and characterization of thermostable DNA ligase from Aquifex pyrophilus, a hyperthermophilic bacterium
Extremophiles
5
161-168
2001
Aquifex pyrophilus (Q9F150), Escherichia coli, Thermus aquaticus
Manually annotated by BRENDA team
Sriskanda, V.; Shuman, S.
Conserved residues in domain Ia are required for the reaction of Escherichia coli DNA ligase with NAD+
J. Biol. Chem.
277
9695-9700
2002
Escherichia coli
Manually annotated by BRENDA team
Brotz-Oesterhelt, H.; Knezevic, I.; Bartel, S.; Lampe, T.; Warnecke-Eberz, U.; Ziegelbauer, K.; Habich, D.; Labischinski, H.
Specific and potent inhibition of NAD+-dependent DNA ligase by pyridochromanones
J. Biol. Chem.
278
39435-39442
2003
Escherichia coli
Manually annotated by BRENDA team
Georlette, D.; Blaise, V.; Dohmen, C.; Bouillenne, F.; Damien, B.; Depiereux, E.; Gerday, C.; Uversky, V.N.; Feller, G.
Cofactor Binding modulates the conformational stabilities and unfolding patterns of NAD+-dependent DNA ligases from Escherichia coli and Thermus scotoductus
J. Biol. Chem.
278
49945-49953
2003
Escherichia coli, Thermus scotoductus
Manually annotated by BRENDA team
Sriskanda, V.; Schwer, B.; Ho, C.K.; Shuman, S.
Mutational analysis of Escherichia coli DNA ligase identifies amino acids required for nick-ligation in vitro and for in vivo complementation of the growth of yeast cells deleted for CDC9 and LIG4
Nucleic Acids Res.
27
3953-3963
1999
Escherichia coli
Manually annotated by BRENDA team
Sriskanda, V.; Shuman, S.
A second NAD+-dependent DNA ligase (LigB) in Escherichia coli
Nucleic Acids Res.
29
4930-4934
2001
Escherichia coli
Manually annotated by BRENDA team
Wilkinson, A.; Sayer, H.; Bullard, D.; Smith, A.; Day, J.; Kieser, T.; Bowater, R.
NAD+-dependent DNA ligases of Mycobacterium tuberculosis and Streptomyces coelicolor
Proteins Struct. Funct. Genet.
51
321-326
2003
Escherichia coli, Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv, Streptomyces coelicolor, Streptomyces coelicolor A3(2)
Manually annotated by BRENDA team
Zauner, G.; Wang, Y.; Lavesa-Curto, M.; MacDonald, A.; Mayes, A.G.; Bowater, R.P.; Butt, J.N.
Tethered DNA hairpins facilitate electrochemical detection of DNA ligation
Analyst
130
345-349
2005
Escherichia coli
Manually annotated by BRENDA team
Wilkinson, A.; Smith, A.; Bullard, D.; Lavesa-Curto, M.; Sayer, H.; Bonner, A.; Hemmings, A.; Bowater, R.
Analysis of ligation and DNA binding by Escherichia coli DNA ligase (LigA)
Biochim. Biophys. Acta
1749
113-122
2005
Escherichia coli
Manually annotated by BRENDA team
Zhu, H.; Shuman, S.
Structure-guided mutational analysis of the nucleotidyltransferase domain of Escherichia coli NAD+-dependent DNA ligase (LigA)
J. Biol. Chem.
280
12137-12144
2005
Escherichia coli
Manually annotated by BRENDA team
Lavesa-Curto, M.; Sayer, H.; Bullard, D.; MacDonald, A.; Wilkinson, A.; Smith, A.; Bowater, L.; Hemmings, A.; Bowater, R.P.
Characterization of a temperature-sensitive DNA ligase from Escherichia coli
Microbiology
150
4171-4180
2004
Escherichia coli, Escherichia coli DSM 3757
Manually annotated by BRENDA team
Miesel, L.; Kravec, C.; Xin, A.T.; McMonagle, P.; Ma, S.; Pichardo, J.; Feld, B.; Barrabee, E.; Palermo, R.
A high-throughput assay for the adenylation reaction of bacterial DNA ligase
Anal. Biochem.
366
9-17
2007
Escherichia coli
Manually annotated by BRENDA team
Nandakumar, J.; Nair, P.A.; Shuman, S.
Last stop on the road to repair: structure of E. coli DNA ligase bound to nicked DNA-adenylate
Mol. Cell
26
257-271
2007
Escherichia coli (P15042)
Manually annotated by BRENDA team
Vacek, J.; Cahova, K.; Palecek, E.; Bullard, D.R.; Lavesa-Curto, M.; Bowater, R.P.; Fojta, M.
Label-free electrochemical monitoring of DNA ligase activity
Anal. Chem.
80
7609-7613
2008
Escherichia coli
Manually annotated by BRENDA team
Li, J.; Jiang, J.H.; Xu, X.M.; Chu, X.; Jiang, C.; Shen, G.; Yu, R.Q.
Simultaneous identification of point mutations via DNA ligase-mediated gold nanoparticle assembly
Analyst
133
939-945
2008
Escherichia coli
Manually annotated by BRENDA team
Pascal, J.M.
DNA and RNA ligases: structural variations and shared mechanisms
Curr. Opin. Struct. Biol.
18
96-105
2008
Escherichia coli, Enterococcus faecalis, Thermus filiformis
Manually annotated by BRENDA team
Wang, L.K.; Nair, P.A.; Shuman, S.
Structure-guided mutational analysis of the OB, HhH, and BRCT domains of Escherichia coli DNA ligase
J. Biol. Chem.
283
23343-23352
2008
Escherichia coli (P15042)
Manually annotated by BRENDA team
Dwivedi, N.; Dube, D.; Pandey, J.; Singh, B.; Kukshal, V.; Ramachandran, R.; Tripathi, R.P.
NAD+-dependent DNA ligase: a novel target waiting for the right inhibitor
Med. Res. Rev.
28
545-568
2008
Escherichia coli, Geobacillus stearothermophilus (O87703), Mycobacterium tuberculosis (P9WNV1), Enterococcus faecalis (Q837V6), Thermus filiformis (Q9ZHI0), Mycobacterium tuberculosis H37Rv (P9WNV1)
Manually annotated by BRENDA team
Luan, Q.; Xue, Y.; Yao, X.; Lu, W.
Hairpin DNA probe based surface plasmon resonance biosensor used for the activity assay of E. coli DNA ligase
Analyst
135
414-418
2010
Escherichia coli
Manually annotated by BRENDA team
Shuman, S.
DNA ligases: progress and prospects
J. Biol. Chem.
284
17365-17369
2009
Escherichia coli (P15042), Enterococcus faecalis (Q837V6)
Manually annotated by BRENDA team
Mills, S.D.; Eakin, A.E.; Buurman, E.T.; Newman, J.V.; Gao, N.; Huynh, H.; Johnson, K.D.; Lahiri, S.; Shapiro, A.B.; Walkup, G.K.; Yang, W.; Stokes, S.S.
Novel bacterial NAD+-dependent DNA ligase inhibitors with broad-spectrum activity and antibacterial efficacy in vivo
Antimicrob. Agents Chemother.
55
1088-1096
2011
Escherichia coli, Escherichia coli MG1655, Haemophilus influenzae, Haemophilus influenzae KW20, Mycoplasma pneumoniae, Mycoplasma pneumoniae M29, Staphylococcus aureus, Staphylococcus aureus RN4220, Streptococcus pneumoniae
Manually annotated by BRENDA team
Akhoon, B.A.; Gupta, S.K.; Dhaliwal, G.; Srivastava, M.; Gupta, S.K.
Virtual screening of specific chemical compounds by exploring E.coli NAD+-dependent DNA ligase as a target for antibacterial drug discovery
J. Mol. Model.
17
265-273
2011
Escherichia coli
Manually annotated by BRENDA team
He, X.; Ni, X.; Wang, Y.; Wang, K.; Jian, L.
Electrochemical detection of nicotinamide adenine dinucleotide based on molecular beacon-like DNA and E. coli DNA ligase
Talanta
83
937-942
2011
Escherichia coli
Manually annotated by BRENDA team
Wang, T.; Duncan, L.; Gu, W.; ODowd, H.; Wei, Y.; Perola, E.; Parsons, J.; Gross, C.H.; Moody, C.S.; Arends, S.J.; Charifson, P.S.
Design, synthesis and biological evaluation of potent NAD+-dependent DNA ligase inhibitors as potential antibacterial agents. Part 2: 4-amino-pyrido[2,3-d]pyrimidin-5(8H)-ones
Bioorg. Med. Chem. Lett.
22
3699-3703
2012
Escherichia coli
Manually annotated by BRENDA team
Surivet, J.P.; Lange, R.; Hubschwerlen, C.; Keck, W.; Specklin, J.L.; Ritz, D.; Bur, D.; Locher, H.; Seiler, P.; Strasser, D.S.; Prade, L.; Kohl, C.; Schmitt, C.; Chapoux, G.; Ilhan, E.; Ekambaram, N.; Athanasiou, A.; Knezevic, A.; Sabato, D.; Chambovey, A.; Gaertner, M.; Enderlin, M.; Boehme, M.; Sipp, S.i.p.p.e.
Structure-guided design, synthesis and biological evaluation of novel DNA ligase inhibitors with in vitro and in vivo anti-staphylococcal activity
Bioorg. Med. Chem. Lett.
22
6705-6711
2012
Escherichia coli
Manually annotated by BRENDA team
Jiang, C.; Kan, Y.Y.; Jiang, J.H.; Yu, R.Q.
A simple and highly sensitive DNAzyme-based assay for nicotinamide adenine dinucleotide by ligase-mediated inhibition of strand displacement amplification
Anal. Chim. Acta
844
70-74
2014
Escherichia coli
Manually annotated by BRENDA team
Murphy-Benenato, K.E.; Gingipalli, L.; Boriack-Sjodin, P.A.; Martinez-Botella, G.; Carcanague, D.; Eyermann, C.J.; Gowravaram, M.; Harang, J.; Hale, M.R.; Ioannidis, G.; Jahic, H.; Johnstone, M.; Kutschke, A.; Laganas, V.A.; Loch, J.T.; Miller, M.D.; Oguto, H.; Patel, S.J.
Negishi cross-coupling enabled synthesis of novel NAD+-dependent DNA ligase inhibitors and SAR development
Bioorg. Med. Chem. Lett.
25
5172-5177
2015
Streptococcus pneumoniae, Escherichia coli, Haemophilus influenzae, Staphylococcus aureus, Haemophilus influenzae ARM158, Escherichia coli ARC524, Streptococcus pneumoniae ARC548, Staphylococcus aureus ARC561
Manually annotated by BRENDA team
Pergolizzi, G.; Wagner, G.K.; Bowater, R.P.
Biochemical and structural characterisation of DNA ligases from bacteria and archaea
Biosci. Rep.
36
e00391
2016
Streptococcus pneumoniae, Escherichia coli, Haemophilus influenzae, Staphylococcus aureus, Mycobacterium tuberculosis, Mycoplasma pneumoniae
Manually annotated by BRENDA team
Chauleau, M.; Shuman, S.
Kinetic mechanism and fidelity of nick sealing by Escherichia coli NAD+-dependent DNA ligase (LigA)
Nucleic Acids Res.
44
2298-2309
2016
Escherichia coli
Manually annotated by BRENDA team
Konomura, N.; Arai, N.; Shinohara, T.; Kobayashi, J.; Iwasaki, W.; Ikawa, S.; Kusano, K.; Shibata, T.
Rad51 and RecA juxtapose dsDNA ends ready for DNA ligase-catalyzed end-joining under recombinase-suppressive conditions
Nucleic Acids Res.
45
337-352
2017
Escherichia coli
Manually annotated by BRENDA team
Pergolizzi, G.; Cominetti, M.M.; Butt, J.N.; Field, R.A.; Bowater, R.P.; Wagner, G.K.
Base-modified NAD and AMP derivatives and their activity against bacterial DNA ligases
Org. Biomol. Chem.
13
6380-6398
2015
Escherichia coli, Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
Manually annotated by BRENDA team