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Literature summary extracted from

  • 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 (2003), J. Biol. Chem., 278, 49945-49953.
    View publication on PubMed

Application

EC Number Application Comment Organism
6.5.1.2 medicine potential target for antibiotics Escherichia coli
6.5.1.2 medicine potential target for antibiotics Thermus scotoductus

Cloned(Commentary)

EC Number Cloned (Comment) Organism
6.5.1.2
-
 Escherichia coli
6.5.1.2
-
 Thermus scotoductus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.5.1.2 NAD+ + (deoxyribonucleotide)n + (deoxyribonucleotide)m Escherichia coli DNA-repair, phosphodiester bond formation between adjacent 5'-phosphate and 3'-hydroxyl groups in double-stranded DNA AMP + nicotinamide nucleotide + (deoxyribonucleotide)n+m
-
 ?
6.5.1.2 NAD+ + (deoxyribonucleotide)n + (deoxyribonucleotide)m Thermus scotoductus DNA-repair, phosphodiester bond formation between adjacent 5'-phosphate and 3'-hydroxyl groups in double-stranded DNA AMP + nicotinamide nucleotide + (deoxyribonucleotide)n+m
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
6.5.1.2 Escherichia coli
-
-
-
6.5.1.2 Thermus scotoductus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
6.5.1.2
-
 Escherichia coli
6.5.1.2
-
 Thermus scotoductus

Reaction

EC Number Reaction Comment Organism Reaction ID
6.5.1.2 ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + beta-nicotinamide D-nucleotide 3 steps of reaction: 1. adenylation of the ligase in the presence of NAD+, 2. transferring the adenylate moiety to the 5'-phosphate of the nicked DNA substrate, 3. sealing the nick through the formation of a phosphodiester bond Escherichia coli
a
6.5.1.2 ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + beta-nicotinamide D-nucleotide 3 steps of reaction: 1. adenylation of the ligase in the presence of NAD+, 2. transferring the adenylate moiety to the 5'-phosphate of the nicked DNA substrate, 3. sealing the nick through the formation of a phosphodiester bond Thermus scotoductus
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.5.1.2 NAD+ + (deoxyribonucleotide)n + (deoxyribonucleotide)m
-
 Escherichia coli AMP + nicotinamide nucleotide + (deoxyribonucleotide)n+m
-
 ?
6.5.1.2 NAD+ + (deoxyribonucleotide)n + (deoxyribonucleotide)m
-
 Thermus scotoductus AMP + nicotinamide nucleotide + (deoxyribonucleotide)n+m
-
 ?
6.5.1.2 NAD+ + (deoxyribonucleotide)n + (deoxyribonucleotide)m DNA-repair, phosphodiester bond formation between adjacent 5'-phosphate and 3'-hydroxyl groups in double-stranded DNA Escherichia coli AMP + nicotinamide nucleotide + (deoxyribonucleotide)n+m
-
 ?
6.5.1.2 NAD+ + (deoxyribonucleotide)n + (deoxyribonucleotide)m DNA-repair, phosphodiester bond formation between adjacent 5'-phosphate and 3'-hydroxyl groups in double-stranded DNA Thermus scotoductus AMP + nicotinamide nucleotide + (deoxyribonucleotide)n+m
-
 ?

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
6.5.1.2 additional information
-
 thermal stability is increased by cofactor binding Escherichia coli
6.5.1.2 additional information
-
 thermal stability is increased by cofactor binding Thermus scotoductus

Cofactor

EC Number Cofactor Comment Organism Structure
6.5.1.2 NAD+ required, binding of cofactor induces conformational rearangement within the active site Escherichia coli
6.5.1.2 NAD+ required, binding of cofactor induces conformational rearangement within the active site Thermus scotoductus