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Literature summary for 6.5.1.2 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
Search for more literature for 6.5.1.2

Application

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

Cloned(Commentary)

Cloned (Comment) Organism
-
 Escherichia coli
-
 Thermus scotoductus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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
-
 ?
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

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Thermus scotoductus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Escherichia coli
-
 Thermus scotoductus

Reaction

Reaction Comment Organism Reaction ID
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
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)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
NAD+ + (deoxyribonucleotide)n + (deoxyribonucleotide)m
-
 Escherichia coli AMP + nicotinamide nucleotide + (deoxyribonucleotide)n+m
-
 ?
NAD+ + (deoxyribonucleotide)n + (deoxyribonucleotide)m
-
 Thermus scotoductus AMP + nicotinamide nucleotide + (deoxyribonucleotide)n+m
-
 ?
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
-
 ?
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]

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

Cofactor

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