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Literature summary for 6.5.1.2 extracted from

  • Feng, H.
    Mutational analysis of bacterial NAD+-dependent DNA ligase: role of motif IV in ligation catalysis (2007), Acta Biochim. Biophys. Sin., 39, 608-616.
    View publication on PubMed
Search for more literature for 6.5.1.2

Protein Variants

Protein Variants Comment Organism
D286E mutant enzyme shows reduced reaction rate on both match and mismatch nicked substrates compared to wild-type enzyme Thermus sp.
G287A mutant enzyme shows reduced reaction rate on both match and mismatch nicked substrates compared to wild-type enzyme. The G287A mutation has a major effect on the second step Thermus sp.
K291R mutant enzyme shows reduced reaction rate on both match and mismatch nicked substrates compared to wild-type enzyme Thermus sp.
V289I mutant enzyme shows reduced reaction rate on both match and mismatch nicked substrates compared to wild-type enzyme Thermus sp.

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
NAD+ + (deoxyribonucleotide)n + (deoxyribonucleotide)m Thermus sp.
-
 AMP + nicotinamide nucleotide + (deoxyribonucleotide)n+m
-
 ?
NAD+ + (deoxyribonucleotide)n + (deoxyribonucleotide)m Thermus sp. TAK16D
-
 AMP + nicotinamide nucleotide + (deoxyribonucleotide)n+m
-
 ?

Organism

Organism UniProt Comment Textmining
Thermus sp.
-
-
-
Thermus sp. TAK16D
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
NAD+ + (deoxyribonucleotide)n + (deoxyribonucleotide)m
-
 Thermus sp. AMP + nicotinamide nucleotide + (deoxyribonucleotide)n+m
-
 ?
NAD+ + (deoxyribonucleotide)n + (deoxyribonucleotide)m
-
 Thermus sp. TAK16D AMP + nicotinamide nucleotide + (deoxyribonucleotide)n+m
-
 ?