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Literature summary 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

Protein Variants

EC Number Protein Variants Comment Organism
6.5.1.2 D286E mutant enzyme shows reduced reaction rate on both match and mismatch nicked substrates compared to wild-type enzyme Thermus sp.
6.5.1.2 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.
6.5.1.2 K291R mutant enzyme shows reduced reaction rate on both match and mismatch nicked substrates compared to wild-type enzyme Thermus sp.
6.5.1.2 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)

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

Organism

EC Number Organism UniProt Comment Textmining
6.5.1.2 Thermus sp.
-
-
-
6.5.1.2 Thermus sp. TAK16D
-
-
-

Substrates and Products (Substrate)

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