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Literature summary for 6.5.1.1 extracted from

  • Zhu, H.; Shuman, S.
    A primer-dependent polymerase function of Pseudomonas aeruginosa ATP-dependent DNA ligase (LigD) (2005), J. Biol. Chem., 280, 418-427.
    View publication on PubMed

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ nick sealing by LigD in the presence of 0.1 mM ATP requires a divalent cation cofactor. Cobalt supports the conversion of the 12-mer pDNA strand to a 24-mer which es elongated to 25-mer and 26-mer products Pseudomonas aeruginosa
Mg2+ nick sealing by LigD in the presence of 0.1 mM ATP requires a divalent cation cofactor. Magnesium supports the conversion of the 12-mer pDNA strand to a discrete 24-mer ligation product. An additional minor species corresponding to AppDNA is also produced Pseudomonas aeruginosa
Mn2+ nick sealing by LigD in the presence of 0.1 mM ATP requires a divalent cation cofactor. Conversion of the 12-mer pDNA strand results in ligated products consisting of a triplet of 24-, 25-, and 26-mer species. In addition, manganese prompted the appearance of discrete radiolabeled 13- and 14-mer species Pseudomonas aeruginosa

Organism

Organism UniProt Comment Textmining
Pseudomonas aeruginosa
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-
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Purification (Commentary)

Purification (Comment) Organism
-
Pseudomonas aeruginosa

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + (deoxyribonucleotide)n + (deoxyribonucleotide)m intrinsic polymerase function resident within an autonomous C-terminal polymerase domain, LigD-(533–840), that flanks an autonomous DNA ligase domain, LigD-(188–527) Pseudomonas aeruginosa AMP + diphosphate + (deoxyribonucleotide)m+n
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Subunits

Subunits Comment Organism
monomer
-
Pseudomonas aeruginosa

Synonyms

Synonyms Comment Organism
LigD
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Pseudomonas aeruginosa