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Literature summary for 6.5.1.1 extracted from

  • Zhu, H.; Shuman, S.
    Gap filling activities of Pseudomonas DNA ligase D (LigD) polymerase and functional interactions of LigD with the DNA end-binding Ku protein (2010), J. Biol. Chem., 285, 4815-4825.
    View publication on PubMedView publication on EuropePMC
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Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli as His-tagged enzyme Pseudomonas aeruginosa

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + (deoxyribonucleotide)n + (deoxyribonucleotide)m Pseudomonas aeruginosa
-
 AMP + diphosphate + (deoxyribonucleotide)n+m
-
 ?

Organism

Organism UniProt Comment Textmining
Pseudomonas aeruginosa
-
-
-

Purification (Commentary)

Purification (Comment) Organism
nickel agarose column chromatography Pseudomonas aeruginosa

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + (deoxyribonucleotide)n + (deoxyribonucleotide)m
-
 Pseudomonas aeruginosa AMP + diphosphate + (deoxyribonucleotide)n+m
-
 ?

Synonyms

Synonyms Comment Organism
ATP-dependent DNA ligase
-
 Pseudomonas aeruginosa
DNA ligase D
-
 Pseudomonas aeruginosa
LigD LigD is a large multifunctional enzyme consisting of an ATP-dependent ligase domain, a polymerase domain, and a 3'-phosphoesterase domain Pseudomonas aeruginosa

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Pseudomonas aeruginosa

General Information

General Information Comment Organism
physiological function protein Ku and DNA ligase D are the central agents of the bacterial nonhomologous end joining pathway of DNA double strand break repair Pseudomonas aeruginosa