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Literature summary for 6.5.1.1 extracted from

  • Gong, C.; Bongiorno, P.; Martins, A.; Stephanou, N.C.; Zhu, H.; Shuman, S.; Glickman, M.S.
    Mechanism of nonhomologous end-joining in mycobacteria: a low-fidelity repair system driven by Ku, ligase D and ligase C (2005), Nat. Struct. Mol. Biol., 12, 304-312.
    View publication on PubMed

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + (deoxyribonucleotide)n + (deoxyribonucleotide)m Mycolicibacterium smegmatis template-dependent and template-independent polymerase functions. LigD directs an imprecise non-homologous end-joining pathway for repairing blunt double-strand breaks. Another ATP-dependent DNA ligase (LigC) provides backup mechanism for LigD-independent error-prone repair of blunt-end double-strand breaks AMP + diphosphate + (deoxyribonucleotide)m+n
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Organism

Organism UniProt Comment Textmining
Mycolicibacterium smegmatis
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + (deoxyribonucleotide)n + (deoxyribonucleotide)m template-dependent and template-independent polymerase functions. LigD directs an imprecise non-homologous end-joining pathway for repairing blunt double-strand breaks. Another ATP-dependent DNA ligase (LigC) provides backup mechanism for LigD-independent error-prone repair of blunt-end double-strand breaks Mycolicibacterium smegmatis AMP + diphosphate + (deoxyribonucleotide)m+n
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?
ATP + (deoxyribonucleotide)n + (deoxyribonucleotide)m template-dependent and template-independent polymerase functions Mycolicibacterium smegmatis AMP + diphosphate + (deoxyribonucleotide)m+n
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?

Synonyms

Synonyms Comment Organism
ATP-dependent DNA ligase
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Mycolicibacterium smegmatis
LigC
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Mycolicibacterium smegmatis
LigD
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Mycolicibacterium smegmatis