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Literature summary for 6.5.1.2 extracted from

  • Chauleau, M.; Shuman, S.
    Kinetic mechanism and fidelity of nick sealing by Escherichia coli NAD+-dependent DNA ligase (LigA) (2016), Nucleic Acids Res., 44, 2298-2309 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 6.5.1.2

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21(DE3) cells Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
NH4+ stimulates enzyme activity at 10 mM Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
NAD+ + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m Escherichia coli
-
 (deoxyribonucleotide)n+m + AMP + beta-nicotinamide D-nucleotide
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Ni-agarose column chromatography, and Superdex 200 gel filtration Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme is relatively tolerant of 5'-phosphate base mispairs and 5' N:abasic lesions Escherichia coli ?
-
 ?
NAD+ + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m
-
 Escherichia coli (deoxyribonucleotide)n+m + AMP + beta-nicotinamide D-nucleotide
-
 ?

Synonyms

Synonyms Comment Organism
LigA
-
 Escherichia coli
NAD+-dependent DNA ligase
-
 Escherichia coli

Cofactor

Cofactor Comment Organism Structure
NAD+
-
 Escherichia coli

General Information

General Information Comment Organism
physiological function the enzyme repairs 3'-OH/5'-PO4 nicks in duplex DNA via reaction with NAD+ to form a covalent enzyme-(lysyl-Nzeta)-AMP intermediate, transfer of AMP to the nick 5'-PO4 to form an AppDNA intermediate (step 2), and attack of the nick 3'-OH on AppDNA to form a 3'-5' phosphodiester Escherichia coli