Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 6.5.1.2 extracted from

  • Wang, L.K.; Nair, P.A.; Shuman, S.
    Structure-guided mutational analysis of the OB, HhH, and BRCT domains of Escherichia coli DNA ligase (2008), J. Biol. Chem., 283, 23343-23352.
    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

Protein Variants

Protein Variants Comment Organism
D450A the helix-hairpin-helix domain mutant retains DNA relaxation function, concordant with the ability to effectively ligate nicks Escherichia coli
D452A mutant with 68% of wild type activity Escherichia coli
D551A mutant with 120% of wild type activity Escherichia coli
D551A the helix-hairpin-helix domain mutant retains DNA relaxation function, concordant with the ability to effectively ligate nicks Escherichia coli
E519A mutant with 71% of wild type activity Escherichia coli
E519A the helix-hairpin-helix domain mutant retains DNA relaxation function, concordant with the ability to effectively ligate nicks Escherichia coli
G489A the mutant retains 25% of wild type activity Escherichia coli
G489D mutant with 0.8% of wild type activity Escherichia coli
G489V mutant with 3.2% of wild type activity Escherichia coli
G521A the mutant is 50fold less active than wild type LigA Escherichia coli
G521D mutant with less than 0.1% of wild type function Escherichia coli
G521V mutant with less than 0.1% of wild type function Escherichia coli
G553A mutant with 38% of wild type activity Escherichia coli
G553D mutant with 2.6% of wild type activity Escherichia coli
G553V mutant with 0.9% of wild type activity Escherichia coli
I384A the mutant is defective for nick sealing, retaining 4% of wild type activity Escherichia coli
K627A mutant with 40% of wild type activity Escherichia coli
K634A/K635A mutant with 44% of wild type activity Escherichia coli
K648A mutant with 37% of wild type activity Escherichia coli
K651A mutant with 35% of wild type activity Escherichia coli
N355A mutant with 30% of wild type activity Escherichia coli
Q330A the mutation has no apparent effect on nick sealing acivity Escherichia coli
Q386A mutant with 30% of wild type activity Escherichia coli
R333A the oligonucleotide-binding domain mutation strongly suppresses DNA relaxation Escherichia coli
R379A the oligonucleotide-binding domain mutation strongly suppresses DNA relaxation Escherichia coli
R487A mutant with 6% of wild type activity Escherichia coli
R510A the helix-hairpin-helix domain mutant retains DNA relaxation function, concordant with the ability to effectively ligate nicks Escherichia coli
R614A mutant with 14% of wild type activity Escherichia coli
V383A the mutant is defective for nick sealing, retaining 4% of wild type activity Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
73610
-
 calculated from amino acid sequence Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P15042
-
-

Purification (Commentary)

Purification (Comment) Organism
Ni-agarose column chromatography Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
NAD+ + (deoxyribonucleotide)n + (deoxyribonucleotide)m
-
 Escherichia coli AMP + nicotinamide nucleotide + (deoxyribonucleotide)n+m
-
 ?

Synonyms

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

Cofactor

Cofactor Comment Organism Structure
NAD+ dependent on Escherichia coli