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Literature summary for 6.5.1.2 extracted from

  • Poidevin, L.; MacNeill, S.A.
    Biochemical characterisation of LigN, an NAD+-dependent DNA ligase from the halophilic euryarchaeon Haloferax volcanii that displays maximal in vitro activity at high salt concentrations (2006), BMC Mol. Biol., 7, 44.
    View publication on PubMedView publication on EuropePMC

Application

Application Comment Organism
biotechnology LigN is unique amongst DNA ligase enzymes in displaying maximal DNA strand joining activity at above 3 M salt levels. As such the LigN enzyme has potential both as a novel tool for biotechnology and as a model enzyme for studying the adaptation of proteins to high intracellular salt levels Haloferax volcanii

Cloned(Commentary)

Cloned (Comment) Organism
wild-type and mutant forms of LigN are expressed in Escherichia coli Haloferax volcanii

Protein Variants

Protein Variants Comment Organism
D141A adenylation-defective mutant Haloferax volcanii
K139A adenylation-defective mutant Haloferax volcanii

Metals/Ions

Metals/Ions Comment Organism Structure
KCl no activity is detected in the absence of KCl. Maximum activity at 3.2 M KCl, close to the intracellular KCl concentration of Haloferax volcanii cells Haloferax volcanii

Organism

Organism UniProt Comment Textmining
Haloferax volcanii
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant Haloferax volcanii

Synonyms

Synonyms Comment Organism
LigN
-
Haloferax volcanii