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 (Comment) | Organism |
---|---|
wild-type and mutant forms of LigN are expressed in Escherichia coli | Haloferax volcanii |
Protein Variants | Comment | Organism |
---|---|---|
D141A | adenylation-defective mutant | Haloferax volcanii |
K139A | adenylation-defective mutant | Haloferax volcanii |
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 | UniProt | Comment | Textmining |
---|---|---|---|
Haloferax volcanii | - |
- |
- |
Purification (Comment) | Organism |
---|---|
recombinant | Haloferax volcanii |
Synonyms | Comment | Organism |
---|---|---|
LigN | - |
Haloferax volcanii |