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Literature summary for 1.5.1.3 extracted from

  • Wright, D.B.; Banks, D.D.; Lohman, J.R.; Hilsenbeck, J.L.; Gloss, L.M.
    The effect of salts on the activity and stability of Escherichia coli and Haloferax volcanii dihydrofolate reductases (2002), J. Mol. Biol., 323, 327-344.
    View publication on PubMed

Metals/Ions

Metals/Ions Comment Organism Structure
KCl dihydrofolate reductase hvDHFR1 and hvDHFR2 unfold at KCl concentrations below 0.5 M. Above 1 M, the KCl dependence of the dihydrofolate reductase activities can be attributed to the effect of salt on substrate affinity Haloferax volcanii

Organic Solvent Stability

Organic Solvent Comment Organism
urea dihydrofolate reductase hvDHFR1 is ,1–2 kcal/mol more stable to urea denaturation than dihydrofolate reductase hvDHFR2. NaCl, KCl, and CsCl enhance the stability to urea denaturation Haloferax volcanii

Organism

Organism UniProt Comment Textmining
Haloferax volcanii
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-
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Synonyms

Synonyms Comment Organism
hvDHFR1
-
Haloferax volcanii
hvDHFR2
-
Haloferax volcanii