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Literature summary for 1.5.1.3 extracted from

  • Ortenberg, R.; Rozenblatt-Rosen, O.; Mevarech, M.
    The extremely halophilic archaeon Haloferax volcanii has two very different dihydrofolate reductases (2000), Mol. Microbiol., 35, 1493-1505.
    View publication on PubMed
Search for more literature for 1.5.1.3

Activating Compound

Activating Compound Comment Organism Structure
KCl hDHFR-2, activation is maximal at 0.5 M Haloferax volcanii

Cloned(Commentary)

Cloned (Comment) Organism
overexpression of hdrB gene in Escherichia coli Haloferax volcanii

Protein Variants

Protein Variants Comment Organism
additional information construction of hdrAgene, hdrB gene and double deletion mutants Haloferax volcanii

General Stability

General Stability Organism
isozyme hDHFR-1, loss of more than 80% activity after exposure to 0.2 M KCl for 24 h at 24°C Haloferax volcanii
isozyme hDHFR-2 loss of less than 10% activity after exposure to 40 mM KCl for 18 h at 52°C Haloferax volcanii

Inhibitors

Inhibitors Comment Organism Structure
trimethoprim hDHFR-1 is much more resistant than hDHFR-2 Haloferax volcanii

Organism

Organism UniProt Comment Textmining
Haloferax volcanii
-
 isozyme hDHFR-1 from gene hdrA and isozyme hDHFR-2 from gene hdrB
-
Haloferax volcanii
-
 extremely halophilic archaebacterium
-

Purification (Commentary)

Purification (Comment) Organism
isozyme hDHFR-2 from hdrB gene overexpressed in Escherichia coli Haloferax volcanii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
7,8-dihydrofolate + NADPH
-
 Haloferax volcanii 5,6,7,8-tetrahydrofolate + NADP+
-
 ?

Synonyms

Synonyms Comment Organism
hDHFR-1
-
 Haloferax volcanii
hDHFR-2
-
 Haloferax volcanii

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
4
-
 isozyme hDHFR-1 Haloferax volcanii
6
-
 isozyme hDHFR-2 Haloferax volcanii