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Literature summary for 2.1.1.45 extracted from

  • Osorio, E.; Aguilera, C.; Naranjo, N.; Marin, M.; Muskus, C.
    Biochemical characterization of the bifunctional enzyme dihydrofolate reductase-thymidylate synthase from Leishmania (Viannia) and its evaluation as a drug target (2014), Biomedica, 33, 393-401.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Leishmania braziliensis

Inhibitors

Inhibitors Comment Organism Structure
methotrexate most potent inhibitor of dihydrofolate reductase activity Leishmania braziliensis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
58000
-
x * 58000, calculated, x * 58000, SDS-PAGE Leishmania braziliensis

Organism

Organism UniProt Comment Textmining
Leishmania braziliensis A4H4P8 bifunctional dihydrofolate reductase-thymidylate synthase
-

Storage Stability

Storage Stability Organism
-20°C, pH 6.0, stable over a period of 1 month Leishmania braziliensis

Subunits

Subunits Comment Organism
? x * 58000, calculated, x * 58000, SDS-PAGE Leishmania braziliensis