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Literature summary for 1.5.1.3 extracted from

  • Baccanari, D.P.; Averett, D.; Briggs, C.; Burchall, J.
    Escherichia coli dihydrofolate reductase: isolation and characterization of two isozymes (1977), Biochemistry, 16, 3566-3572.
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information
-
Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
18500
-
? * 18500, SDS-PAGE, isozyme I and II Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
isoenzymes type I and type II, resistant to trimethoprim
-

Purification (Commentary)

Purification (Comment) Organism
trimethoprim-resistant Escherichia coli

Source Tissue

Source Tissue Comment Organism Textmining

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
7.4
-
isozyme II Escherichia coli
85
-
isozyme I Escherichia coli

Subunits

Subunits Comment Organism
? ? * 18500, SDS-PAGE, isozyme I and II Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
additional information
-
trimethoprim-resistant, form 2: no detectable pH-optimum, continuous increase of activity as pH decreases from pH 9.0 to pH 4.0 Escherichia coli
4.5
-
trimethoprim-resistant, 7,8-dihydrofolate, form I Escherichia coli

Cofactor

Cofactor Comment Organism Structure
NADPH
-
Escherichia coli

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
additional information
-
additional information Ki of substrates 7,8-dihydrofolate and NADPH for the 2 isozymes Escherichia coli