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Literature summary extracted from

  • Baumann, H.; Wilson, K.L.
    Dihydrofolate reductase from bovine liver. Enzymatic and structural properties (1975), Eur. J. Biochem., 60, 9-15.
    View publication on PubMed

General Stability

EC Number General Stability Organism
1.5.1.3 7,8-dihydrofolate protects against inactivation Bos taurus
1.5.1.3 unstable to dialysis and lyophilization and concentration by membrane filtration under nitrogen Bos taurus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.5.1.3 23000
-
SDS-PAGE in presence of 2-mercaptoethanol Bos taurus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.5.1.3 additional information Bos taurus key enzyme in the biosynthesis of purines, pyrimidines and several amino acids ?
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.5.1.3 Bos taurus
-
2 forms
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.5.1.3 2 forms Bos taurus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.5.1.3 liver
-
Bos taurus
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.5.1.3 29.69
-
-
Bos taurus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.5.1.3 7,8-dihydrofolate + NADPH
-
Bos taurus 5,6,7,8-tetrahydrofolate + NADP+
-
r
1.5.1.3 additional information key enzyme in the biosynthesis of purines, pyrimidines and several amino acids Bos taurus ?
-
?

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.5.1.3 4
-
above, for extended length of time, unstable Bos taurus

Cofactor

EC Number Cofactor Comment Organism Structure
1.5.1.3 NADPH
-
Bos taurus