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Literature summary for 1.5.1.3 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

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

Molecular Weight [Da]

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Bos taurus
-
2 forms
-

Purification (Commentary)

Purification (Comment) Organism
2 forms Bos taurus

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Bos taurus
-

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

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

Temperature Stability [°C]

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

Cofactor

Cofactor Comment Organism Structure
NADPH
-
Bos taurus