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Literature summary for 1.5.1.3 extracted from

  • Gundersen, L.E.; Dunlap, R.B.; Harding, N.G.L.; Freisheim, J.H.; Otting, F.; Huennekens, F.M.
    Dihydrofolate reductase from amethopterin-resistant Lactobacillus casei (1972), Biochemistry, 11, 1018-1023.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
Urea slight activation Lacticaseibacillus casei

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information
-
Lacticaseibacillus casei

Metals/Ions

Metals/Ions Comment Organism Structure
organic mercurials no activation Lacticaseibacillus casei

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
14900
-
gel filtration, ultracentrifugation, isoenzyme I Lacticaseibacillus casei

Organism

Organism UniProt Comment Textmining
Lacticaseibacillus casei
-
isozymes I and II
-
Lacticaseibacillus casei
-
amethopterin-resistant
-

Purification (Commentary)

Purification (Comment) Organism
isozymes I and II Lacticaseibacillus casei

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
7,8-dihydrofolate + NADPH
-
Lacticaseibacillus casei 5,6,7,8-tetrahydrofolate + NADP+
-
r

Subunits

Subunits Comment Organism
monomer 1 * 14900, isozyme I, SDS-PAGE Lacticaseibacillus casei

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
isozyme I Lacticaseibacillus casei

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3
-
7,8-dihydrofolate isozyme I Lacticaseibacillus casei

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.5
-
isozyme I Lacticaseibacillus casei

Cofactor

Cofactor Comment Organism Structure
NADPH isozymes I and II Lacticaseibacillus casei