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Literature summary for 1.5.1.3 extracted from

  • Navarro-Peran, E.; Cabezas-Herrera, J.; Hiner, A.N.; Sadunishvili, T.; Garcia-Canovas, F.; Rodriguez-Lopez, J.N.
    Kinetics of the inhibition of bovine liver dihydrofolate reductase by tea catechins: origin of slow-binding inhibition and pH studies (2005), Biochemistry, 44, 7512-7525.
    View publication on PubMed
Search for more literature for 1.5.1.3

Inhibitors

Inhibitors Comment Organism Structure
(-)-epicatechin gallate competitive to 7,8-dihydrofolate, formation of a slow dissociation ternary complex by the reaction of NADPH with the enzyme-inhibitor complex. Ionization state of E30 is critical for inhibitory activity Bos taurus
(-)-epigallocatechin gallate competitive to 7,8-dihydrofolate, formation of a slow dissociation ternary complex by the reaction of NADPH with the enzyme-inhibitor complex. Ionization state of E30 is critical for inhibitory activity Bos taurus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.00043
-
 NADPH 25°C, pH 7.6 Bos taurus

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
 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+
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
5.1
-
 NADPH 25°C, pH 7.6 Bos taurus

Cofactor

Cofactor Comment Organism Structure
NADP+
-
 Bos taurus
NADPH
-
 Bos taurus

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.000082
-
 (-)-epicatechin gallate 25°C, pH 7.6 Bos taurus
0.00012
-
 (-)-epigallocatechin gallate 25°C, pH 7.6 Bos taurus