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Literature summary for 1.5.1.3 extracted from

  • Batruch, I.; Javasky, E.; Brown, E.D.; Organ, M.G.; Johnson, P.E.
    Thermodynamic and NMR analysis of inhibitor binding to dihydrofolate reductase (2010), Bioorg. Med. Chem., 18, 8485-8492.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
1,4-bis-([N-(1-imino-1-guanidino-methyl)]sulfanylmethyl)-3,6-dimethyl-benzene binding of the inhibitor has both a favorable entropy and enthalpy of binding. Positive binding cooperativity between inhibitor and the cofactor NADPH. Binding of inhibitor to DHFR is 285fold tighter in the presence of the NADPH cofactor than in its absence Escherichia coli
1-([N-(1-imino-guanidino-methyl)]sulfanylmethyl)-3-trifluoromethyl-benzene binding of the inhibitor has both a favorable entropy and enthalpy of binding. Positive binding cooperativity between inhibitor and the cofactor NADPH. Binding of inhibitor to DHFR in the absence of NADPH is not observed Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P0ABQ4
-
-

Purification (Commentary)

Purification (Comment) Organism
using gel filtration Escherichia coli

Synonyms

Synonyms Comment Organism
DHFR
-
Escherichia coli
dihydrofolate reductase
-
Escherichia coli

Cofactor

Cofactor Comment Organism Structure
NADPH
-
Escherichia coli