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1.5.1.3: dihydrofolate reductase

This is an abbreviated version!
For detailed information about dihydrofolate reductase, go to the full flat file.

Word Map on EC 1.5.1.3

Reaction

5,6,7,8-tetrahydrofolate
+
NADP+
=
7,8-dihydrofolate
 +
NADPH
 +
H+

Synonyms

5,6,7,8-tetrahydrofolate: NADP+ oxidoreductase, 7,8-dihydrofolate reductase, At2g16370, At4g34570, bifunctional dihydrofolate reductase-thymidylate synthase, bifunctional TS-DHFR, BmDHFR, dehydrogenase, tetrahydrofolate, DFR-TS, DFR1, DfrA, DfrB, DHFR, DHFR type IIIC, DHFR-TS, DHFR-TS1, DHFR-TS2, DHFR2, DHFRL1, DHFRLS, dihydrofolate reductase, dihydrofolate reductase-like, dihydrofolate reductase-thymidylate synthase, dihydrofolate reductase:thymidylate synthase, dihydrofolic acid reductase, dihydrofolic reductase, EC 1.5.1.4, ecDHFR, folA, folA3, folic acid reductase, folic reductase, FolM, hDHFR, hDHFR-1, hDHFR-2, HjDHFR, hvDHFR1, hvDHFR2, LAU_0427, LBRM_06_0830, mDHFR, mjDHFR, More, myDHFR, NADPH-dihydrofolate reductase, pcDHFR, PKNH_0509600, ppDHFR, pteridine reductase, pteridine reductase:dihydrofolate reductase, PTR2, R-plasmid-encoded dihydrofolate reductase, R67 DHFR, R67 dihydrofolate reductase, reductase, dihydrofolate, S3DHFR, Smdhfr, Smp 175230, spDHFR, svDHFR, tcptr1, tetrahydrofolate dehydrogenase, THY-1, THY-2, thymidylate synthase-dihydrofolate reductase, thymidylate synthetase-dihydrofolate reductase, Trimethoprim resistance protein, TS-DHFR, WUBG_00817

ECTree

     1 Oxidoreductases
         1.5 Acting on the CH-NH group of donors
             1.5.1 With NAD+ or NADP+ as acceptor
                1.5.1.3 dihydrofolate reductase

Renatured

Renatured on EC 1.5.1.3 - dihydrofolate reductase

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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
both the chaperone systems GroEL (minichaperone) and GroEL-GroES prevent thermal aggregation and assist in refolding of DHFR
-
denaturation with 4 M urea, no renaturation by removing urea by dialysis
-
enzyme denatured with 8 M urea cannot be renatured by removal of urea
-
kinetic of refolding upon dilution of unfolded enzyme in 4.5 M urea to 1.29 M urea
-
NMR measurements of amide proton exchange protection during folding in the presence of methotrextae and ATP either free in solution or inside the stable cavity formed between a single ring variant of GroEL, SR1, and GroES chaperonins. In the SR1-GroES-mediated reaction, recovery of dihydrofolate reductase is twofold higher than in the spontaneous reaction. In both reactions, folding follows the same trajectories
refolding after solubilisation from inclusion bodies with 4 M guanidium hydrochloride in 0.5% polyethylene glycol 1450, pH 7.0
-
refolding of enzyme reversibly unfolded in 7 M urea, effect of several peptide fragments, derived from limited proteolytic cleavage of dihydrofolate reductase on the attainment of the folded state
-
refolding of recombinant enzymes from inclusion bodies due to expression in E. coli
-
sodium docecyl sulfate causes irreversible inactivation
-
study on kinetic folding of urea-denatured dihydrofolate reductase and comparison with Haloferax volcanii enzyme. Folding follows similar kinetics for both enzymes, with a 5-ms stopped-flow burst-phase species that folds to the native state through two sequential intermediateswith relaxation times of 0.1-3 sec and 25-100 sec. The unfolding of Haloferax volcanii enzyme at low ionic strength is relatively slow. Increased KCl concentrations slow the urea-induced unfolding of both enzymes, but much less than expected from equilibrium studies. Unfolding rates are relatively independent of ionic strength
-
study on kinetic folding of urea-denaturedc dihydrofolate reductase and comparison with Escherichia coli enzyme. Folding follows similar kinetics for both enzymes, with a 5-ms stopped-flow burst-phase species that folds to the native state through two sequential intermediateswith relaxation times of 0.1-3 sec and 25-100 sec. The unfolding of Haloferax volcanii enzyme at low ionic strength is relatively slow. Increased KCl concentrations slow the urea-induced unfolding of both enzymes, but much less than expected from equilibrium studies. Unfolding rates are relatively independent of ionic strength
-
very fast and total reconstitution of active recombinant wild-type enzyme from inclusion bodies due to overexpression in E. coli by 6 M guanidine hydrochloride followed by dilution into 1 M NaCl or KCl solution
-
wild-type and mutant, renaturation from inclusion bodies due to expression in E. coli, 200 mM KCl, 20 mM potassium phosphate, pH 7.0, 0.1 mM EDTA, 10 mM dithiothreitol
-