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Literature summary for 1.5.1.53 extracted from

  • Jencks, D.A.; Mathews, R.G.
    Allosteric inhibition of methylenetetrahydrofolate reductase by adenosylmethionine. Effects of adenosylmethionine and NADPH on the equilibrium between active and inactive forms of the enzyme and on the kinetics of approach to equilibrium (1987), J. Biol. Chem., 262, 2485-2493 .
    View publication on PubMed
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Inhibitors

Inhibitors Comment Organism Structure
NADPH substrate inhibition. NADPH and S-adenosyl-L-methionine play antagonistic roles in the allosteric regulation, with NADPH recruiting active forms of the enzyme and S-adenosyl-L-methionine recruiting inactive forms. Enzyme can adopt two states, R and T. NADPH and S-adenosyl-L-methionine exhibit antagonistic binding to a given subunit, so that occupancy by one ligand decreases or abolishes affinity for the other ligand. Within a given state, the subunits do not interact with each other. R-T transitions occur between all similarly ligated states Sus scrofa
S-adenosyl-L-methionine NADPH and S-adenosyl-L-methionine play antagonistic roles in the allosteric regulation, with NADPH recruiting active forms of the enzyme and S-adenosyl-L-methionine recruiting inactive forms. Enzyme can adopt two states, R and T. NADPH and S-adenosyl-L-methionine exhibit antagonistic binding to a given subunit, so that occupancy by one ligand decreases or abolishes affinity for the other ligand. Within a given state, the subunits do not interact with each other. R-T transitions occur between all similarly ligated states Sus scrofa

Organism

Organism UniProt Comment Textmining
Sus scrofa
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