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Literature summary for 1.5.1.3 extracted from

  • McElheny, D.; Schnell, J.R.; Lansing, J.C.; Dyson, H.J.; Wright, P.E.
    Defining the role of active-site loop fluctuations in dihydrofolate reductase catalysis (2005), Proc. Natl. Acad. Sci. USA, 102, 5032-5037.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
study on enzyme ternary complex with substrate analogue folates and oxidized NADP+ cofactor using NMR relaxation methods. Conformational exchanges of protein between a ground state with closed conformation of active site loops and an excited state with loops in occluded conformation. Fluctuations include motions of the nicotinamide ring of the cofactor into and out of the active site Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P0ABQ4
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Reaction

Reaction Comment Organism Reaction ID
5,6,7,8-tetrahydrofolate + NADP+ = 7,8-dihydrofolate + NADPH + H+ study on enzyme ternary complex with substrate analogue folates and oxidized NADP+ cofactor using NMR relaxation methods. Conformational exchanges of protein between a ground state with closed conformation of active site loops and an excited state with loops in occluded conformation. Fluctuations include motions of the nicotinamide ring of the cofactor into and out of the active site Escherichia coli