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Literature summary for 1.5.1.3 extracted from

  • Boehr, D.D.; McElheny, D.; Dyson, H.J.; Wright, P.E.
    The dynamic energy landscape of dihydrofolate reductase catalysis (2006), Science, 313, 1638-1642.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
analysis of higher energy conformational substrates by NMR relaxation dispersion. The maximum hydride transfer and steady-state turnover rates are governed by the dynamics of transitions between ground and excited states of the intermediates. Model of conformational changes during the catalytic cycle 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+ analysis of higher energy conformational substrates by NMR relaxation dispersion. The maximum hydride transfer and steady-state turnover rates are governed by the dynamics of transitions between ground and excited states of the intermediates. Model of conformational changes during the catalytic cycle Escherichia coli