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Literature summary for 1.5.1.3 extracted from

  • Swanwick, R.S.; Maglia, G.; Tey, L.H.; Allemann, R.K.
    Coupling of protein motions and hydrogen transfer during catalysis by Escherichia coli dihydrofolate reductase (2006), Biochem. J., 394, 259-265.
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
G121V reduced catalytic efficiency due to significantly reduced pre-exponential factors, the chemical mechanism of catalysis is not impaired Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
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additional information analysis of steady-state kinetics at pH 9.5 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+ model for hydrogen transfer includes contributions from quantum mechanical tunnelling coupled with protein motions that actively modulate the tunnelling distance Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
additional information
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strong dependence of reaction rates on temperature. Temperature-independent kinetic isotope effects between 15 and 35°C Escherichia coli