Literature summary for 1.5.1.3 extracted from

Boehr, D.D.; Dyson, H.J.; Wright, P.E.
Conformational relaxation following hydride transfer plays a limiting role in dihydrofolate reductase catalysis (2008), Biochemistry, 47, 9227-9233.

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Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P0ABQ4	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
5,6,7,8-tetrahydrofolate + NADP+ = 7,8-dihydrofolate + NADPH + H+	the active-site loop dynamics access a closed conformation, and the accompanying closed to occluded rate constant is comparable to the maximum pH-independent hydride transfer rate constant. The closed to occluded conformational transition in the product ternary complex is a prerequisite for progression through the catalytic cycle. The rate of this process places an effective limit on the maximum rate of the hydride transfer step. The dynamics of the C-terminally associated region is pH-dependent, but the dynamics of the active-site loops and cofactor binding cleft are pH-independent	Escherichia coli	a

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
additional information	-	additional information	analysis of kinetic and thermodynamic fitting parameters and relaxation dispersion curves at different pH values and temperatures	Escherichia coli

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Release 2023.1 (January 2023)