Dihydrofolate reductase: structural aspects of mechanisms of enzyme catalysis and inhibition
β Scribed by V. I. Polshakov
- Book ID
- 110328046
- Publisher
- Springer
- Year
- 2001
- Tongue
- English
- Weight
- 585 KB
- Volume
- 50
- Category
- Article
- ISSN
- 1573-9171
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π SIMILAR VOLUMES
The ability of the enzyme dihydrofolate reductase to catalyze the formation of tetrahydrobiopterin from dihydrobiopterin was used to develop a method for measuring the activity ofthis enzyme in viva. This method can be used to determine the activity of the enzyme in tissues as well as the extent and
We have investigated the importance of polarization by the enzyme dihydrofolate reductase (DHFR) on its substrates, folate and dihydrofolate, using a series of quantum mechanical (QM) techniques (Hartree-Fock (HF), MΓΈller-Plesset second-order perturbation theory (MP2), local density approximation (L
## Abstract The migration of electron density of a substrate (folate) on binding to an enzyme (dihydrofolate reductase) is studied by a quantumβmechanical method originally developed in solid state physics. A significant polarization of the substrate is induced by the enzyme, toward the transition