Enzyme polarization of substrates of dihydrofolate reductase by different theoretical methods
نویسندگان
چکیده
منابع مشابه
Theoretical studies on the dihydrofolate reductase mechanism: electronic polarization of bound substrates.
We have applied local density functional theory, an ab initio quantum mechanical method, to study the shift in the spatial electron density of the substrate dihydrofolate that accompanies binding to the enzyme dihydrofolate reductase. The results shed light on fundamental electronic effects due to the enzyme that may contribute to catalysis. In particular, the enzyme induces a long-range polari...
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Construction of a homodimeric dihydrofolate reductase-thymidylate synthase bifunctional enzyme.
A gene encoding a bifunctional homodimeric dihydrofolate reductase-thymidylate synthase (DHFR-TS) was constructed by destroying the stop codon of Escherichia coli dihydrofolate reductase (DHFR) and joining the coding sequences of the monofunctional enzymes by a five amino acid linker. The protein was designed to mimic features of active site proximity and electrostatics in the protozoan DHFR-TS...
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Hybrid quantum-classical molecular dynamics simulations of a mutant Escherichia coli dihydrofolate reductase enzyme are presented. Although residue 121 is on the exterior of the enzyme, experimental studies have shown that the mutation of Gly-121 to valine reduces the rate of hydride transfer by a factor of 163. The simulations indicate that the decrease in the hydride transfer rate for the G12...
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ژورنال
عنوان ژورنال: Proteins: Structure, Function, and Genetics
سال: 1999
ISSN: 0887-3585,1097-0134
DOI: 10.1002/(sici)1097-0134(19991101)37:2<157::aid-prot2>3.3.co;2-a