Evolution Conserves the Network of Coupled Residues in Dihydrofolate Reductase.

ABSTRACT: Understanding protein motions and their role in enzymatic reactions is an important and timely topic in enzymology. Protein motions that are involved in the chemical step of catalysis are particularly intriguing but difficult to identify. A global network of coupled residues in Escherichia coli dihydrofolate reductase (E. coli DHFR), which assists in catalyzing the chemical step, has previously been demonstrated through quantum mechanical/molecular mechanical and molecular dynamics simulations as well as bioinformatic analyses. A few specific residues (M42, G121, F125, and I14) were shown to function synergistically with measurements of single-turnover rates and the temperature dependence of intrinsic kinetic isotope effects (KIEs_int) of site-directed mutants. This

SUBMITTER: Li J 

PROVIDER: S-EPMC7296831 | biostudies-literature | 2019 Sep

REPOSITORIES: biostudies-literature