Journal
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 136, Issue 19, Pages 6862-6865Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ja502673h
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Funding
- UK Biotechnology and Biological Sciences Research Council (BBSRC) [BB/J005266/1]
- BBSRC [BB/J005266/1, BB/J005398/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/J005398/1, BB/J005266/1] Funding Source: researchfish
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The role of protein dynamics in the reaction catalyzed by dihydrofolate reductase from the hyperthermophile Thermotoga maritima (TmDHFR) has been examined by enzyme isotope substitution (N-15, C-13, H-2). In contrast to all other enzyme reactions investigated previously, including DHFR from Escherichia coli (EcDHFR), for which isotopic substitution led to decreased reactivity, the rate constant for the hydride transfer step is not affected by isotopic substitution of TmDHFR. TmDHFR therefore appears to lack the coupling of protein motions to the reaction coordinate that have been identified for EcDHFR catalysis. Clearly, dynamical coupling is not a universal phenomenon that affects the efficiency of enzyme catalysis.
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