Luk, Louis Yu Pan, Loveridge, Edric Joel and Allemann, Rudolf Konrad 2014. Different dynamical effects in mesophilic and hyperthermophilic dihydrofolate reductases. Journal of the American Chemical Society 136 (19) , pp. 6862-6865. 10.1021/ja502673h |
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Abstract
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 (15N, 13C, 2H). 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.
Item Type: | Article |
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Date Type: | Publication |
Status: | Published |
Schools: | Chemistry |
Subjects: | Q Science > QD Chemistry |
Publisher: | American Chemical Society |
ISSN: | 0002-7863 |
Funders: | BBSRC |
Date of First Compliant Deposit: | 30 March 2016 |
Date of Acceptance: | 16 March 2014 |
Last Modified: | 05 Jun 2017 04:30 |
URI: | http://orca.cf.ac.uk/id/eprint/60381 |
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Cited 4 times in Google Scholar. View in Google Scholar
Cited 12 times in Scopus. View in Scopus. Powered By Scopus® Data
Cited 5 times in Web of Science. View in Web of Science.
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