Different dynamical effects in mesophilic and hyperthermophilic dihydrofolate reductases

Luk, Louis Y. P. ORCID: https://orcid.org/0000-0002-7864-6261, Loveridge, E. Joel and Allemann, Rudolf K. ORCID: https://orcid.org/0000-0002-1323-8830 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
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:	10 May 2023 07:59
URI:	https://orca.cardiff.ac.uk/id/eprint/60381

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