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The Role of Arginine 28 in Catalysis by Dihydrofolate Reductase from the HyperthermophileThermotoga maritima

Loveridge, Edric Joel, Maglia, Giovanni and Allemann, Rudolf Konrad 2009. The Role of Arginine 28 in Catalysis by Dihydrofolate Reductase from the HyperthermophileThermotoga maritima. ChemBioChem 10 (16) , pp. 2624-2627. 10.1002/cbic.200900465

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Abstract

Dihydrofolate reductase from Thermotoga maritima (TmDHFR) is unusual in that it has an arginine residue within its active site (ringed residue). Here, we address the role of this residue in catalysis. We find no evidence that Arg28 compromises catalysis in TmDHFR by preventing protonation of the substrate or that it acts as an acid to protonate the substrate. Instead, it appears that this residue plays an important role in binding the substrate tightly to ensure its thermal stability.

Item Type: Article
Date Type: Publication
Status: Published
Schools: Chemistry
Cardiff Catalysis Institute (CCI)
Subjects: Q Science > QD Chemistry
Uncontrolled Keywords: dihydrofolate reductase; enzyme catalysis; enzymes; mutagenesis; Thermotoga maritima
Publisher: Wiley-Blackwell
ISSN: 1439-4227
Funders: BBSRC
Last Modified: 05 Jun 2017 02:41
URI: http://orca.cf.ac.uk/id/eprint/17464

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Cited 7 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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