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Titolo:
Differential effects of isomeric incorporation of fluorophenylalanines into PvuII endonuclease
Autore:
Dominguez, MA; Thornton, KC; Melendez, MG; Dupureur, CM;
Indirizzi:
Texas A&M Univ, Dept Biochem & Biophys, College Stn, TX 77843 USA Texas A&M Univ College Stn TX USA 77843 iophys, College Stn, TX 77843 USA
Titolo Testata:
PROTEINS-STRUCTURE FUNCTION AND GENETICS
fascicolo: 1, volume: 45, anno: 2001,
pagine: 55 - 61
SICI:
0887-3585(20011001)45:1<55:DEOIIO>2.0.ZU;2-3
Fonte:
ISI
Lingua:
ENG
Soggetto:
NUCLEAR-MAGNETIC-RESONANCE; D-LACTATE DEHYDROGENASE; RESTRICTION-ENDONUCLEASE; ESCHERICHIA-COLI; F-19 NMR; CONFORMATIONAL-CHANGES; PROTEIN-STRUCTURE; DNA-BINDING; AMINO-ACID; RECOGNITION;
Keywords:
fluorine; F-19-NMR spectroscopy; phenylalanine; isomer; restriction endonuclease;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
37
Recensione:
Indirizzi per estratti:
Indirizzo: Dupureur, CM Texas A&M Univ, Dept Biochem & Biophys, College Stn, TX 77843USA Texas A&M Univ College Stn TX USA 77843 ge Stn, TX 77843 USA
Citazione:
M.A. Dominguez et al., "Differential effects of isomeric incorporation of fluorophenylalanines into PvuII endonuclease", PROTEINS, 45(1), 2001, pp. 55-61

Abstract

Incorporation of fluorine into proteins has long served as a means of probing structure and function, yet there are few studies that examine the impact of fluorine substitution, particularly at locations distant from the active sites of enzymes. The flexibility of isomeric fluorine incorporation atPhe is used to explore subtle substitution effects on enzyme activity and conformation. The unnatural amino acids o-, m-, and p-fluorophenylalanines were incorporated biosynthetically into the representative PvuII restriction endonuclease. Interestingly, m-fluoro-Phe-PvuII endonuclease exhibits very similar conformational stability to that of the native enzyme, but it exhibits a reproducible, 2-fold higher average specific activity. Given the level of incorporation and the distribution of species, the species of modified enzyme responsible for this increase in specific activity is most likelyeven faster. Further, moving the fluorine atom from the meta- to the para-position of Phe results in a 4-fold decrease in specific activity and a decrease in conformational stability of 1.5 kcal/mol. Since none of the Phe residues in PvuII endonuclease lies near the DNA recognition or catalytic sites, this differential behavior alludes to the impact of subtle changes in enzyme conformation on endonuclease activity and suggests novel ways to influence catalytic behavior. (C) 2001 Wiley-Liss, Inc.

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Documento generato il 13/07/20 alle ore 07:14:06