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Titolo:
Evidence for an essential arginine in the flavoprotein nitroalkane oxidase
Autore:
Gadda, G; Banerjee, A; Fleming, GS; Fitzpatrick, PF;
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 Texas A&M Univ, Dept Chem, College Stn, TX 77843 USA Texas A&M Univ College Stn TX USA 77843 t Chem, College Stn, TX 77843 USA
Titolo Testata:
JOURNAL OF ENZYME INHIBITION
fascicolo: 2, volume: 16, anno: 2001,
pagine: 157 - 163
SICI:
8755-5093(2001)16:2<157:EFAEAI>2.0.ZU;2-G
Fonte:
ISI
Lingua:
ENG
Soggetto:
FAD-CONTAINING FORM; AMINO-ACID OXIDASE; FUSARIUM-OXYSPORUM; ACTIVE-SITE; SUBSTRATE-SPECIFICITY; CRYSTAL-STRUCTURE; IDENTIFICATION; MECHANISM; ENZYME; RESOLUTION;
Keywords:
nitroalkanes; flavoprotein; chemical modification; active site; arginine; phenylglyoxal; flavoprotein nitroalkane oxidase;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
24
Recensione:
Indirizzi per estratti:
Indirizzo: Fitzpatrick, PF Texas A&M Univ, Dept Biochem & Biophys, College Stn, TX 77843 USA Texas A&M Univ College Stn TX USA 77843 Stn, TX 77843 USA
Citazione:
G. Gadda et al., "Evidence for an essential arginine in the flavoprotein nitroalkane oxidase", J ENZ INHIB, 16(2), 2001, pp. 157-163

Abstract

The flavoprotein nitroalkane oxidase from the fungus Fusarium oxysporum catalyzes the oxidative denitrification of primary or secondary nitroalkanes to yield the respective aldehydes or ketones, hydrogen peroxide and nitrite. The enzyme is inactivated in a time-dependent fashion upon treatment withthe arginine-directed reagents phenylglyoxal, 2,3-butanedione, and cyclohexanedione. The inactivation shows first order kinetics with all reagents. Valerate, a competitive inhibitor of the enzyme, fully protects the enzyme from inactivation, indicating that modification is active site directed. Themost rapid inactivation is seen with phenylglyoxal, with a k(inact) of 14.3 +/- 1.1 M-1 min(-1) in phosphate buffer at pH 7.3 and 30 degreesC. The lack of increase in the enzymatic activity of the phenylglyoxal-inactivated enzyme after removing the unreacted reagent by gel filtration is consistent with inactivation being due to covalent modification of the enzyme. A possible role for an active site arginine in substrate binding is discussed.

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Documento generato il 01/04/20 alle ore 10:24:49