Substrate specificity of a nitroalkane-oxidizing enzyme

Giovanni Gadda, Paul F. Fitzpatrick

Research output: Contribution to journalArticlepeer-review

36 Scopus citations

Abstract

The flavoprotein nitroalkane oxidase from Fusarium oxysporum catalyzes the oxidation of nitroalkanes to aldehydes with production of hydrogen peroxide and nitrite. The substrate specificity of the FAD-containing enzyme has been determined as a probe of the active site structure. Nitroalkane oxidase is active on primary and secondary nitroalkanes, with a marked preference for unbranched primary nitroalkanes. The V/K values for primary nitroalkanes increase with increasing length of the alkyl chain, reaching a maximum with 1-nitrobutane, suggesting a hydrophobic binding site sufficient to accommodate a four carbon chain. Each methylene group of the substrate contributes ~2.6 kcal mol-1 in binding energy. The V/K values for substrates containing a hydroxyl group are two orders of magnitude smaller than those of the corresponding nitroalkanes, also consistent with a hydrophobic binding site. 3-Nitro-1-propionate is a competitive inhibitor with a K(is) value of 3.1 ± 0.2 mM.

Original languageEnglish (US)
Pages (from-to)309-313
Number of pages5
JournalArchives of Biochemistry and Biophysics
Volume363
Issue number2
DOIs
StatePublished - Mar 15 1999

Keywords

  • Active site
  • Flavoprotein
  • Oxidase
  • Steady-state kinetics
  • Substrate specificity

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology

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