Expression and characterization of the nitrile reductase queF from E. coli

Enzyme Microb Technol. 2013 Mar 5;52(3):129-33. doi: 10.1016/j.enzmictec.2012.12.003. Epub 2012 Dec 14.

Abstract

The expression and characterization of a nitrile reductase from Escherichia coli K-12 (EcoNR), a newly discovered enzyme class, is described. This enzyme has a potential application for an alternative nitrile reduction pathway. The enzyme activity towards its natural substrate, preQ(0), was demonstrated and optimal working conditions were found to be at 37°C and at pH 7 with Tris buffer.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacillus subtilis / enzymology
  • Bacillus subtilis / genetics
  • Base Sequence
  • Catalytic Domain
  • Enzyme Stability
  • Escherichia coli K12 / enzymology*
  • Escherichia coli K12 / genetics
  • Escherichia coli Proteins / chemistry
  • Escherichia coli Proteins / genetics
  • Escherichia coli Proteins / metabolism*
  • Genes, Bacterial
  • Hydrogen-Ion Concentration
  • Kinetics
  • Models, Molecular
  • Molecular Sequence Data
  • NADP / metabolism
  • Nuclear Magnetic Resonance, Biomolecular
  • Nucleoside Q / biosynthesis
  • Oxidoreductases / chemistry
  • Oxidoreductases / genetics
  • Oxidoreductases / metabolism*
  • Protein Conformation
  • Pyrimidinones / metabolism
  • Pyrroles / metabolism
  • Recombinant Fusion Proteins / isolation & purification
  • Recombinant Fusion Proteins / metabolism
  • Substrate Specificity
  • Temperature

Substances

  • 7-(aminomethyl)-7-deazaguanine
  • Escherichia coli Proteins
  • Pyrimidinones
  • Pyrroles
  • Recombinant Fusion Proteins
  • NADP
  • Nucleoside Q
  • Oxidoreductases
  • QueF protein, E coli