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.
Copyright © 2012 Elsevier Inc. All rights reserved.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Bacillus subtilis / enzymology
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Bacillus subtilis / genetics
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Base Sequence
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Catalytic Domain
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Enzyme Stability
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Escherichia coli K12 / enzymology*
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Escherichia coli K12 / genetics
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Escherichia coli Proteins / chemistry
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Escherichia coli Proteins / genetics
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Escherichia coli Proteins / metabolism*
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Genes, Bacterial
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Hydrogen-Ion Concentration
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Kinetics
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Models, Molecular
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Molecular Sequence Data
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NADP / metabolism
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Nuclear Magnetic Resonance, Biomolecular
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Nucleoside Q / biosynthesis
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Oxidoreductases / chemistry
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Oxidoreductases / genetics
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Oxidoreductases / metabolism*
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Protein Conformation
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Pyrimidinones / metabolism
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Pyrroles / metabolism
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Recombinant Fusion Proteins / isolation & purification
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Recombinant Fusion Proteins / metabolism
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Substrate Specificity
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Temperature
Substances
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7-(aminomethyl)-7-deazaguanine
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Escherichia coli Proteins
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Pyrimidinones
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Pyrroles
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Recombinant Fusion Proteins
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NADP
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Nucleoside Q
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Oxidoreductases
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QueF protein, E coli