ArticleWorld journal of microbiology & biotechnology2018
Conversion of aliphatic nitriles by the arylacetonitrilase from Pseudomonas fluorescens EBC191.
Article in World journal of microbiology & biotechnology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed, 21 citations in OpenAlex.
- Isolation and Characterization of a Nitrilase-Producing Geotrichum Strain and Optimization of the Fermentation Conditions.Current microbiology · 2025Article
- Arylacetonitrilases: Potential Biocatalysts for Green Chemistry.Applied biochemistry and biotechnology · 2024Review
- Geometric Remodeling of Nitrilase Active Pocket Based on ALF-Scanning Strategy To Enhance Aromatic Nitrile Substrate Preference and Catalytic Efficiency.Applied and environmental microbiology · 2023Article
- Functional metagenomics uncovers nitrile-hydrolysing enzymes in a coal metagenome.Frontiers in molecular biosciences · 2023Article
- Synthesis of (R)-mandelic acid and (R)-mandelic acid amide by recombinant E. coli strains expressing a (R)-specific oxynitrilase and an arylacetonitrilase.Biotechnology letters · 2021Article
- Purification and Characterization of NitFrontiers in bioengineering and biotechnology · 2021Article
- Plant Nitrilase Homologues in Fungi: Phylogenetic and Functional Analysis with Focus on Nitrilases inMolecules (Basel, Switzerland) · 2020Article
- Rolling circle amplification of synthetic DNA accelerates biocatalytic determination of enzyme activity relative to conventional methods.Scientific reports · 2020Article
- Genetic and Functional Diversity of Nitrilases in Agaricomycotina.International journal of molecular sciences · 2019Article
- Comparative Analysis of the Conversion of Mandelonitrile and 2-Phenylpropionitrile by a Large Set of Variants Generated from a Nitrilase Originating fromMolecules (Basel, Switzerland) · 2019Review
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5 authors at 1 institution in 1 country.
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Abstract
The conversion of aliphatic nitriles by the arylacetonitrilase from Pseudomonas fluorescens EBC191 (NitA) was analyzed. The nitrilase hydrolysed a wide range of aliphatic mono- and dinitriles and showed a preference for unsaturated aliphatic substrates containing 5-6 carbon atoms. In addition, increased reaction rates were also found for aliphatic nitriles carrying electron withdrawing substituents (e.g. chloro- or hydroxy-groups) close to the nitrile group. Aliphatic dinitriles were attacked only at one of the nitrile groups and with most of the tested dinitriles the monocarboxylates were detected as major products. In contrast, fumarodinitrile was converted to the monocarboxylate and the monocarboxamide in a ratio of about 65:35. Significantly different relative amounts of the two products were observed with two nitrilase variants with altered reaction specifities. NitA converted some aliphatic substrates with higher rates than 2-phenylpropionitrile, which is one of the standard substrates for arylacetonitrilases. This indicated that the traditional classification of nitrilases as "arylacetonitrilases", "aromatic" or "aliphatic" nitrilases might require some corrections. This was also suggested by the construction of some variants of NitA which were modified in an amino acid residue which was previously suggested to be essential for the conversion of aliphatic substrates by a homologous nitrilase.
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