A comparative study of nitrilases identified by genome mining
Language English Country Switzerland Media print
Document type Comparative Study, Journal Article, Research Support, Non-U.S. Gov't
- MeSH
- Aminohydrolases chemistry genetics metabolism MeSH
- Hydro-Lyases chemistry genetics metabolism MeSH
- Escherichia coli genetics MeSH
- Fungal Proteins chemistry genetics metabolism MeSH
- Genome, Fungal * MeSH
- Genomics MeSH
- Fungi enzymology genetics MeSH
- Recombinant Proteins chemistry genetics metabolism MeSH
- Sequence Analysis, DNA MeSH
- Sequence Homology, Amino Acid MeSH
- Sequence Alignment MeSH
- Substrate Specificity MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Comparative Study MeSH
- Names of Substances
- Aminohydrolases MeSH
- cyanide hydratase MeSH Browser
- Hydro-Lyases MeSH
- Fungal Proteins MeSH
- nitrilase MeSH Browser
- Recombinant Proteins MeSH
Escherichia coli strains expressing different nitrilases transformed nitriles or KCN. Six nitrilases (from Aspergillus niger (2), A. oryzae, Neurospora crassa, Arthroderma benhamiae, and Nectria haematococca) were arylacetonitrilases, two enzymes (from A. niger and Penicillium chrysogenum) were cyanide hydratases and the others (from P. chrysogenum, P. marneffei, Gibberella moniliformis, Meyerozyma guilliermondi, Rhodococcus rhodochrous, and R. ruber) preferred (hetero)aromatic nitriles as substrates. Promising nitrilases for the transformation of industrially important substrates were found: the nitrilase from R. ruber for 3-cyanopyridine, 4-cyanopyridine and bromoxynil, the nitrilases from N. crassa and A. niger for (R,S)-mandelonitrile, and the cyanide hydratase from A. niger for KCN and 2-cyanopyridine.
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