A comparative study of nitrilases identified by genome mining
Jazyk angličtina Země Švýcarsko Médium print
Typ dokumentu srovnávací studie, časopisecké články, práce podpořená grantem
- MeSH
- aminohydrolasy chemie genetika metabolismus MeSH
- dehydratasy chemie genetika metabolismus MeSH
- Escherichia coli genetika MeSH
- fungální proteiny chemie genetika metabolismus MeSH
- genom fungální * MeSH
- genomika MeSH
- houby enzymologie genetika MeSH
- rekombinantní proteiny chemie genetika metabolismus MeSH
- sekvenční analýza DNA MeSH
- sekvenční homologie aminokyselin MeSH
- sekvenční seřazení MeSH
- substrátová specifita MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- srovnávací studie MeSH
- Názvy látek
- aminohydrolasy MeSH
- cyanide hydratase MeSH Prohlížeč
- dehydratasy MeSH
- fungální proteiny MeSH
- nitrilase MeSH Prohlížeč
- rekombinantní proteiny 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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