The biotransformation of t-butylacetonitrile and its boron-containing analogue trimethylamine-cyanoborane by Brevibacterium R312.
The ability of the nitrile hydratase/amidase system from Brevibacterium R312 to biotransform tert-butylacetonitrile was studied with a view to their utilisation in the production of novel amino acids from isostructural compounds. Brevibacterium R312 was able to transform nitriles with this structure; however, the wide spectrum amidase from this organism was unable to biotransform the corresponding amide to the carboxylic acid.
Millais
A J
AJ
The Research School of the Biosciences, Biological Laboratory, University of Kent, Canterbury, Kent, UK CT2 7NJ.
Casson
D
D
Lovelady
J
J
Nicholson
A M
AM
Knowles
C J
CJ
D000097:Acetonitriles / Q000378:metabolism*; D001711:Biotransformation; D001896:Boron Compounds / Q000378:metabolism*; D001951:Brevibacterium / Q000378:metabolism*; D002087:Butyrates / Q000378:metabolism; D020148:Butyric Acid; D009570:Nitriles / Q000378:metabolism*
D000097:Acetonitriles; D001896:Boron Compounds; D002087:Butyrates; D009570:Nitriles; C108230:tert-butylacetonitrile; D020148:Butyric Acid; C108231:trimethylamine cyanoborane