Nitrile biotransformations for the synthesis of enantiomerically enriched Baylis-Hillman adducts.
Catalysed by the nitrile hydratase/amidase-containing Rhodococcus sp. AJ270 cells, a number of beta-aryl- and beta-alkyl- beta-hydroxy-alpha-methylenepropiononitriles (the Baylis-Hillman nitriles) 1 underwent hydrolysis under mild conditions to produce the corresponding enantiomerically enriched Baylis-Hillman amides 2 and acids 3. The enantioselectivity of the biotransformations was strongly determined by the steric effect of the substituents at the beta-position of the substrates. The protection of the free hydroxy of beta-phenyl-beta-hydroxy-alpha-methylenepropiononitrile 1a by methylation led to the enhancement of enantiocontrol of the biohydrolysis.
Wang
Mei-Xiang
MX
Laboratory of Chemical Biology, Centre for Molecular Science, Institute of Chemistry, Chinese Academy of Sciences, Beijing 100080, China. mxwang@infoc3.icas.ac.cn
Wu
Yan
Y
D000577:Amides / Q000138:chemical synthesis* / Q000378:metabolism; D000581:Amidohydrolases / Q000737:chemistry / Q000378:metabolism; D001711:Biotransformation; D002264:Carboxylic Acids / Q000138:chemical synthesis* / Q000378:metabolism; D002384:Catalysis; D006836:Hydro-Lyases / Q000737:chemistry / Q000378:metabolism; D006868:Hydrolysis; D008745:Methylation; D009570:Nitriles / Q000737:chemistry* / Q000378:metabolism; D012240:Rhodococcus / Q000201:enzymology; D013237:Stereoisomerism; D013379:Substrate Specificity
D000577:Amides; D002264:Carboxylic Acids; D009570:Nitriles; D000581:Amidohydrolases; D006836:Hydro-Lyases; C048831:nitrile hydratase