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Upstream product

• 65984-59-0 3-(4-bromophenyl)-3-hydroxypropanenitrile 

Relevant academic research and scientific papers

Enzymatic nitrile hydrolysis catalyzed by nitrilase ZmNIT2 from maize. An unprecedented β-hydroxy functionality enhanced amide formation

To explore the synthetic potential of nitrilase ZmNIT2 from maize, the substrate specificity of this nitrilase was studied with a diverse collection of nitriles. The nitrilase ZmNIT2 showed high activity for all the tested nitriles except benzonitrile, producing both acids and amides. For the hydrolysis of aliphatic, aromatic nitriles, phenylacetonitrile derivatives and dinitriles, carboxylic acids were the major products. Unexpectedly, amides were found to be the major products in nitrilase ZmNIT2-catalyzed hydrolysis of β-hydroxy nitriles. The hydrogen bonding between the hydroxyl group and nitrogen in the enzyme-substrate complex intermediates that disfavors the loss of ammonia and formation of acyl-enzyme intermediate, which was further hydrolyzed to acid, was proposed to be responsible for the unprecedented β-hydroxy functionality assisted high yield of amide formation.

Exploring the synthetic applicability of a cyanobacterium nitrilase as catalyst for nitrile hydrolysis

The substrate specificity and synthetic applicability of the nitrilase from cyanobacterium Synechocystis sp. strain PCC 6803 have been examined. This nitrilase catalyzed the hydrolysis of both aromatic and aliphatic nitriles to the corresponding acids in high yields. Furthermore, the stereoselective hydrolysis of phenyl-substituted β-hydroxy nitriles to (S)-enriched β-hydroxy carboxylic acids and selective hydrolysis of α,ω- dinitriles with five or less methylene groups to ω-cyano carboxylic acids have been achieved. This suggested that nitrilase from Synechocystis sp. PCC 6803 could be a useful enzyme catalyst for the "green" nitrile hydrolysis. Wiley-VCH Verlag GmbH & Co. KGaA, 2006.