Literature summary for 4.1.2.47 extracted from

Van Rantwijk, F.; Stolz, A.
Enzymatic cascade synthesis of (S)-2-hydroxycarboxylic amides and acids Cascade reactions employing a hydroxynitrile lyase, nitrile-converting enzymes and an amidase (2015), J. Mol. Catal. B, 114, 25-30 .

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Application

Application	Comment	Organism
synthesis	synthesis of pure 2-hydroxycarboxylic acids as valuable synthetic building blocks. Development of bienzymatic cascades to convert aldehydes, via hydrocyanation and subsequent hydration or hydrolysis, into the corresponding (S)-2-hydroxycarboxylic amides and acids. The biocatalysts comprise an (S)-specific hydroxynitrile lyase combined with a nonselective nitrile hydratase or nitrilase. The key to success is preventing racemisation of the intermediate (S)-2-hydroxynitrile while adequately protecting the nitrile-converting enzyme, either in a cross-linked enzyme aggregate (CLEA) or in resting cells.Two biocatalyst systems for the synthesis of (S)-mandelic acid are developed: a combined cross-linked enzyme aggregate (combi-CLEA) of an (S)-hydroxynitrile lyase and a nitrilase, as well as a whole-cell Escherichia coli biocatalyst expressing both enzymes. The nitrilase formed large amounts of mandelicamide, which was remedied by including an amidase in the combi-CLEA as well as by using nitrilasevariants obtained by directed mutagenesis in the whole-cell biocatalyst. Excellent results with more than 95% conversion of benzaldehyde into (S)-mandelic acid with near-quantitative enantiomeric purity are obtained with both biocatalyst systems. Directed mutagenesis of the nitrilase provides an amide-selective whole-cell biocatalyst, which produces (S)-mandelic amide in near-stoichiometric yields. (S)-2-hydroxylalkanoic carboxamides are synthesised in the presence of CLEAs of hydroxynitrile lyase and nitrile hydratase	Manihot esculenta

Organism

Organism	UniProt	Comment	Textmining
Manihot esculenta	P52705	-	-

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Release 2023.1 (January 2023)