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Hydroxynitrile lyases in stereoselective catalysis

✍ Scribed by Franz Effenberger; Siegfried Förster; Harald Wajant


Book ID
104361529
Publisher
Elsevier Science
Year
2000
Tongue
English
Weight
229 KB
Volume
11
Category
Article
ISSN
0958-1669

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✦ Synopsis


(R)- as well as (S)-cyanohydrins are now easily available as a result of the excellent accessibility, the relatively high stability and the easy handling of hydroxynitrile lyases (HNLs). The optimization of reaction conditions (solvent, temperature, and using site-directed mutagenesis, etc.) has enabled HNL-catalyzed preparations of optically active cyanohydrins on a technical scale. The enantioselectivity of chiral metal-complex-catalyzed additions of trimethylsilyl cyanide to aldehydes has been improved, but is, by far, not yet competitive with the HNL-catalyzed reactions.


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Hydroxynitrile lyase from Hevea brasilie
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S)-Hydroxynitrile lyase (Hnl) from the tropical rubber tree Hevea brasiliensis is a 29 kDa single chain protein that catalyses the breakdown or formation of a C-C bond by reversible addition of hydrocyanic acid to aldehydes or ketones. The primary sequence of Hnl has no significant homology to known

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## Abstract __The influence of Trp128‐substituted mutants of the hydroxynitrile lyase from__ Manihot esculenta __(MeHNL) on the stereoselectivity of MeHNL‐catalyzed HCN additions to aldehydes with stereogenic centers, which yield the corresponding cyanohydrins, is described. In__ rac__‐2‐phenylprop