2.1. 4 Enzymatic Carboxylation and Decarboxylation
Buch
Herausgeber: Faber, K.; Fessner, W.-D.; Turner, N. J.
Titel: Biocatalysis Organic Synthesis 2
Print ISBN: 9783131741615; Online ISBN: 9783131975317; Buch-DOI: 10.1055/b-003-125813
1st edition © 2015. Thieme. All rights reserved.
Georg Thieme Verlag KG, Stuttgart
Fachgebiete: Organische Chemie
Science of Synthesis Reference Libraries
Übergeordnete Publikation
Titel: Science of Synthesis
DOI: 10.1055/b-00000101
Typ: Mehrbändiges Werk
Abstract
![](https://www.thieme-connect.de/media/10.1055-b-003-125813/thumbnails/a_210ccd.jpg)
Carboxylation reactions utilizing whole cells or purified carboxylase/decarboxylase enzymes enable the regioselective formation of new C—C bonds under more benign conditions than are typically used in nonenzymatic transformations such as the Kolbe–Schmitt reaction. A wide variety of substrates have been used in enzymatic carboxylation reactions including phenols, styrenes, pyrroles, and indoles.
Enzymatic decarboxylation can be used to transform simple achiral carboxylic acid substrates into more valuable homochiral building blocks through stereoselective C—H or C—C bond formation. For example, arylmalonate decarboxylases catalyze the enantioselective decarboxylative protonation of α-aryl- and α-alkenylmalonic acids under mild conditions and with excellent enantioselectivity. In addition, thiamine diphosphate dependent decarboxylases catalyze C—C bond formation with a broad range of α-keto acid and aldehyde substrates to produce homochiral α-hydroxy ketones.
Schlüsselwörter
carboxylation - Kolbe–Schmitt reaction - regioselectivity - whole-cell reaction - C—C bond formation - enantioselectivity - decarboxylation - arylmalonate decarboxylase - malonic acids - stereoselectivity - enantioselective decarboxylative protonation- 4 Kirimura K, Gunji H, Wakayama R, Hattori T, Ishii Y. Biochem. Biophys. Res. Commun. 2010; 394: 279
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