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. 2021 Mar 10;14(8):1781–1804. doi: 10.1002/cssc.202100159

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© 2021 The Authors. ChemSusChem published by Wiley-VCH GmbH

This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.

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Scheme 1 — A selection of synthetically promising (de)carboxylases acting on distinct but diverse substrate groups and showing site of carboxylation: (a) acting on phenolic compounds; (b) acting on heteroaromatic and nonphenolic aromatic compounds; (c) acting on aliphatic compounds. Organic/divalent metal ions cofactors presented in red. Organic cofactors: ATP=adenosine triphosphate; prFMN=prenylated flavin; TPP=thiamine pyrophosphate; NADPH=nicotinamide adenine dinucleotide phosphate (reduced). Enzymes: PhPC=phenylphosphate carboxylase; pHBD=para‐hydroxybenzoic acid decarboxylase; DBHD=dihydroxybenzoate decarboxylase; PAD=phenolic acid decarboxylase; P2CDC=pyrrole‐2‐carboxylate decarboxylase; I3CDC=indole‐3‐carboxylate decarboxylase; HmfF=2,5‐furan dicarboxylic acid decarboxylase; FDC=(fungal) ferulic acid decarboxylases; PEPC=phosphoenolpyruvate carboxylase; pyruvate decarboxylases; KdcA=branched‐chain α‐ketoacid dehydrogenase; ECR=carboxylating enoyl‐thioester reductases; GCC=glycolyl‐CoA carboxylase.