| Autor: |
Aleku GA; Manchester Institute of Biotechnology School of Chemistry University of Manchester 131 Princess Street Manchester M1 7DN United Kingdom., Prause C; Department of Chemistry University of Graz Heinrichstrasse 28 8010 Graz Austria)., Bradshaw-Allen RT; Manchester Institute of Biotechnology School of Chemistry University of Manchester 131 Princess Street Manchester M1 7DN United Kingdom., Plasch K; Department of Chemistry University of Graz Heinrichstrasse 28 8010 Graz Austria)., Glueck SM; Austrian Centre of Industrial Biotechnology (ACIB) 8010 Graz Austria) c/o.; Department of Chemistry University of Graz Heinrichstrasse 28 8010 Graz Austria)., Bailey SS; Manchester Institute of Biotechnology School of Chemistry University of Manchester 131 Princess Street Manchester M1 7DN United Kingdom., Payne KAP; Manchester Institute of Biotechnology School of Chemistry University of Manchester 131 Princess Street Manchester M1 7DN United Kingdom., Parker DA; Innovation/Biodomain Shell International Exploration and Production Inc. Westhollow Technology Center Houston USA., Faber K; Department of Chemistry University of Graz Heinrichstrasse 28 8010 Graz Austria)., Leys D; Manchester Institute of Biotechnology School of Chemistry University of Manchester 131 Princess Street Manchester M1 7DN United Kingdom. |
| Jazyk: |
angličtina |
| Zdroj: |
ChemCatChem [ChemCatChem] 2018 Sep 07; Vol. 10 (17), pp. 3736-3745. Date of Electronic Publication: 2018 Jul 17. |
| DOI: |
10.1002/cctc.201800643 |
| Abstrakt: |
Fungal ferulic acid decarboxylases (FDCs) belong to the UbiD-family of enzymes and catalyse the reversible (de)carboxylation of cinnamic acid derivatives through the use of a prenylated flavin cofactor. The latter is synthesised by the flavin prenyltransferase UbiX. Herein, we demonstrate the applicability of FDC/UbiX expressing cells for both isolated enzyme and whole-cell biocatalysis. FDCs exhibit high activity with total turnover numbers (TTN) of up to 55000 and turnover frequency (TOF) of up to 370 min -1 . Co-solvent compatibility studies revealed FDC's tolerance to some organic solvents up 20 % v/v. Using the in-vitro (de)carboxylase activity of holo-FDC as well as whole-cell biocatalysts, we performed a substrate profiling study of three FDCs, providing insights into structural determinants of activity. FDCs display broad substrate tolerance towards a wide range of acrylic acid derivatives bearing (hetero)cyclic or olefinic substituents at C3 affording conversions of up to >99 %. The synthetic utility of FDCs was demonstrated by a preparative-scale decarboxylation. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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