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Discovery of Novel Tyrosine Ammonia Lyases for the Enzymatic Synthesis of p-Coumaric Acid
- p-Coumaric acid (p-CA) is a key precursor for the biosynthesis of flavonoids. Tyrosine ammonia lyases (TALs) specifically catalyze the synthesis of p-CA from l-tyrosine, which is a convenient enzymatic pathway. To explore novel and highly active TALs, a phylogenetic tree-building approach was conducted including 875 putative TALs and 46 putative phenylalanine/tyrosine ammonia lyases (PTALs). Among them, 5 TALs and 3 PTALs were successfully characterized and found to exhibit the proposed enzymatic activity. The TAL from Chryseobacterium luteum sp. nov (TALclu) has the highest affinity (Km=0.019 mm) and conversion efficiency (kcat/Km=1631 s−1 ⋅ mm−1) towards l-tyrosine. The reaction conditions for two purified enzymes and their E. coli recombinant cells were optimized and p-CA yields of 2.03 g/L after 8 hours by TALclu and 2.35 g/L after 24 h by TAL from Rivularia sp. PCC 7116 (TALrpc) in whole cells were achieved. These TALs are thus candidates for the construction of whole-cell systems to produce the flavonoid precursor p-CA.
Author: | Yannik Brack, Chenghai Sun, Dong Yi, Uwe T. BornscheuerORCiD |
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URN: | urn:nbn:de:gbv:9-opus-106808 |
DOI: | https://doi.org/10.1002/cbic.202200062 |
ISSN: | 1439-7633 |
Parent Title (English): | ChemBioChem |
Publisher: | Wiley |
Place of publication: | Hoboken, NJ |
Document Type: | Article |
Language: | English |
Date of Publication (online): | 2022/03/30 |
Date of first Publication: | 2022/05/18 |
Release Date: | 2024/02/21 |
Tag: | biocatalysis; flavonoids; p-coumaric acid; phenylalanine ammonia lyase; tyrosine ammonia lyase |
Volume: | 23 |
Issue: | 10 |
Article Number: | e202200062 |
Page Number: | 7 |
Faculties: | Mathematisch-Naturwissenschaftliche Fakultät / Institut für Biochemie |
Collections: | weitere DFG-förderfähige Artikel |
Licence (German): | Creative Commons - Namensnennung-Nicht kommerziell-Keine Bearbeitung 4.0 International |