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Pathway discovery and engineering for cleavage of a β-1 lignin-derived biaryl compound.
- Source :
-
Metabolic engineering [Metab Eng] 2021 May; Vol. 65, pp. 1-10. Date of Electronic Publication: 2021 Feb 23. - Publication Year :
- 2021
-
Abstract
- Lignin biosynthesis typically results in a polymer with several inter-monomer bond linkages, and the heterogeneity of linkages presents a challenge for depolymerization processes. While several enzyme classes have been shown to cleave common dimer linkages in lignin, the pathway of bacterial β-1 spirodienone linkage cleavage has not been elucidated. Here, we identified a pathway for cleavage of 1,2-diguaiacylpropane-1,3-diol (DGPD), a β-1 linked biaryl representative of a ring-opened spirodienone linkage, in Novosphingobium aromaticivorans DSM12444. In vitro assays using cell lysates demonstrated that RS14230 (LsdE) converts DGPD to a lignostilbene intermediate, which the carotenoid oxygenase, LsdA, then converts to vanillin. A Pseudomonas putida KT2440 strain engineered with lsdEA expression catabolizes erythro-DGPD, but not threo-DGPD. We further engineered P. putida to convert DGPD to a product, cis,cis-muconic acid. Overall, this work demonstrates the potential to identify new enzymatic reactions in N. aromaticivorans and expands the biological funnel of P. putida for microbial lignin valorization.<br /> (Copyright © 2021 International Metabolic Engineering Society. All rights reserved.)
- Subjects :
- Lignin
Pseudomonas putida genetics
Sphingomonadaceae
Subjects
Details
- Language :
- English
- ISSN :
- 1096-7184
- Volume :
- 65
- Database :
- MEDLINE
- Journal :
- Metabolic engineering
- Publication Type :
- Academic Journal
- Accession number :
- 33636323
- Full Text :
- https://doi.org/10.1016/j.ymben.2021.02.003