Efficient production of salvianic acid A from l-dihydroxyphenylalanine through a tri-enzyme cascade

Yang, Jiahui; Wei, Wanqing; Gao, Changzheng; Song, Wei; Gao, Cong; Chen, Xiulai; Liu, Jia; Guo, Liang; Li, Liming; Wu, Jing

doi:10.1186/s40643-023-00649-0

Cited by 2 publications

(1 citation statement)

References 38 publications

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“…A Verify 3D analysis of CsLCYB and CsLCYE revealed that 83.87% and 86.18% of the amino acid residues scored above 0.2 in the 3D-1D profile, respectively (Figure S4), meeting the criterion of at least 80%. A Ramachandran plot analysis indicated that high percentages (93.5% and 91.6% for CsLCYB and CsLCYE, respectively) of residues were located within favored regions (Figure S4), thus confirming the reliability of the models [27]. In addition, the conserved secondary structure consisting of a β chain-α helix-β chain was apparent in both CsLCYB and CsLCYE (Figure 2 and Figure S5), which is consistent with other previously reported predicted models of LCYs [28,29].…”

Section: Gene Cloning and Sequence Analysis Of Cslcyb And Cslcyementioning

confidence: 60%

Functional Characterization of Lycopene β- and ε-Cyclases from a Lutein-Enriched Green Microalga Chlorella sorokiniana FZU60

Fang

Liu

et al. 2023

Marine Drugs

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Lutein is a high-value carotenoid with many human health benefits. Lycopene β- and ε-cyclases (LCYB and LCYE, respectively) catalyze the cyclization of lycopene into distinct downstream branches, one of which is the lutein biosynthesis pathway, via α-carotene. Hence, LCYB and LCYE are key enzymes in lutein biosynthesis. In this study, the coding genes of two lycopene cyclases (CsLCYB and CsLCYE) of a lutein-enriched marine green microalga, Chlorella sorokiniana FZU60, were isolated and identified. A sequence analysis and computational modeling of CsLCYB and CsLCYE were performed using bioinformatics to identify the key structural domains. Further, a phylogenetic analysis revealed that CsLCYB and CsLCYE were homogeneous to the proteins of other green microalgae. Subcellular localization tests in Nicotiana benthamiana showed that CsLCYB and CsLCYE localized in chloroplasts. A pigment complementation assay in Escherichia coli revealed that CsLCYB could efficiently β-cyclize both ends of lycopene to produce β-carotene. On the other hand, CsLCYE possessed a strong ε-monocyclase activity for the production of δ-carotene and a weak ε-bicyclic activity for the production of ε-carotene. In addition, CsLCYE was able to catalyze lycopene into β-monocyclic γ-carotene and ultimately produced α-carotene with a β-ring and an ε-ring via γ-carotene or δ-carotene. Moreover, the co-expression of CsLCYB and CsLCYE in E. coli revealed that α-carotene was a major product, which might lead to the production of a high level of lutein in C. sorokiniana FZU60. The findings provide a theoretical foundation for performing metabolic engineering to improve lutein biosynthesis and accumulation in C. sorokiniana FZU60.

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Section: Gene Cloning and Sequence Analysis Of Cslcyb And Cslcyementioning

confidence: 60%

Functional Characterization of Lycopene β- and ε-Cyclases from a Lutein-Enriched Green Microalga Chlorella sorokiniana FZU60

Fang

Liu

et al. 2023

Marine Drugs

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Development of a Thermodynamically Favorable Multi‐enzyme Cascade Reaction for Efficient Sustainable Production of ω‐Amino Fatty Acids and α,ω‐Diamines

Li,

Shi,

et al. 2024

ChemSusChem

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Aliphatic ω‐amino fatty acids (ω‐AFAs) and α,ω‐diamines (α,ω‐DMs) are essential monomers for the production of nylons. Development of a sustainable biosynthesis route for ω‐AFAs and α,ω‐DMs is crucial in addressing the challenges posed by climate change. Herein, we constructed an unprecedented thermodynamically favorable multi‐enzyme cascade (TherFavMEC) for the efficient sustainable biosynthesis of ω‐AFAs and α,ω‐DMs from cheap α,ω‐dicarboxylic acids (α,ω‐DAs). This TherFavMEC was developed by incorporating bioretrosynthesis analysis tools, reaction Gibbs free energy calculations, thermodynamic equilibrium shift strategies and cofactor (NADPH&ATP) regeneration systems. The molar yield of 6‐aminohexanoic acid (6‐ACA) from adipic acid (AA) was 92.3%, while the molar yield from 6‐ACA to 1,6‐hexanediamine (1,6‐HMD) was 96.1%, which were significantly higher than those of previously reported routes. Furthermore, the biosynthesis of ω‐AFAs and α,ω‐DMs from 20.0 mM α,ω‐DAs (C6‐C9) was also performed, giving 11.2 mM 1,6‐HMD (56.0% yield), 14.8 mM 1,7‐heptanediamine (74.0% yield), 17.4 mM 1,8‐octanediamine (87.0% yield), and 19.7 mM 1,9‐nonanediamine (98.5% yield), respectively. The titers of 1,9‐nonanediamine, 1,8‐octanediamine, 1,7‐heptanediamine and 1,6‐HMD were improved by 328‐fold, 1740‐fold, 87‐fold and 3.8‐fold compared to previous work. Therefore, this work holds great potential for the bioproduction of ω‐AFAs and α,ω‐DMs.

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Efficient production of salvianic acid A from l-dihydroxyphenylalanine through a tri-enzyme cascade

Cited by 2 publications

References 38 publications

Functional Characterization of Lycopene β- and ε-Cyclases from a Lutein-Enriched Green Microalga Chlorella sorokiniana FZU60

Functional Characterization of Lycopene β- and ε-Cyclases from a Lutein-Enriched Green Microalga Chlorella sorokiniana FZU60

Development of a Thermodynamically Favorable Multi‐enzyme Cascade Reaction for Efficient Sustainable Production of ω‐Amino Fatty Acids and α,ω‐Diamines

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