Developing efficient vanillin biosynthesis system by regulating feruloyl-CoA synthetase and enoyl-CoA hydratase enzymes

Chen, Qi Hang; Xie, Dao Tao; Shan, Qiang; Hu, Ching Yuan; Meng, Yong Hong

doi:10.1007/s00253-021-11709-w

Cited by 17 publications

(18 citation statements)

References 40 publications

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“…15,18,19 Referring to the catalytic mechanism of FCS from a chemical perspective, researchers have attempted to break the speed limit factor of aromatic aldehydes biosynthetic progress by regulating the ratio of FCS/ECH and optimizing cofactor supply. 19,48 However, the production of aromatic aldehydes was still limited by the catalytic ability of FCS. 6 This might be because the catalytic pocket of wild-type FCS could not fit phenylpropanoid acids.…”

Section: ■ Resultsmentioning

confidence: 99%

“…FCS, a rate-limiting enzyme in the bioconversion of aromatic aldehydes from phenylpropanoid acids, could ligate the acrylic group of phenylpropanoid acids and CoA to form acyl–CoA by ATP driving. ,, Referring to the catalytic mechanism of FCS from a chemical perspective, researchers have attempted to break the speed limit factor of aromatic aldehydes biosynthetic progress by regulating the ratio of FCS/ECH and optimizing cofactor supply. , However, the production of aromatic aldehydes was still limited by the catalytic ability of FCS . This might be because the catalytic pocket of wild-type FCS could not fit phenylpropanoid acids.…”

Section: Discussionmentioning

confidence: 99%

“…Then the enoyl–CoA hydratase (ECH) converts acyl–CoA into an aldehyde group . FCS is the rate-limiting enzyme throughout the progress of aromatic aldehyde synthesis. − Our previous study elevated vanillin production by enhancing the expression level of FCS . However, significant differences exist in the ability of FCS to catalyze the synthesis of different phenylpropanoid acids. , For example, the substrate affinity of FCS for CIA and 4-methoxycinnamic acid (MA) was significantly lower than that of HA, CA, and FA .…”

Section: Introductionmentioning

confidence: 96%

“…V-1 has higher enzyme activity for phenylpropanoid acids than that from Pseudomonas. However, the catalytic functional domain of the FCS enzyme is unknown, which poses great difficulties for the enzyme’s specific catalytic pocket engineering . Nevertheless, the FCS structure has been constructed by our laboratory through homology modeling .…”

Section: Introductionmentioning

confidence: 99%

“…18−20 Our previous study elevated vanillin production by enhancing the expression level of FCS. 19 However, significant differences exist in the ability of FCS to catalyze the synthesis of different phenylpropanoid acids. 1,21 For example, the substrate affinity of FCS for CIA and 4-methoxycinnamic acid (MA) was significantly lower than that of HA, CA, and FA.…”

Section: ■ Introductionmentioning

confidence: 99%

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Engineering a Feruloyl–Coenzyme A Synthase for Bioconversion of Phenylpropanoid Acids into High-Value Aromatic Aldehydes

Chen

Jiang

Kang³

et al. 2022

J. Agric. Food Chem.

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Aromatic aldehydes find extensive applications in food, perfume, pharmaceutical, and chemical industries. However, a limited natural enzyme selectivity has become the bottleneck of bioconversion of aromatic aldehydes from natural phenylpropanoid acids. Here, based on the original structure of feruloyl–coenzyme A (CoA) synthetase (FCS) from Streptomyces sp. V-1, we engineered five substrate-binding domains to match specific phenylpropanoid acids. FcsCIAE407A/K483L, FcsMAE407R/I481R/K483R, FcsHAE407K/I481K/K483I, FcsCAE407R/I481R/K483T, and FcsFAE407R/I481K/K483R showed 9.96-, 10.58-, 4.25-, 6.49-, and 8.71-fold enhanced catalytic efficiency for degrading CoA thioesters of cinnamic acid, 4-methoxycinnamic acid, 4-hydroxycinnamic acid, caffeic acid, and ferulic acid, respectively. Molecular dynamics simulation illustrated that novel substrate-binding domains formed strong interaction forces with substrates’ methoxy/hydroxyl group and provided hydrophobic/alkaline catalytic surfaces. Five recombinant E. coli with FCS mutants were constructed with the maximum benzaldehyde, p-anisaldehyde, p-hydroxybenzaldehyde, protocatechualdehyde, and vanillin productivity of 6.2 ± 0.3, 5.1 ± 0.23, 4.1 ± 0.25, 7.1 ± 0.3, and 8.7 ± 0.2 mM/h, respectively. Hence, our study provided novel and efficient enzymes for the bioconversion of phenylpropanoid acids into aromatic aldehydes.

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