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学者姓名：苏冰梅
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Abstract ：
Baeyer-Villiger monooxygenases (BVMOs) can catalyze the asymmetric sulfoxidation to form pharmaceutical prazoles in environmentally friendly approach. In this work, the thermostable BVMO named PockeMO had high sulfoxidation activity towards rabeprazole sulfide to form (R)-rabeprazole but demonstrated significant overoxidation activity to form undesired sulfone by-product. To address this issue, the enzyme was engineered based on the computer assisted comparison for the substrate binding conformations. A mutant S482Y/L532Q (MU2) was obtained with much alleviated overoxidation activity and enhanced sulfoxidation activity towards rabeprazole sulfide. The catalytic efficiency for (R)-rabeprazole oxidation decreased 35 folds and increased 40 folds for the sulfoxidation of lansoprazole sulfide. The structural mechanism for the selectivity improvement was illuminated to find a selectivity decision pocket that was conservatively present in BVMOs composed of 4 loops. In upscaled reaction system, the substrate loading for MU2 increased from 40 mM to 100 mM for the synthesis of enantiopure (R)-rabeprazole. The sulfone content decreased from 16.6 % to 1.2 % compared to PockeMO. Lansoprazole sulfide could also be fully converted into enantiopure (R)-lansoprazole at 50 mM in 4 h by MU2 while PockeMO almost did not have activity. This work indicated the synthetic applicability of MU2 for active pharmaceutical (R)-prazoles.
Keyword ：
Baeyer-Villiger monooxygenase Baeyer-Villiger monooxygenase ( R )-prazole ( R )-prazole Substrate selectivity Substrate selectivity
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| GB/T 7714 | Xu, Xinqi , Xu, Fahui , Chen, Jingjing et al. Engineering of a (R)-selective Baeyer-Villiger monooxygenase to minimize overoxidation activity for asymmetric synthesis of active pharmaceutical prazoles [J]. | INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES , 2025 , 296 . |
| MLA | Xu, Xinqi et al. "Engineering of a (R)-selective Baeyer-Villiger monooxygenase to minimize overoxidation activity for asymmetric synthesis of active pharmaceutical prazoles" . | INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES 296 (2025) . |
| APA | Xu, Xinqi , Xu, Fahui , Chen, Jingjing , Wang, Shumin , Wang, Xialian , Su, Bingmei et al. Engineering of a (R)-selective Baeyer-Villiger monooxygenase to minimize overoxidation activity for asymmetric synthesis of active pharmaceutical prazoles . | INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES , 2025 , 296 . |
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4-Acetoxy-azacyclobutanone (4AA) is a highly demanded chemical compound used in the production of Penem and Carbapenem antibiotics. However, its synthesis is constrained by the preparation of methyl (2S,3R)-2-[(benzoylamino)methyl]-3-hydroxybutanoate [(2S,3R)-BHME]. In light of stringent environmental regulations, there is an urgent need to develop an effective enzymatic method using 2-benzoylaminomethyl-3-oxy-butyrate methyl ester (BOME) as the substrate. This study mined a carbonyl reductase AxSDR from Algoriella xinjiangensis, which asymmetrically reduces BOME to (2S,3R)-BHME using isopropanol (IPA) as a cosubstrate. The mechanisms underlying the high stereoselectivity, substrate selectivity, and limited activity of AxSDR toward BOME were analyzed using computer-aided technology. Based on these analyses, AxSDR was rationally designed, leading to the identification of a triple-point variant, G94T/H145Y/Y188L (Mu3), which exhibited a 2-fold increase in catalytic efficiency. After condition optimization, Mu3 cells were able to convert 300 mM BOME, achieving a space-time yield of 15.1 g/L/h. The sustainability of the (2S,3R)-BHME biosynthesis method was further enhanced by immobilizing Mu3 on IPA-tolerant amino resin. The space-time yield of the immobilized enzyme Mu3-imm increased to 75.3 g/(Lh) and was maintained at 50.2 g/(Lh) after 100 uses. These results demonstrate the significant industrial application potential of Mu3-imm in reducing the costs and environmental risks associated with the preparation of (2S,3R)-BHME and its downstream products such as 4-AA, Penem, and Carbapenem antibiotics.
Keyword ：
asymmetrically reduction asymmetrically reduction carbonyl reductases carbonyl reductases immobilization immobilization methyl (2S,3R)-2-[(benzoylamino)methyl]-3-hydroxybutanoate methyl (2S,3R)-2-[(benzoylamino)methyl]-3-hydroxybutanoate rational design rational design sustainability sustainability
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| GB/T 7714 | Meng, Fengwei , Su, Bingmei , Lin, Juan . Biosynthesis of Methyl (2S,3R)-2-[(Benzoylamino)methyl]-3-hydroxybutanoate in High Space-Time Yield with Immobilized Engineered Carbonyl Reductase [J]. | ACS SUSTAINABLE CHEMISTRY & ENGINEERING , 2025 , 13 (2) : 767-777 . |
| MLA | Meng, Fengwei et al. "Biosynthesis of Methyl (2S,3R)-2-[(Benzoylamino)methyl]-3-hydroxybutanoate in High Space-Time Yield with Immobilized Engineered Carbonyl Reductase" . | ACS SUSTAINABLE CHEMISTRY & ENGINEERING 13 . 2 (2025) : 767-777 . |
| APA | Meng, Fengwei , Su, Bingmei , Lin, Juan . Biosynthesis of Methyl (2S,3R)-2-[(Benzoylamino)methyl]-3-hydroxybutanoate in High Space-Time Yield with Immobilized Engineered Carbonyl Reductase . | ACS SUSTAINABLE CHEMISTRY & ENGINEERING , 2025 , 13 (2) , 767-777 . |
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Esomeprazole is the most popular proton pump inhibitor for treating gastroesophageal reflux disease. Previously, a phenylacetone monooxygenase mutant LnPAMOmu15 (LM15) was obtained by protein engineering for asymmetric synthesis of esomeprazole using pyrmetazole as substrate. To scale up the whole cell asymmetric synthesis of esomeprazole and reduce the cost, in this work, an Escherichia coli whole-cell catalyst harboring LM15 and formate dehydrogenase from Burkholderia stabilis 15516 (BstFDH) were constructed through optimized gene assembly patterns. CRISPR/Cas9 mediated insertion of Ptrc promoter in genome was done to enhance the expression of key genes to increase the cellular NADP supply in the whole cell catalyst, by which the amount of externally added NADP+ for the asymmetric synthesis of esomeprazole decreased to 0.05 mM from 0.3 mM for reducing the cost. After the optimization of reaction conditions in the reactor, the scalable synthesis of esomeprazole was performed using the efficient LM15-BstFDH whole-cell as catalyst, which showed the highest reported space-time yield of 3.28 g/L/h with 50 mM of pyrmetazole loading. Isolation procedure was conducted to obtain esomeprazole sodium of 99.55 % purity and > 99.9 % ee with 90.1 % isolation yield. This work provides the basis for production of enantio-pure esomeprazole via cost-effective whole cell biocatalysis. © 2024
Keyword ：
Asymmetric sulfoxidation Asymmetric sulfoxidation Cofactor engineering Cofactor engineering CRISPR/Cas9 CRISPR/Cas9 Esomeprazole Esomeprazole Whole-cell catalysis Whole-cell catalysis
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| GB/T 7714 | Xu, X. , Meng, Y. , Su, B. et al. Development of whole cell biocatalytic system for asymmetric synthesis of esomeprazole with enhancing coenzyme biosynthesis pathway [J]. | Enzyme and Microbial Technology , 2024 , 179 . |
| MLA | Xu, X. et al. "Development of whole cell biocatalytic system for asymmetric synthesis of esomeprazole with enhancing coenzyme biosynthesis pathway" . | Enzyme and Microbial Technology 179 (2024) . |
| APA | Xu, X. , Meng, Y. , Su, B. , Lin, J. . Development of whole cell biocatalytic system for asymmetric synthesis of esomeprazole with enhancing coenzyme biosynthesis pathway . | Enzyme and Microbial Technology , 2024 , 179 . |
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Ectoine, so-called tetrahydropyrimidine, is an important osmotic adjustment solute and widely applied in cosmetics and protein protectant. Some attempts have been made to improve the ectoine productivity. However, the strains with both high ectoine production capacity and high glucose conversion were still absent so far. Aim to construct a strain for efficiently producing ectoine, ectoine synthetic gene cluster ectABC from Pseudomonas stutzeri was overexpressed in E. coli BL21 (DE3). The ection production was improved by 382 % (ectoine titer increased from 1.73 g/L to 8.33 g/L) after the rational design of rate-limiting enzyme L-2,4-diaminobutyrate transaminase EctBps (protein engineering) combined with the metabolic engineering that focused on the enrichment and conversion of precursors. The final strain YW20 was applied to overproduce ectoine in fed-batch fermentation and yield 68.9 g/L of ectoine with 0.88 g/L/h of space-time yield and the highest glucose conversion reported [34 % (g/g)]. From the fermentation broth, ectoine was purified with 99.7 % purity and 79.8 % yield. This study successfully provided an engineered strain as well as an efficient method for the industrial biosynthesis and preparation of ectoine.
Keyword ：
Ectoine Ectoine L-2,4-diaminobutyrate transaminase L-2,4-diaminobutyrate transaminase Metabolic engineering Metabolic engineering
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| GB/T 7714 | Su, Bingmei , Yang, Wen , Zhou, Yi et al. Efficiently manufacturing ectoine via metabolic engineering and protein engineering of L-2,4-diaminobutyrate transaminase [J]. | INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES , 2024 , 275 . |
| MLA | Su, Bingmei et al. "Efficiently manufacturing ectoine via metabolic engineering and protein engineering of L-2,4-diaminobutyrate transaminase" . | INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES 275 (2024) . |
| APA | Su, Bingmei , Yang, Wen , Zhou, Yi , Lin, Juan . Efficiently manufacturing ectoine via metabolic engineering and protein engineering of L-2,4-diaminobutyrate transaminase . | INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES , 2024 , 275 . |
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S-omeprazole and R-rabeprazole are important proton pump inhibitors (PPIs) used for treating peptic disorders. They can be biosynthesized from the corresponding sulfide catalyzed by Baeyer-Villiger monooxygenases (BVMOs). During the development of BVMOs for target sulfoxide preparation, stereoselectivity and over- oxidation degree are important factors considered most. In the present study, LnPAMO-Mu15 designed previously and TtPAMO from Thermothelomyces thermophilus showed high (S)- and (R)-configuration stereoselectivity respectively towards thioethers. TtPAMO was found to be capable of oxidating omeprazole sulfide (OPS) and rabeprazole sulfide (RPS) into R-omeprazole and R-rabeprazole respectively. However, the overoxidation issue existed and limited the application of TtPAMO in the biosynthesis of sulfoxides. The structural mechanisms for adverse stereoselectivity between LnPAMO-Mu15 and TtPAMO towards OPS and the overoxidation of OPS by TtPAMO were revealed, based on which, TtPAMO was rationally designed focused on the flexibility of loops near catalytic sites. The variant TtPAMO-S482Y was screened out with lowest overoxidation degree towards OPS and RPS due to the decreased flexibility of catalytic center than TtPAMO. The success in this study not only proved the rationality of the overoxidation mechanism proposed in this study but also provided hints for the development of BVMOs towards thioether substrate for corresponding sulfoxide preparation.
Keyword ：
Baeyer-Villiger monooxygenase Baeyer-Villiger monooxygenase Flexibility Flexibility Overoxidation Overoxidation R-rabeprazole R-rabeprazole S-omeprazole S-omeprazole Stereoselectivity Stereoselectivity
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| GB/T 7714 | Su, Bingmei , Xu, Fahui , Zhong, Jinchang et al. Rational design on loop regions for precisely regulating flexibility of catalytic center to mitigate overoxidation of prazole sulfides by Baeyer-Villiger monooxygenase [J]. | BIOORGANIC CHEMISTRY , 2024 , 151 . |
| MLA | Su, Bingmei et al. "Rational design on loop regions for precisely regulating flexibility of catalytic center to mitigate overoxidation of prazole sulfides by Baeyer-Villiger monooxygenase" . | BIOORGANIC CHEMISTRY 151 (2024) . |
| APA | Su, Bingmei , Xu, Fahui , Zhong, Jinchang , Xu, Xinqi , Lin, Juan . Rational design on loop regions for precisely regulating flexibility of catalytic center to mitigate overoxidation of prazole sulfides by Baeyer-Villiger monooxygenase . | BIOORGANIC CHEMISTRY , 2024 , 151 . |
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Norepinephrine, a kind of beta-adrenergic receptor agonist, is commonly used for treating shocks and hypotension caused by a variety of symptoms. The development of a straightforward, efficient and environmentally friendly biocatalytic route for manufacturing norepinephrine remains a challenge. Here, we designed and realized an artificial biocatalytic cascade to access norepinephrine starting from 3, 4-dihydroxybenzaldehyde and L-threonine mediated by a tailored-made L-threonine transaldolase PsLTTA-Mu1 and a newly screened tyrosine decarboxylase ErTDC. To overcome the imbalance of multi-enzymes in a single cell, engineering of PsLTTA for improved activity and fine-tuning expression mode of multi-enzymes in single E.coli cells were combined, leading to a robust whole cell biocatalyst ES07 that could produce 100 mM norepinephrine with 99% conversion, delivering a highest time-space yield (3.38 g/L/h) ever reported. To summarized, the current study proposed an effective biocatalytic approach for the synthesis of norepinephrine from low-cost substrates, paving the way for industrial applications of enzymatic norepinephrine production.
Keyword ：
Biocatalytic cascade Biocatalytic cascade L-threonine transaldolase L-threonine transaldolase Tyrosine decarboxylase Tyrosine decarboxylase
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| GB/T 7714 | Xu, Lian , Shen, Jun-Jiang , Wu, Ming et al. An artificial biocatalytic cascade for efficient synthesis of norepinephrine by combination of engineered L-threonine transaldolase with multi-enzyme expression fine-tuning [J]. | INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES , 2024 , 265 . |
| MLA | Xu, Lian et al. "An artificial biocatalytic cascade for efficient synthesis of norepinephrine by combination of engineered L-threonine transaldolase with multi-enzyme expression fine-tuning" . | INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES 265 (2024) . |
| APA | Xu, Lian , Shen, Jun-Jiang , Wu, Ming , Su, Bing-Mei , Xu, Xin-Qi , Lin, Juan . An artificial biocatalytic cascade for efficient synthesis of norepinephrine by combination of engineered L-threonine transaldolase with multi-enzyme expression fine-tuning . | INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES , 2024 , 265 . |
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Organofluorine compounds find extensive application in the fields of agrochemicals, pharmaceuticals, materials science, and molecular imaging. Introducing fluorine atoms can provide organic compounds with unique physicochemical properties or improve their biological activity. Although significant progress has been made in the chemical synthesis of fluorine-containing compounds, achieving selective fluorination under mild conditions remains extremely challenging. Introducing biocatalytic approaches in organofluorine chemistry is an important strategy given their high efficiency, selectivity, and environmental friendliness. In this review, we present the discovery of fluorinated natural products and fluorinases, the crystal structure and the directed evolution of fluorinases, with a focus on recent advances in the enzymatic synthesis of fluorine-containing compounds in recent years. It is hoped that this review will help to promote the field of biocatalytic organofluorine compound synthesis. Organofluorine compounds play a crucial role in agrochemicals, pharmaceuticals, and materials science. Biocatalysis has emerged as an essential strategy in the synthesis of fluorinated molecules under mild conditions. This review mainly focused on recent advances in the enzymatic synthesis of fluorine-containing compounds. Furthermore, the identification of fluorinated natural products and fluorinases, the crystal structure and the directed evolution of fluorinases were discussed. image
Keyword ：
C-F bond C-F bond enzyme enzyme fluorinase fluorinase fluorinated compounds fluorinated compounds fluorination fluorination
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| GB/T 7714 | Lin, Yuqi , Xue, Wanqing , Li, Hechen et al. Advances in Enzymatic Incorporation of Small Fluorine Modules [J]. | EUROPEAN JOURNAL OF ORGANIC CHEMISTRY , 2024 , 27 (17) . |
| MLA | Lin, Yuqi et al. "Advances in Enzymatic Incorporation of Small Fluorine Modules" . | EUROPEAN JOURNAL OF ORGANIC CHEMISTRY 27 . 17 (2024) . |
| APA | Lin, Yuqi , Xue, Wanqing , Li, Hechen , Su, Bingmei , Lin, Juan , Ye, Ke-Yin . Advances in Enzymatic Incorporation of Small Fluorine Modules . | EUROPEAN JOURNAL OF ORGANIC CHEMISTRY , 2024 , 27 (17) . |
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Esomeprazole is the most popular proton pump inhibitor for treating gastroesophageal reflux disease. Previously, a phenylacetone monooxygenase mutant LnPAMOmu15 (LM15) was obtained by protein engineering for asymmetric synthesis of esomeprazole using pyrmetazole as substrate. To scale up the whole cell asymmetric synthesis of esomeprazole and reduce the cost, in this work, an Escherichia coli whole-cell catalyst harboring LM15 and formate dehydrogenase from Burkholderia stabilis 15516 (BstFDH) were constructed through optimized gene assembly patterns. CRISPR/Cas9 mediated insertion of P-trc promoter in genome was done to enhance the expression of key genes to increase the cellular NADP supply in the whole cell catalyst, by which the amount of externally added NADP(+) for the asymmetric synthesis of esomeprazole decreased to 0.05 mM from 0.3 mM for reducing the cost. After the optimization of reaction conditions in the reactor, the scalable synthesis of esomeprazole was performed using the efficient LM15-BstFDH whole-cell as catalyst, which showed the highest reported space-time yield of 3.28 g/L/h with 50 mM of pyrmetazole loading. Isolation procedure was conducted to obtain esomeprazole sodium of 99.55 % purity and > 99.9 % ee with 90.1 % isolation yield. This work provides the basis for production of enantio-pure esomeprazole via cost-effective whole cell biocatalysis.
Keyword ：
Asymmetric sulfoxidation Asymmetric sulfoxidation Cofactor engineering Cofactor engineering CRISPR/Cas9 CRISPR/Cas9 Esomeprazole Esomeprazole Whole-cell catalysis Whole-cell catalysis
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| GB/T 7714 | Xu, Xinqi , Meng, Yaping , Su, Bingmei et al. Development of whole cell biocatalytic system for asymmetric synthesis of esomeprazole with enhancing coenzyme biosynthesis pathway [J]. | ENZYME AND MICROBIAL TECHNOLOGY , 2024 , 179 . |
| MLA | Xu, Xinqi et al. "Development of whole cell biocatalytic system for asymmetric synthesis of esomeprazole with enhancing coenzyme biosynthesis pathway" . | ENZYME AND MICROBIAL TECHNOLOGY 179 (2024) . |
| APA | Xu, Xinqi , Meng, Yaping , Su, Bingmei , Lin, Juan . Development of whole cell biocatalytic system for asymmetric synthesis of esomeprazole with enhancing coenzyme biosynthesis pathway . | ENZYME AND MICROBIAL TECHNOLOGY , 2024 , 179 . |
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Enantiopure 1,2-diols are widely used in the production of pharmaceuticals, cosmetics, and functional materials as essential building blocks or bioactive compounds. Nevertheless, developing a mild, efficient and environmentally friendly biocatalytic route for manufacturing enantiopure 1,2-diols from simple substrate remains a challenge. Here, we designed and realized a step-wise biocatalytic cascade to access chiral 1,2-diols starting from aromatic aldehyde and formaldehyde enabled by a newly mined benzaldehyde lyase from Sphingobium sp. combined with a pair of tailored-made short-chain dehydrogenase/reductase from Pseudomonas monteilii (PmSDR-MuR and PmSDR-MuS) capable of producing (R)- and (S)-1-phenylethane-1,2-diol with 99% ee. The planned biocatalytic cascade could synthesize a series of enantiopure 1,2-diols with a broad scope (16 samples), excellent conversions (94%-99%), and outstanding enantioselectivity (up to 99% ee), making it an effective technique for producing chiral 1,2-diols in a more environmentally friendly and sustainable manner. A step-wise biocatalytic cascade to access chiral 1,2-diols starting from aromatic aldehyde and formaldehyde enabled by a newly mined ThDP-dependent benzaldehyde lyase from Sphingobium sp. combined with a pair of tailored-made short-chain dehydrogenase/reductase from Pseudomonas monteilii (PmSDR-MuR and PmSDR-MuS). image
Keyword ：
benzaldehyde lyase benzaldehyde lyase chiral 1,2-diols chiral 1,2-diols rational design rational design short-chain dehydrogenase/reductase short-chain dehydrogenase/reductase
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| GB/T 7714 | Ren, Xiu-Xin , Su, Bing-Mei , Xu, Xin-Qi et al. Rational design of short-chain dehydrogenase/reductase for enantio-complementary synthesis of chiral 1,2-diols by successive hydroxymethylation and reduction of aldehydes [J]. | BIOTECHNOLOGY AND BIOENGINEERING , 2024 , 121 (12) : 3796-3807 . |
| MLA | Ren, Xiu-Xin et al. "Rational design of short-chain dehydrogenase/reductase for enantio-complementary synthesis of chiral 1,2-diols by successive hydroxymethylation and reduction of aldehydes" . | BIOTECHNOLOGY AND BIOENGINEERING 121 . 12 (2024) : 3796-3807 . |
| APA | Ren, Xiu-Xin , Su, Bing-Mei , Xu, Xin-Qi , Xu, Lian , Lin, Juan . Rational design of short-chain dehydrogenase/reductase for enantio-complementary synthesis of chiral 1,2-diols by successive hydroxymethylation and reduction of aldehydes . | BIOTECHNOLOGY AND BIOENGINEERING , 2024 , 121 (12) , 3796-3807 . |
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The synthesis of steroids is challenging through multistep steroidal core modifications with high site-selectivity and productivity. In this work, a novel enzymatic cascade system was constructed for synthesis of testolactone by specific C17 lactonization/A1-dehydrogenation from inexpensive androstenedione using an engineered polycyclic ketone monooxygenase (PockeMO) and an appropriate 3-ketosteroid-A1-dehydrogenase (ReKstD). The focused saturation mutagenesis in the substrate binding pocket was implemented for evolution of PockeMO to eliminate the bottleneck effect. A best mutant MU3 (I225L/L226V/L532Y) was obtained with 20-fold higher specific activity compared to PockeMO. The catalytic efficiency (kcat/Km) of MU3 was 171-fold higher and the substrate scope shifted to polycyclic ketones. Molecular dynamic simulations suggested that the activity was improved by stabilization of the pre-lactonization state and generation of productive orientation of 4-AD mediated by distal L532Y mutation. Based on that, the three genes, MU3, ReKstD and a ketoreductase for NADPH regeneration, were rationally integrated in one cell via expression fine-tuning to form the efficient single cell catalyst E. coli S9. The single whole-cell biocatalytic process was scaled up and could generate 9.0 g/L testolactone with the high space time yield of 1 g/L/h without steroidal by-product, indicating the potential for site-specific and one-pot synthesis of steroid.
Keyword ：
Enzymatic cascade Enzymatic cascade Gene co-expression tuning Gene co-expression tuning Polycyclic ketone monooxygenase Polycyclic ketone monooxygenase Protein engineering Protein engineering Testolactone Testolactone
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| GB/T 7714 | Xu, Xinqi , Zhong, Jinchang , Su, Bingmei et al. Single-cell enzymatic cascade synthesis of testolactone enabled by engineering of polycyclic ketone monooxygenase and multi-gene expression fine-tuning [J]. | INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES , 2024 , 275 . |
| MLA | Xu, Xinqi et al. "Single-cell enzymatic cascade synthesis of testolactone enabled by engineering of polycyclic ketone monooxygenase and multi-gene expression fine-tuning" . | INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES 275 (2024) . |
| APA | Xu, Xinqi , Zhong, Jinchang , Su, Bingmei , Xu, Lian , Hong, Xiaokun , Lin, Juan . Single-cell enzymatic cascade synthesis of testolactone enabled by engineering of polycyclic ketone monooxygenase and multi-gene expression fine-tuning . | INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES , 2024 , 275 . |
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