Wei Zhang

Nanjing Tech University

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Shengying Li

Shandong University

Xingwang Zhang

Shandong University

Lei Du

Shandong University

Min Lin

Chinese Academy of Agricultural Sciences

Fengwei Li

Shandong University

Li Ma

Shandong University

Yuemao Shen

Shandong University

Ce Geng

Qingdao Institute of Bioenergy and Bioprocess Technology

Moli Sang

City University of Hong Kong, Shenzhen Research Institute

Feifei Qi

Chinese Academy of Medical Sciences & Peking Union Medical College

Cooperative Institutions

Chinese Academy of Sciences

235

Shandong University

205

University of Chinese Academy of Sciences

130

Chinese Academy of Medical Sciences & Peking Union Medical College

Shanghai Jiao Tong University

Sun Yat-sen University

Zhejiang University

Ministry of Education of the People's Republic of China

Fudan University

Chinese Academy of Agricultural Sciences

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Somalactams A–D: Anti‐inflammatory Macrolide Lactams with Unique Ring Systems from an Arctic Actinomycete Strain

Angewandte Chemie International Edition (2023)

Fan Yang Moli Sang Jingrong Lü Huimin Zhao Yike Zou

Abstract Four new PKS‐NRPS‐derived macrolide lactams with three unique ring fusion types were discovered from the Arctic sponge associated actinomycete Streptomyces somaliensis 1107 using a genome mining strategy. Their structures were elucidated by a combination of MS, NMR spectroscopic analysis, and single‐crystal X‐ray diffraction. Biosynthetically, a novel gene cluster sml consisting of three polyketide synthases and one hybrid polyketide synthase‐nonribosomal peptide synthetase together with cytochrome P450s and flavin‐containing monooxygenases and oxidoreductases was demonstrated to assemble the unique skeleton. Pharmacological studies revealed that compound 1 displayed a potent anti‐inflammatory effect without cytotoxicity. It inhibited IL‐6 and TNF‐α release in the serum of LPS‐stimulated RAW264.7 macrophage cells with IC 50 values of 5.76 and 0.18 μM, respectively, and modulated the MAPK pathway. Moreover, compound 1 alleviated LPS‐induced systemic inflammation in our transgenic fluorescent zebrafish model.

Nonribosomal peptide

Polyketide synthase

Gene cluster

Strain (injury)

10.1002/anie.202218085

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Citations (7)

Mutagenesis and redox partners analysis of the P450 fatty acid decarboxylase OleTJE

Scientific Reports (2017)

Bo Fang Huifang Xu Yi Liu Fengxia Qi Wei Zhang

Abstract The cytochrome P450 enzyme OleT JE from Jeotgalicoccus sp. ATCC 8456 is capable of converting free long-chain fatty acids into α-alkenes via one-step oxidative decarboxylation in presence of H 2 O 2 as cofactor or using redox partner systems. This enzyme has attracted much attention due to its intriguing but unclear catalytic mechanism and potential application in biofuel production. Here, we investigated the functionality of a select group of residues (Arg245, Cys365, His85, and Ile170) in the active site of OleT JE through extensive mutagenesis analysis. The key roles of these residues for catalytic activity and reaction type selectivity were identified. In addition, a range of heterologous redox partners were found to be able to efficiently support the decarboxylation activity of OleT JE . The best combination turned out to be Se Fdx-6 (ferredoxin) from Synechococcus elongatus PCC 7942 and Cg FdR-2 (ferredoxin reductase) from Corynebacterium glutamicum ATCC 13032, which gave the highest myristic acid conversion rate of 94.4%. Moreover, Michaelis-Menton kinetic parameters of OleT JE towards myristic acid were determined.

Corynebacterium glutamicum

Decarboxylation

Oxidative decarboxylation

Bioconversion

Myristic acid

Site-directed mutagenesis

10.1038/srep44258

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Citations (49)

H2S scavenger as a broad-spectrum strategy to deplete bacteria-derived H2S for antibacterial sensitization

Nature Communications (2024)

Jingfeng Sun Xu Wang Ye Gao Shuangyu Li Ziwei Hu

Bacteria-derived H

Scavenger

Broad spectrum

10.1038/s41467-024-53764-7

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Citations (1)

Engineering cytochrome P450 enzyme systems for biomedical and biotechnological applications

Journal of Biological Chemistry (2019)

Zhong Li Yuanyuan Jiang F. Peter Guengerich Li Ma Shengying Li

Cytochrome P450 enzymes (P450s) are broadly distributed among living organisms and play crucial roles in natural product biosynthesis, degradation of xenobiotics, steroid biosynthesis, and drug metabolism. P450s are considered as the most versatile biocatalysts in nature because of the vast variety of substrate structures and the types of reactions they catalyze. In particular, P450s can catalyze regio- and stereoselective oxidations of nonactivated C–H bonds in complex organic molecules under mild conditions, making P450s useful biocatalysts in the production of commodity pharmaceuticals, fine or bulk chemicals, bioremediation agents, flavors, and fragrances. Major efforts have been made in engineering improved P450 systems that overcome the inherent limitations of the native enzymes. In this review, we focus on recent progress of different strategies, including protein engineering, redox-partner engineering, substrate engineering, electron source engineering, and P450-mediated metabolic engineering, in efforts to more efficiently produce pharmaceuticals and other chemicals. We also discuss future opportunities for engineering and applications of the P450 systems.

10.1074/jbc.rev119.008758

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Citations (132)

Iconography : Proteomic analysis for anti-atherosclerotic effect of tetrahydroxystilbene glucoside in rats

Wenjuan Yao Wenjun Fan Chao Huang Zhong Hui Xiangfan Chen

Glucoside

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ChemInform Abstract: The Homocoupling of Arylsulfonylhydrazides by Palladium‐Catalyzed Desulfonation in Air.

ChemInform (2014)

Wei Zhang Baoli Zhao Ke Li

Zhàng

10.1002/chin.201424092

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pH-Dependent Aggregation Behavior and Emulsion Stability of Comb-Like Surfactant Containing PEO Grafts

Journal of Dispersion Science and Technology (2012)

Wei Zhang Zhiping Du Wanxu Wang Guojin Li

Abstract The aggregation behavior of the comb-like surfactant, poly(styrene-co-maleic anhydride)-g-(poly(ethylene glycol) monomethyl ether) (SMA-M), prepared via the one-pot method, at surface and in solution, was investigated by equilibrium surface tension, rheological technology, and transmission electron microscopy (TEM). The emulsion prepared from n-decane/water/C13E7 was used as a model system to determine the influence of SMA-M on the stability of the emulsion. The equilibrium surface tensions of SMA-M solution with various pH were measured. The adsorption data, that is, the saturation surface excess concentration (Γmax) and the minimum area (A min) were evaluated using the average monomeric molecular weight (M nA ). The results showed that Γmax decreased with the increase of pH, but the A min enlarged with the increase of pH. The results of the steady-state shear experiment indicated that the aggregate structure of the as-prepared comb-like surfactant SMA-M in aqueous solution evolved from interlinked micelle-like aggregates to isolated inflated micelle-like aggregates, then to rod-like aggregates with the increasing pH, which were confirmed by the TEM images. The investigation of the stabilization of n-decane/water/C13E7/SMA-M emulsion system indicated that SMA-M obviously slows down the phase separation, and the most effectively stabilized sample was obtained at pH 5.0. Supplemental materials are available for this article. Go to the publisher's online edition of the Journal of Dispersion Science and Technology to view the free supplemental file. Keywords: Aggregate conformationaggregation behaviorcomb-like surfactantemulsion stability Acknowledgments The authors are grateful to National Natural Science Foundation of China (Grant No. 21073234) and Shanxi Natural Science Foundation (Grant No. 2012011046-3) for financial support. Notes a Determined by GPC with THF as an eluent and linear PS as standards calibration. b Determined by 1H NMR. a Deduced from the data in investigated range.

Decane

10.1080/01932691.2011.623544

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Citations (1)

The first ratiometric fluorescent probes for aminopeptidase N cell imaging

Organic & Biomolecular Chemistry (2012)

Laizhong Chen Wei Sun Jing Li Zhenzhen Liu Zhao Ma

In the current paper, three activity-based colorimetric and ratiometric fluorescent probes based on a naphthalimide fluorophore were well designed and synthesized, which can be recognized and hydrolyzed by aminopeptidase N (APN) at both the enzymatic and cellular level by following the fluorescent emission wavelength change from blue to green light. As a result, these molecules were successfully identified as the first ratiometric fluorescent probes for APN cell imaging.

Live cell imaging

10.1039/c2ob26564h

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Citations (53)

Simulation of Solid Oxide Fuel Cell - Based Power Generation Processes with CO 2 Capture

Wei Zhang

Source

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Citations (18)

Improved Efficiency of the Desulfurization of Oil Sulfur Compounds in Escherichia coli Using a Combination of Desensitization Engineering and DszC Overexpression

ACS Synthetic Biology (2019)

Lu Li Yi-Bo Liao Yifan Luo Guangming Zhang Xihao Liao

The 4S pathway of biodesulfurization, which can specifically desulfurize aromatic S-heterocyclic compounds without destroying their combustion value, is a low-cost and environmentally friendly technology that is complementary to hydrodesulfurization. The four Dsz enzymes convert the model compound dibenzothiophene (DBT) into the sulfur-free compound 2-hydroxybiphenyl (HBP). Of these four enzymes, DszC, the first enzyme in the 4S pathway, is the most severely affected by the feedback inhibition caused by HBP. This study is the first attempt to directly modify DszC to decrease its inhibition by HBP, with the results showing that the modified protein is insensitive to HBP. On the basis of the principle that the final HBP product could show a blue color with Gibbs reagent, a high-throughput screening method for its rapid detection was established. The screening method and the combinatorial mutagenesis generated the mutant AKWC (A101K/W327C) of DszC. After the IC50 was calculated, the feedback inhibition of the AKWC mutant was observed to have been substantially reduced. Interestingly, the substrate inhibition of DszC had also been reduced as a result of directed evolution. Finally, the recombinant BL21(DE3)/BADC*+C* (C* represents AKWC) strain exhibited a specific conversion rate of 214.84 μmolHBP/gDCW/h, which was 13.8-fold greater than that of the wild-type strain. Desensitization engineering and the overexpression of the desensitized DszC protein resulted in the elimination of the feedback inhibition bottleneck in the 4S pathway, which is practical and effective progress toward the production of sulfur-free fuel oil. The results of this study demonstrate the utility of desensitization of feedback inhibition regulation in metabolic pathways by protein engineering.

Dibenzothiophene

Protein Engineering

Biocatalysis

10.1021/acssynbio.9b00126

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Citations (17)