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multienzyme system

Namrata Singh, Mohammed Azharuddin Savanur, Shubhi Srivastava, Patrick D'Silva, Govindasamy Mugesh
Biocompatible nanoparticles with an intrinsic ability to mimic the cellular antioxidant enzymes are potential candidates for the development of new therapeutics for various oxidative stress related disorders. However, the understanding of the interaction and the mechanistic crosstalk between the nanoparticles and the cellular biomolecules is limited. Here we show that the multienzyme mimic manganese(ii,iii) oxide, Mn3O4, in nanoform (Mp) rescues the cells from oxidative damage induced by reactive oxygen species (ROS)...
February 13, 2019: Nanoscale
Xiaoyu Mu, Junying Wang, Yonghui Li, Fujuan Xu, Wei Long, Lufei Ouyang, Haile Liu, Yaqi Jing, Jingya Wang, Haitao Dai, Qiang Liu, Yuanming Sun, Changlong Liu, Xiao-Dong Zhang
Metal nanozyme has attracted wide interest for biomedicine, and a highly catalytic material in physiological environment is highly desired. However, catalytic selectivity of nanozyme is still highly challenged, limiting its wide application. Here, we show a trimetallic (triM) nanozyme with highly catalytic activity and environmental selectivity. Enzyme-mimicked investigations find that triM system possesses multienzyme mimetics activity for removing reactive oxygen species (ROS) and reactive nitrogen species (RNS), such as 1O2, H2O2, •OH, and •NO...
February 12, 2019: ACS Nano
Wanqing Li, John B McArthur, Xi Chen
Carbohydrates are structurally complex but functionally important biomolecules. Therefore, they have been challenging but attractive synthetic targets. While substantial progress has been made on advancing chemical glycosylation methods, incorporating enzymes into carbohydrate synthetic schemes has become increasingly practical as more carbohydrate biosynthetic and metabolic enzymes as well as their mutants with synthetic application are identified and expressed for preparative and large-scale synthesis. Chemoenzymatic strategies that integrate the flexibility of chemical derivatization with enzyme-catalyzed reactions have been extremely powerful...
November 24, 2018: Carbohydrate Research
Anders Barth, Jelle Hendrix, Daniel Fried, Yoav Barak, Edward A Bayer, Don C Lamb
Efficient degradation of plant cell walls by selected anaerobic bacteria is performed by large extracellular multienzyme complexes termed cellulosomes. The spatial arrangement within the cellulosome is organized by a protein called scaffoldin, which recruits the cellulolytic subunits through interactions between cohesin modules on the scaffoldin and dockerin modules on the enzymes. Although many structural studies of the individual components of cellulosomal scaffoldins have been performed, the role of interactions between individual cohesin modules and the flexible linker regions between them are still not entirely understood...
November 27, 2018: Proceedings of the National Academy of Sciences of the United States of America
Chaoyu Tian, Jiangang Yang, Yan Zeng, Tong Zhang, Yingbiao Zhou, Yan Men, Chun You, Yueming Zhu, Yuanxia Sun
Herein, we presented a biocatalytic method to produce raffinose and stachyose using sucrose as the substrate. An in vitro multienzyme system was developed using five enzymes, namely, sucrose synthase (SUS), UDP-glucose 4-epimerase (GalE), galactinol synthase (GS), raffinose synthase (RS), and stachyose synthase (STS), and two intermedia, namely, uridine diphosphate (UDP) and inositol, which can be recycled. This reaction system produced 11.1 mM raffinose using purified enzymes under optimal reaction conditions and substrate concentrations...
November 2, 2018: Applied and Environmental Microbiology
Zhiping Zhang, Yanzhi He, Yue Huang, Li Ding, Lei Chen, Yaxian Liu, Yesen Nie, Xinyue Zhang
No abstract text is available yet for this article.
October 26, 2018: Journal of Agricultural and Food Chemistry
An Xiao, Teri J Slack, Yanhong Li, Dashuang Shi, Hai Yu, Wanqing Li, Yang Liu, Xi Chen
Streptococcus pneumoniae sialidase SpNanB is an intramolecular trans-sialidase (IT-sialidase) and a virulence factor that is essential for streptococcal infection of the upper and lower respiratory tract. SpNanB catalyzes the formation of 2,7-anhydro- N-acetylneuraminic acid (2,7-anhydro-Neu5Ac), a potential prebiotic that can be used as the sole carbon source of a common human gut commensal anaerobic bacterium. We report here the development of an efficient one-pot multienzyme (OPME) system for synthesizing 2,7-anhydro-Neu5Ac and its derivatives...
September 21, 2018: Journal of Organic Chemistry
Mengke Wang, Dandan Su, Guannan Wang, Xingguang Su
In this work, a facile, label-free, and sensitive fluorometric strategy for detection of trypsin and its inhibitor was established on the basis of the fluorescence resonance energy transfer (FRET) between mercaptoundecanoic acid functionalized gold nanoclusters (AuNCs) and gold nanoparticles (AuNPs) via protamine as a bridge. Protamine can trigger the aggregation of AuNPs and link AuNCs with aggregated AuNPs through electrostatic interaction. Compared with monodisperse AuNPs, the UV-vis absorption band of aggregated AuNPs overlapped considerably with the emission spectrum of AuNCs...
October 2018: Analytical and Bioanalytical Chemistry
Veronika Baresova, Vaclava Skopova, Olga Souckova, Matyas Krijt, Stanislav Kmoch, Marie Zikanova
BACKGROUND: The enzymes involved in de novo purine synthesis (DNPS), one of the basic processes in eukaryotic cells, transiently and reversibly form a dynamic multienzyme complex called the purinosome in the cytoplasm. The purinosome has been observed in a broad spectrum of cells, but some studies claim that it is an artefact of the constructs used for visualization or stress granules resulting from the exposure of cells to nutrient-reduced growth media. Both may be true depending on the method of observation...
2018: PloS One
Zhiping Zhang, Yanzhi He, Yue Huang, Li Ding, Lei Chen, Yaxian Liu, Yesen Nie, Xinyue Zhang
An in vitro multienzyme synthetic system was developed and optimized to efficiently produce kaempferol in a single reaction tube. Two key genes, Atf3h and Atfls1, in the biosynthetic pathway of kaempferol were cloned into a prokaryotic expression vector and overexpressed in Escherichia coli. The recombinant proteins were purified through affinity chromatography and showed activities of flavanone 3-hydroxylase and flavonol synthase, respectively, followed by development of an in vitro synthetic system for producing kaempferol...
August 8, 2018: Journal of Agricultural and Food Chemistry
Xinyun Cao, Tobias Koch, Lydia Steffens, Julia Finkensieper, Renate Zigann, John E Cronan, Christiane Dahl
Many Bacteria and Archaea employ the heterodisulfide reductase (Hdr)-like sulfur oxidation pathway. The relevant genes are inevitably associated with genes encoding lipoate-binding proteins (LbpA). Here, deletion of the gene identified LbpA as an essential component of the Hdr-like sulfur-oxidizing system in the Alphaproteobacterium Hyphomicrobium denitrificans . Thus, a biological function was established for the universally conserved cofactor lipoate that is markedly different from its canonical roles in central metabolism...
July 13, 2018: ELife
Li Zhou, Yu Liu, Hui Shi, Xiaohai Yang, Jin Huang, Songyang Liu, Qiaoshu Chen, Jianbo Liu, Kemin Wang
Spatial organization of multiple enzymes at specific positions for a controlled reaction cascade has attracted wide attention in recent years. Here, we report the construction of a biomimetic enzyme cascade organized on DNA triangle prism (TP) nanostructures to enable the efficient catalytic production of nitric oxide (NO) on a single microbead. Two enzymes, glucose oxidase (GOx) and horseradish peroxidase (HRP), were assembled at adjacent locations on a DNA TP nanostructure by using DNA-binding protein adaptors with small interenzyme distances...
October 4, 2018: Chembiochem: a European Journal of Chemical Biology
Huan Wang, Ze Zhao, Yuxiao Liu, Changmin Shao, Feika Bian, Yuanjin Zhao
Mimicking subcellular compartments containing enzymes in organisms is considered a promising approach to substitute for missing or lost cellular functions. Inspired by the multicompartment structures of cellular architectures, we present a novel multienzyme system based on hollow hydrogel microcapsules with flexible enzymatic inverse opal particles. Benefiting from the precise operation capability of the microfluidic electrospray and the remarkable structural color marks in the inverse opal particles, we developed a multienzyme system with controllable number, type, and spatial arrangement of the encapsulated enzymes...
June 2018: Science Advances
Moritz Hunkeler, Anna Hagmann, Edward Stuttfeld, Mohamed Chami, Yakir Guri, Henning Stahlberg, Timm Maier
Acetyl-CoA carboxylase catalyses the ATP-dependent carboxylation of acetyl-CoA, a rate-limiting step in fatty acid biosynthesis1,2 . Eukaryotic acetyl-CoA carboxylases are large, homodimeric multienzymes. Human acetyl-CoA carboxylase occurs in two isoforms: the metabolic, cytosolic ACC1, and ACC2, which is anchored to the outer mitochondrial membrane and controls fatty acid β-oxidation1,3 . ACC1 is regulated by a complex interplay of phosphorylation, binding of allosteric regulators and protein-protein interactions, which is further linked to filament formation1,4-8 ...
June 2018: Nature
Alan T Culbertson, Jacqueline J Ehrlich, Jun-Yong Choe, Richard B Honzatko, Olga A Zabotina
The plant cell wall is primarily a polysaccharide mesh of the most abundant biopolymers on earth. Although one of the richest sources of biorenewable materials, the biosynthesis of the plant polysaccharides is poorly understood. Structures of many essential plant glycosyltransferases are unknown and suitable substrates are often unavailable for in vitro analysis. The dearth of such information impedes the development of plants better suited for industrial applications. Presented here are structures of Arabidopsis xyloglucan xylosyltransferase 1 (XXT1) without ligands and in complexes with UDP and cellohexaose...
June 5, 2018: Proceedings of the National Academy of Sciences of the United States of America
Cyril Lefebvre, Richard Boulon, Manuelle Ducoux, Sabine Gavalda, Françoise Laval, Stevie Jamet, Nathalie Eynard, Anne Lemassu, Kaymeuang Cam, Marie-Pierre Bousquet, Fabienne Bardou, Odile Burlet-Schiltz, Mamadou Daffé, Annaïk Quémard
Mycolic acids (MAs) have a strategic location within the mycobacterial envelope, deeply influencing its architecture and permeability, and play a determinant role in the pathogenicity of mycobacteria. The fatty acid synthase type II (FAS-II) multienzyme system is involved in their biosynthesis. A combination of pull-downs and proteomics analyses led to the discovery of a mycobacterial protein, HadD, displaying highly specific interactions with the dehydratase HadAB of FAS-II. In vitro activity assays and homology modeling showed that HadD is, like HadAB, a hot dog folded (R)-specific hydratase/dehydratase...
April 16, 2018: Scientific Reports
Namrata Singh, Motika Geethika, Sandeep M Eswarappa, Govindasamy Mugesh
Nanomaterials having enzyme-like activity (nanozymes) make them suitable candidates for various biomedical applications. In this study, we demonstrate the morphology-dependent enzyme mimetic activity of Mn3 O4 nanoparticles. It is found that Mn3 O4 nanoparticles mimic the functions of all three cellular antioxidant enzymes: superoxide dismutase (SOD), catalase (CAT), and glutathione peroxidase (GPx). Interestingly, the nanozyme activity of Mn3 O4 depends on various factors including size, morphology, surface area, and the redox properties of the metal ions...
June 12, 2018: Chemistry: a European Journal
Jean Felix Mukerabigwi, Zhishen Ge, Kazunori Kataoka
Therapeutic nanoreactors have been proposed as nanoplatforms to treat diseases through in situ production of therapeutic agents. When this treatment strategy is applied in cancer therapy, it can efficiently produce highly toxic anticancer drugs in situ from low-toxic prodrugs or some biomolecules in tumor tissues, which can maximize the therapeutic efficacy with a significantly low systemic toxicity. An ideal therapeutic nanoreactor can provide the reaction space, protect the loaded fragile catalysts, target the desired pathological site, and be selectively activated...
October 22, 2018: Chemistry: a European Journal
Hui-Lei Yu, Tuo Li, Fei-Fei Chen, Xiao-Jing Luo, Aitao Li, Chao Yang, Gao-Wei Zheng, Jian-He Xu
Biocatalytic C-H amination is one of the most challenging tasks. C-H amination reaction can hardly be driven efficiently by solely one enzyme so far. Thus, enzymatic synergy represents an alternative strategy. Herein, we report an "Artificially Bioamination Pathway" for C-H amination of cyclohexane as a model substrate. Three enzymes, a monooxygenase P450BM3 mutant, an alcohol dehydrogenase ScCR from Streptomyces coelicolor and an amine dehydrogenase EsLeuDH from Exiguobacterium sibiricum, constituted a clean cascade reaction system with easy product isolation...
May 2018: Metabolic Engineering
Qi Zhang, Shuo Chen, Hua Wang, Hongtao Yu
Hydrogen peroxide (H2 O2 ) is a key reactant in the Fenton process. As a byproduct of enzymatic reaction, H2 O2 can be obtained via catalytical oxidation of glucose using glucose oxidase in the presence of O2 . Another oxidation product (gluconic acid) can suitably adjust the microenvironmental pH contributing to the Fe3+ /Fe2+ cycle in the Fenton reaction. Enzymes are extremely efficient at catalyzing a variety of reactions with high catalytic activity, substrate specificity, and yields in living organisms...
March 14, 2018: ACS Applied Materials & Interfaces
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