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One-step synthesis of thermally stable artificial multienzyme cascade system for efficient enzymatic electrochemical detection

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Nano Research 2019年第12期12卷 3031-3036页

作者： Xiqing Cheng Jinhong Zhou Jiayu Chen Zhaoxiong Xie Qin Kuang Lansun Zheng State Key Laboratory of Physical Chemistry of Solid Surfaces Collaborative Innovation Center of Chemistry for Energy Materialsand Department of ChemistryCollege of Chemistry and Chemical Engineering Xiamen UniversityXiamen 361005China Pen-Tung Sah Institute of Micro-Nano Science and Technology Xiamen UniversityXiamen 361005China

Recently,metal-organic framework(MOF)-based multienzyme systems integrating different functional natural enzymes and/or nanomaterial-basedartificial enzymes are attracting increasing attention due to their high catalytic efficiency and promising application in *** controllable integration of enzymes or nanozymes within MOFs is crucial for achieving efficient cascade catalysis and high ***,we report a facile electrochemical assisted biomimetic mineralization strategy to prepare an artificial multienzyme system for efficient electrochemicaldetection of *** using the G0x@Cu-MOF/copper foam(G0x@Cu-MOF/CF)architecture as a proof of concept,efficientenzyme immobilization and cascade catalysis were achieved by in situ encapsulation of glucose oxidase(GOx)within MOFs layer grown onthree-dimensional(3D)porous conducting CF via a facile one-step electrochemical assisted biomimetic mineralization *** to thebio-electrocatalytic cascade reaction mechanism,this well-designed GOx@Cu-MOF modified electrode exhibited superior catalytic activityand thermal stability for glucose ***,the activity of GOx@Cu-MOF/CF still remained at ca.80%after being incubated at 80℃.In sharp contrast,the activity of the unprotected electrode was reduced to the original 10%after the same *** design strategypresented here may be useful in fabricating highly stable enzyme@MOF composites applied for efficient photothermal therapy and otherplatform under high temperature.

关键词： metal-organic frameworks artificial multienzyme electrochemical assisted biomimetic mineralization glucose detection thermal stability

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A unique insertion of low complexity amino acid sequence underlies protein-protein interaction in human malaria parasite orotate phosphoribosyltransferase and orotidine 5'-monophosphate decarboxylase

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Asian Pacific Journal of Tropical Medicine 2014年第3期7卷 184-192页

作者： Waranya Imprasittichai Sittiruk Roytrakul Sudaratana R.Krungkrai Jcrapan Krungkrai Department of Biochemistry.Faculty of Medicine.Chulalongkorn University National Center for Genetic Engineering and Biotechnology Unit of Biochemistry.Department of Medical Science.Faculty of Science Rangsit University

Objective:To investigate the multienzyine complex formation of human malaria parasite Plasmodium falciparum[***)orotate phosphoribosyltransferase(OPRT)and orotidine5'-monophosphate decarboxylase(OMPDC),the fifth and sixth enzyme of the de novo pyrimidine biosynthetic ***,we have clearly established that the two enzymes in the malaria parasite exist physically as a heterotetrameric(OPRT)_2(OMPDG)_2 complex containing two subunits each of OPRT and *** that the complex have catalytic kinetic advantages over the monofunetional ***:Both enzymes were cloned and expressed as recombinant *** protein-protein interaction in the enzyme complex was identified using bifunctionul chemical cross-linker,liquid chromatography-mass spectrometric analysis and homology modeling,Results:The unique insertions of low complexity region at the a 2 and a 5 helices of the parasite OMPDC,characterized by single amino acid repeat sequence which was not found in homologous proteins from other organisms,was located on the OPRT-OMPDC *** structural models for the protein-prolein interaction of the helerotetrameric(OPRT)_2(OMPDC)_2multienzyme complex were ***:Based on the proteomic data and structural modeling,it is surmised that the human malaria parasite low complexity region is responsible for the OPRT-OMPDC *** structural complex of the parasite enzymes,thus,represents an efficient functional kinetic advantage,which in line with co-localization principles of evolutional origin,and allosteric control in protein-protein-interactions.

关键词： Malaria Plasmodium falciparum Pyrimidine biosynthesis Orotate phosphoribosyltransferase Orotidine 5’-monophosphate decarboxylase multienzyme complex Proteomics

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Boosted activity by engineering the enzyme microenvironment in cascade reaction: A molecular understanding

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Synthetic and Systems Biotechnology 2021年第3期6卷 163-172页

作者： Jing Wang Haiyang Zhang Deping Yin Xiao Xu Tianwei Tan Yongqin Lv Beijing Key Laboratory of Bioprocess College of Life Science and TechnologyBeijing University of Chemical TechnologyBeijing100029China Department of Biological Science and Engineering School of Chemistry and Biological EngineeringUniversity of Science and Technology BeijingBeijing100083China School of Chemical Engineering Nanjing University of Science and TechnologyNanjing210094China

Engineering of enzyme microenvironment can surprisingly boost the apparent ***,the underlying regulation mechanism is not well-studied at a molecular level so ***,we present a modulation of two model enzymes of cytochrome c(Cty C)and D-amino acid oxidase(DAAO)with opposite pH-activity profiles using ionic *** operational pH of poly(acrylic acid)modified Cyt C and polyallylamine modified DAAO was extended to 3-7 and 2-10 where the enzyme activity was larger than that at their optimum pH of 4.5 and 8.5 by 106%and 28%,*** cascade reaction catalyzed by two modified enzymes reveals a 1.37-fold enhancement in catalytic efficiency compared with their native *** enzyme activity boosting is understood by performing the UV-vis/CD spectroscopy and molecular dynamics simulations in the atomistic *** increased activity is ascribed to the favorable microenvironment in support of preserving enzyme native structures nearby cofactor under external perturbations.

关键词： Engineering of microenvironment Ionic polymers multienzyme Boosted activity Molecular dynamics simulation Molecular understanding

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