Skip Navigation
Skip to contents

Journal of Microbiology : Journal of Microbiology

OPEN ACCESS
SEARCH
Search

Search

Page Path
HOME > Search
7 "NADPH"
Filter
Filter
Article category
Keywords
Publication year
Review
[MINIREVIEW] Antimicrobial actions of dual oxidases and lactoperoxidase
Demba Sarr , Eszter Tóth , Aaron Gingerich , Balázs Rada
J. Microbiol. 2018;56(6):373-386.   Published online June 1, 2018
DOI: https://doi.org/10.1007/s12275-018-7545-1
  • 44 View
  • 0 Download
  • 56 Crossref
AbstractAbstract
The NOX/DUOX family of NADPH oxidases are transmembrane proteins generating reactive oxygen species as their primary enzymatic products. NADPH oxidase (NOX) 1–5 and Dual oxidase (DUOX) 1 and 2 are members of this family. These enzymes have several biological functions including immune defense, hormone biosynthesis, fertilization, cell proliferation and differentiation, extracellular matrix formation and vascular regulation. They are found in a variety of tissues such as the airways, salivary glands, colon, thyroid gland and lymphoid organs. The discovery of NADPH oxidases has drastically transformed our view of the biology of reactive oxygen species and oxidative stress. Roles of several isoforms including DUOX1 and DUOX2 in host innate immune defense have been implicated and are still being uncovered. DUOX enzymes highly expressed in the respiratory and salivary gland epithelium have been proposed as the major sources of hydrogen peroxide supporting mucosal oxidative antimicrobial defenses. In this review, we shortly present data on DUOX discovery, structure and function, and provide a detailed, upto- date summary of discoveries regarding antibacterial, antiviral, antifungal, and antiparasitic functions of DUOX enzymes. We also present all the literature describing the immune functions of lactoperoxidase, an enzyme working in partnership with DUOX to produce antimicrobial substances.

Citations

Citations to this article as recorded by  
  • Study the effect of lactoperoxidase activation in combination with heat treatment or nisin on the microbiological quality of raw milk
    Chedia Aouadhi, Souhir Kmiha, Faten Trakhna, Abderrazak Maaroufi
    Applied Food Research.2024; 4(2): 100521.     CrossRef
  • Identification and multimodal characterization of a specialized epithelial cell type associated with Crohn’s disease
    Jia Li, Alan J. Simmons, Caroline V. Hawkins, Sophie Chiron, Marisol A. Ramirez-Solano, Naila Tasneem, Harsimran Kaur, Yanwen Xu, Frank Revetta, Paige N. Vega, Shunxing Bao, Can Cui, Regina N. Tyree, Larry W. Raber, Anna N. Conner, Jennifer M. Pilat, Just
    Nature Communications.2024;[Epub]     CrossRef
  • To activate NAD(P)H oxidase with a brief pulse of photodynamic action
    Xiao Bing Xie, Yu Shu, Zong Jie Cui
    The FASEB Journal.2024;[Epub]     CrossRef
  • The Known and Unknown “Knowns” of Human Susceptibility to Coccidioidomycosis
    Amy P. Hsu
    Journal of Fungi.2024; 10(4): 256.     CrossRef
  • Mycobacterium tuberculosis: immune response, biomarkers, and therapeutic intervention
    Li Zhuang, Ling Yang, Linsheng Li, Zhaoyang Ye, Wenping Gong
    MedComm.2024;[Epub]     CrossRef
  • The therapeutic potential of thiocyanate and hypothiocyanous acid against pulmonary infections
    Nuha Milad Ashtiwi, Susan O. Kim, Joshua D. Chandler, Balázs Rada
    Free Radical Biology and Medicine.2024; 219: 104.     CrossRef
  • Bacteria colonization and gene expression related to immune function in colon mucosa is associated with growth in neonatal calves regardless of live yeast supplementation
    Koki Nishihara, Clothilde Villot, Lautaro Cangiano, Le Luo Guan, Michael Steele
    Journal of Animal Science and Biotechnology.2024;[Epub]     CrossRef
  • Dual oxidase 2 (duox 2) participates in the intestinal antibacterial innate immune responses of Procambarus clarkii by regulating ROS levels
    Qianqian Li, Mingda Zhang, Shiyu Qin, Jing Wen, Xiuli Shen, Zhiqiang Du
    Developmental & Comparative Immunology.2024; 153: 105116.     CrossRef
  • Dual oxidase 1 is dispensable during Mycobacterium tuberculosis infection in mice
    Tuhina Gupta, Demba Sarr, Kayla Fantone, Nuha Milad Ashtiwi, Kaori Sakamoto, Frederick D. Quinn, Balázs Rada
    Frontiers in Immunology.2023;[Epub]     CrossRef
  • Activation of lactoperoxidase system and its potential for microbial inhibition and preservation of milk in the Great African Rift Valley climate
    Kedir Awol, Mestawet Taye, Binyam Kassa
    Cogent Food & Agriculture.2023;[Epub]     CrossRef
  • Time-Course of Transcriptomic Change in the Lungs of F344 Rats Repeatedly Exposed to a Multiwalled Carbon Nanotube in a 2-Year Test
    Motoki Hojo, Ai Maeno, Yoshimitsu Sakamoto, Yukio Yamamoto, Yuhji Taquahashi, Akihiko Hirose, Jin Suzuki, Akiko Inomata, Dai Nakae
    Nanomaterials.2023; 13(14): 2105.     CrossRef
  • Bioactive peptides of whey: obtaining, activity, mechanism of action, and further applications
    L. B. Olvera-Rosales, A. E. Cruz-Guerrero, J. M. García-Garibay, L. C. Gómez-Ruíz, E. Contreras-López, F. Guzmán-Rodríguez, L. G. González-Olivares
    Critical Reviews in Food Science and Nutrition.2023; 63(30): 10351.     CrossRef
  • Neutrophil defect and lung pathogen selection in cystic fibrosis
    Scott Jennings, Yawen Hu, Dianne Wellems, Meng Luo, Callie Scull, Christopher M Taylor, William M Nauseef, Guoshun Wang
    Journal of Leukocyte Biology.2023; 113(6): 604.     CrossRef
  • Hypothiocyanite and host–microbe interactions
    Julia D. Meredith, Michael J. Gray
    Molecular Microbiology.2023; 119(3): 302.     CrossRef
  • TMT-based proteomics analysis of growth advantage of triploid Apostichopus japonicus
    Jiahui Xie, Yi Sun, Yuanxin Li, Xianglei Zhang, Pengfei Hao, Lingshu Han, Yue Cao, Beichen Ding, Yaqing Chang, Donghong Yin, Jun Ding
    Comparative Biochemistry and Physiology Part D: Genomics and Proteomics.2023; 45: 101043.     CrossRef
  • Expression Profiling along the Murine Intestine: Different Mucosal Protection Systems and Alterations in Tff1-Deficient Animals
    Franz Salm, Eva B. Znalesniak, Aikaterini Laskou, Sönke Harder, Hartmut Schlüter, Werner Hoffmann
    International Journal of Molecular Sciences.2023; 24(16): 12684.     CrossRef
  • SpNox regulates the homeostasis in the hemolymph and gut of mud crab (Scylla paramamosain) by generating ROS
    Ming Zhang, Ngoc Tuan Tran, Yongsheng Zhang, Qiuhua Yang, Yong Tang, Yueling Zhang, Shengkang Li
    Aquaculture.2023; 575: 739760.     CrossRef
  • Iodine contrast exposure and incident COVID-19 infection
    Karen Tsai, Kosuke Inoue, Michael McClean, Jonathan D. Kaunitz, Yasutada Akiba, Martin L. Lee, Natalia V. Neverova, Jesse W. Currier, Ramin Ebrahimi, Muhammad T. Bashir, Angela M. Leung
    Frontiers in Medicine.2022;[Epub]     CrossRef
  • Structural evidence of the oxidation of iodide ion into hyper‐reactive hypoiodite ion by mammalian heme lactoperoxidase
    Prashant K. Singh, Nayeem Ahmad, Shavait Yamini, Rashmi P. Singh, Amit K. Singh, Pradeep Sharma, Michael L. Smith, Sujata Sharma, Tej P. Singh
    Protein Science.2022; 31(2): 384.     CrossRef
  • IFN-induced cell-autonomous immune mechanisms in the control of intracellular protozoa
    Sini Skariah, Ali A. Sultan, Dana G. Mordue
    Parasitology Research.2022; 121(6): 1559.     CrossRef
  • Epithelial chemerin–CMKLR1 signaling restricts microbiota-driven colonic neutrophilia and tumorigenesis by up-regulating lactoperoxidase
    Yuli Lin, Qian Cai, Yaxin Luo, Bingji Li, Yu Chen, Xuguang Yang, Yan Xuan, Huifan Yang, Rui He
    Proceedings of the National Academy of Sciences.2022;[Epub]     CrossRef
  • Redox-Mediated Inactivation of the Transcriptional Repressor RcrR is Responsible for Uropathogenic Escherichia coli’s Increased Resistance to Reactive Chlorine Species
    Sadia Sultana, Mary E. Crompton, Kennadi Meurer, Olivia Jankiewicz, Grace H. Morales, Colton Johnson, Elise Horbach, Kevin Pierre Hoffmann, Pooja Kr, Ritika Shah, Greg M. Anderson, Nathan T. Mortimer, Jonathan E. Schmitz, Maria Hadjifrangiskou, Alessandro
    mBio.2022;[Epub]     CrossRef
  • Cannabinoid control of gingival immune activation in chronically SIV-infected rhesus macaques involves modulation of the indoleamine-2,3-dioxygenase-1 pathway and salivary microbiome
    Marina McDew-White, Eunhee Lee, Xavier Alvarez, Karol Sestak, Binhua J Ling, Siddappa N Byrareddy, Chioma M Okeoma, Mahesh Mohan
    eBioMedicine.2022; 75: 103769.     CrossRef
  • Antimicrobial Activity of Films and Coatings Containing Lactoperoxidase System: A Review
    Mojtaba Yousefi, Amene Nematollahi, Mahdi Shadnoush, Amir M. Mortazavian, Nasim Khorshidian
    Frontiers in Nutrition.2022;[Epub]     CrossRef
  • Functional edible films/coatings integrated with lactoperoxidase and lysozyme and their application in food preservation
    Wanli Zhang, Jong-Whan Rhim
    Food Control.2022; 133: 108670.     CrossRef
  • Transcriptomic Analysis of Genes Associated with Oxidative Stress in Chronic Rhinosinusitis Patients with Nasal Polyps: Identifying Novel Genes Involved in Nasal Polyposis
    Yih-Jeng Tsai, Yu-Ting Hsu, Ming-Chieh Ma, Chun-Kuang Wu, Sheng-Dean Luo, Wen-Bin Wu
    Antioxidants.2022; 11(10): 1899.     CrossRef
  • Intrathyroidal feedforward and feedback network regulating thyroid hormone synthesis and secretion
    Li Jing, Qiang Zhang
    Frontiers in Endocrinology.2022;[Epub]     CrossRef
  • Exopolyphosphatases PPX1 and PPX2 from Mycobacterium tuberculosis regulate dormancy response and pathogenesis
    Prabhakar Tiwari, Tannu Priya Gosain, Saurabh Chugh, Mamta Singh, Gaurav D. Sankhe, Garima Arora, Saqib Kidwai, Sakshi Agarwal, Deepak K. Saini, Ramandeep Singh
    Microbial Pathogenesis.2022; 173: 105885.     CrossRef
  • The Pseudomonas aeruginosa DksA1 protein is involved in H2O2 tolerance and within-macrophages survival and can be replaced by DksA2
    Alessandra Fortuna, Diletta Collalto, Veronica Schiaffi, Valentina Pastore, Paolo Visca, Fiorentina Ascenzioni, Giordano Rampioni, Livia Leoni
    Scientific Reports.2022;[Epub]     CrossRef
  • Atmospheric Reactive Oxygen Species and Some Aspects of the Antiviral Protection at the Respiratory Epithelium
    V. V. Salmin, A. V. Morgun, R. Ya. Olovyannikova, V. A. Kutyakov, E. V. Lychkovskaya, E. B. Brusina, A. B. Salmina
    Biochemistry (Moscow), Supplement Series B: Biomedical Chemistry.2022; 16(2): 79.     CrossRef
  • The Hypothiocyanite and Amantadine Combination Treatment Prevents Lethal Influenza A Virus Infection in Mice
    Nuha Milad Ashtiwi, Demba Sarr, Tamás Nagy, Z. Beau Reneer, Ralph A. Tripp, Balázs Rada
    Frontiers in Immunology.2022;[Epub]     CrossRef
  • Electric Field Induced Biomimetic Transmembrane Electron Transport Using Carbon Nanotube Porins
    Jacqueline M. Hicks, Yun‐Chiao Yao, Sydney Barber, Nigel Neate, Julie A. Watts, Aleksandr Noy, Frankie J. Rawson
    Small.2021;[Epub]     CrossRef
  • DUOX1 in mammalian disease pathophysiology
    Nuha Milad Ashtiwi, Demba Sarr, Balázs Rada
    Journal of Molecular Medicine.2021; 99(6): 743.     CrossRef
  • Stimulation of Toll-Like Receptor 3 Diminishes Intracellular Growth of Salmonella Typhimurium by Enhancing Autophagy in Murine Macrophages
    Hyo-Ji Lee, Sun-Hye Lee, Ji-Hui Jeon, Hyo-Jung Kim, Eui-Kwon Jeong, Min-Jeong Kim, Young Mee Jung, Yu-Jin Jung
    Metabolites.2021; 11(9): 602.     CrossRef
  • Atmospheric reactive oxygen species and some aspects of the antiviral protection of the respiratory epithelium
    V.V. Salmin, A.V. Morgun, R.Ya. Olovyannikova, V.A. Kutyakov, E.V. Lychkovskaya, E.B. Brusina, A.B. Salmina
    Biomeditsinskaya Khimiya.2021; 67(5): 383.     CrossRef
  • Dual oxidase 1 promotes antiviral innate immunity
    Demba Sarr, Aaron D. Gingerich, Nuha Milad Asthiwi, Faris Almutairi, Giuseppe A. Sautto, Jeffrey Ecker, Tamás Nagy, Matthew B. Kilgore, Joshua D. Chandler, Ted M. Ross, Ralph A. Tripp, Balázs Rada
    Proceedings of the National Academy of Sciences.2021;[Epub]     CrossRef
  • Reactive Oxygen Species-Related Ceftazidime Resistance Is Caused by the Pyruvate Cycle Perturbation and Reverted by Fe3 + in Edwardsiella tarda
    Jinzhou Ye, Yubin Su, Xuanxian Peng, Hui Li
    Frontiers in Microbiology.2021;[Epub]     CrossRef
  • Milk-derived anti-infectives and their potential to combat bacterial and viral infection
    Sinead T. Morrin, Rachael H. Buck, Michael Farrow, Rita M. Hickey
    Journal of Functional Foods.2021; 81: 104442.     CrossRef
  • Di-Tyrosine Crosslinking and NOX4 Expression as Oxidative Pathological Markers in the Lungs of Patients with Idiopathic Pulmonary Fibrosis
    Sanja Blaskovic, Yves Donati, Isabelle Ruchonnet-Metrailler, Tamara Seredenina, Karl-Heinz Krause, Jean-Claude Pache, Dan Adler, Constance Barazzone-Argiroffo, Vincent Jaquet
    Antioxidants.2021; 10(11): 1833.     CrossRef
  • Distinctive Under-Expression Profile of Inflammatory and Redox Genes in the Blood of Elderly Patients with Cardiovascular Disease
    Elena Milanesi, Gina Manda, Maria Dobre, Elena Codrici, Ionela V Neagoe, Bogdan O Popescu, Ovidiu Alexandru Bajenaru, Luiza Spiru, Catalina Tudose, Gabriel I Prada, Eugenia I Davidescu, Gerard Piñol-Ripoll, Antonio Cuadrado
    Journal of Inflammation Research.2021; Volume 14: 429.     CrossRef
  • Proteomic analysis of the host–pathogen interface in experimental cholera
    Abdelrahim Zoued, Hailong Zhang, Ting Zhang, Rachel T. Giorgio, Carole J. Kuehl, Bolutife Fakoya, Brandon Sit, Matthew K. Waldor
    Nature Chemical Biology.2021; 17(11): 1199.     CrossRef
  • Raising the ‘Good’ Oxidants for Immune Protection
    Alexia Dumas, Ulla G. Knaus
    Frontiers in Immunology.2021;[Epub]     CrossRef
  • Microbicidal Activity of Hypothiocyanite against Pneumococcus
    Edriss Yassine, Balázs Rada
    Antibiotics.2021; 10(11): 1313.     CrossRef
  • Lactoperoxidase system in the dairy industry: Challenges and opportunities
    Emmanuelle Silva, Juliana Oliveira, Yhelda Silva, Stela Urbano, Danielle Sales, Edgar Moraes, Adriano Rangel, Katya Anaya
    Czech Journal of Food Sciences.2020; 38(6): 337.     CrossRef
  • Oxidative killing of encapsulated and nonencapsulated Streptococcus pneumoniae by lactoperoxidase-generated hypothiocyanite
    Aaron D. Gingerich, Fayhaa Doja, Rachel Thomason, Eszter Tóth, Jessica L. Bradshaw, Martin V. Douglass, Larry S. McDaniel, Balázs Rada, Mariola J. Edelmann
    PLOS ONE.2020; 15(7): e0236389.     CrossRef
  • Antimicrobials offered from nature: Peroxidase-catalyzed systems and their mimics
    Lilit Tonoyan, Diego Montagner, Ruairi Friel, Vincent O'Flaherty
    Biochemical Pharmacology.2020; 182: 114281.     CrossRef
  • Mini review: immunologic functions of dual oxidases in mucosal systems of vertebrates
    H. T. Yang, Y. H. Huang, G. W. Yang
    Brazilian Journal of Biology.2020; 80(4): 948.     CrossRef
  • Airway Redox Homeostasis and Inflammation Gone Awry: From Molecular Pathogenesis to Emerging Therapeutics in Respiratory Pathology
    Javier Checa, Josep M. Aran
    International Journal of Molecular Sciences.2020; 21(23): 9317.     CrossRef
  • Microbial Safety of Milk Production and Fermented Dairy Products in Africa
    James Owusu-Kwarteng, Fortune Akabanda, Dominic Agyei, Lene Jespersen
    Microorganisms.2020; 8(5): 752.     CrossRef
  • Innate and adaptive immune responses in respiratory virus infection: implications for the clinic
    John Stambas, Chunni Lu, Ralph A Tripp
    Expert Review of Respiratory Medicine.2020; 14(11): 1141.     CrossRef
  • Investigation of Potential Genetic Biomarkers and Molecular Mechanism of Ulcerative Colitis Utilizing Bioinformatics Analysis
    Jiaqi Zhang, Xue Wang, Lin Xu, Zedan Zhang, Fengyun Wang, Xudong Tang
    BioMed Research International.2020; 2020: 1.     CrossRef
  • Mechanistic insight into heterogeneity of trans-plasma membrane electron transport in cancer cell types
    Harry G. Sherman, Carolyn Jovanovic, Alaa Abuawad, Dong-Hyun Kim, Hilary Collins, James E. Dixon, Robert Cavanagh, Robert Markus, Snow Stolnik, Frankie J. Rawson
    Biochimica et Biophysica Acta (BBA) - Bioenergetics.2019; 1860(8): 628.     CrossRef
  • Human myeloperoxidase (hMPO) is expressed in neurons in the substantia nigra in Parkinson's disease and in the hMPO-α-synuclein-A53T mouse model, correlating with increased nitration and aggregation of α-synuclein and exacerbation of motor impairment
    Richard A. Maki, Michael Holzer, Khatereh Motamedchaboki, Ernst Malle, Eliezer Masliah, Gunther Marsche, Wanda F. Reynolds
    Free Radical Biology and Medicine.2019; 141: 115.     CrossRef
  • The Role of Iron Regulation in Immunometabolism and Immune-Related Disease
    Shane J. F. Cronin, Clifford J. Woolf, Guenter Weiss, Josef M. Penninger
    Frontiers in Molecular Biosciences.2019;[Epub]     CrossRef
  • The Functional Power of the Human Milk Proteome
    Jing Zhu, Kelly A. Dingess
    Nutrients.2019; 11(8): 1834.     CrossRef
  • Peroxidase Activity of Human Hemoproteins: Keeping the Fire under Control
    Irina I. Vlasova
    Molecules.2018; 23(10): 2561.     CrossRef
Journal Article
The NADPH oxidase AoNoxA in Arthrobotrys oligospora functions as an initial factor in the infection of Caenorhabditis elegans
Xin Li , Ying-Qian Kang , Yan-Lu Luo , Ke-Qin Zhang , Cheng-Gang Zou , Lian-Ming Liang
J. Microbiol. 2017;55(11):885-891.   Published online October 27, 2017
DOI: https://doi.org/10.1007/s12275-017-7169-x
  • 45 View
  • 0 Download
  • 15 Crossref
AbstractAbstract
Reactive oxygen species (ROS) produced by NADPH oxidases can serve as signaling molecules to regulate a variety of physiological processes in multi-cellular organisms. In the nematophagous fungus Arthrobotrys oligospora, we found that ROS were produced during conidial germination, hyphal extension, and trap formation in the presence of nematodes. Generation of an AoNoxA knockout strain demonstrated the crucial role of NADPH oxidase in the production of ROS in A. oligospora, with trap formation impaired in the AoNoxA mutant, even in the presence of the nematode host. In addition, the expression of virulence factor serine protease P186 was up-regulated in the wild-type strain, but not in the mutant strain, in the presence of Caenorhabditis elegans. These results indicate that ROS derived from AoNoxA are essential for full virulence of A. oligospora in nematodes.

Citations

Citations to this article as recorded by  
  • AoPrdx2 Regulates Oxidative Stress, Reactive Oxygen Species, Trap Formation, and Secondary Metabolism in Arthrobotrys oligospora
    Na Zhao, Meichen Zhu, Qianqian Liu, Yanmei Shen, Shipeng Duan, Lirong Zhu, Jinkui Yang
    Journal of Fungi.2024; 10(2): 110.     CrossRef
  • Tools and basic procedures of gene manipulation in nematode-trapping fungi
    Shunxian Wang, Xingzhong Liu
    Mycology.2023; 14(2): 75.     CrossRef
  • Caenorhabditis elegansLIN‐24, a homolog of bacterial pore‐forming toxin, protects the host from microbial infection
    Huijie Zhang, Weirong Zeng, Ming‐Ming Zhao, Jiali Wang, Qiquan Wang, Ting Chen, Yuyan Zhang, Wenhui Lee, Shenghan Chen, Yun Zhang, Xinqiang Lan, Yang Xiang
    The FASEB Journal.2023;[Epub]     CrossRef
  • Key processes required for the different stages of fungal carnivory by a nematode-trapping fungus
    Hung-Che Lin, Guillermo Vidal-Diez de Ulzurrun, Sheng-An Chen, Ching-Ting Yang, Rebecca J. Tay, Tomoyo Iizuka, Tsung-Yu Huang, Chih-Yen Kuo, A. Pedro Gonçalves, Siou-Ying Lin, Yu-Chu Chang, Jason E. Stajich, Erich M. Schwarz, Yen-Ping Hsueh, Aaron P. Mitc
    PLOS Biology.2023; 21(11): e3002400.     CrossRef
  • Recent Advances in Life History Transition with Nematode-Trapping Fungus Arthrobotrys oligospora and Its Application in Sustainable Agriculture
    Da Wang, Nan Ma, Wanqin Rao, Ying Zhang
    Pathogens.2023; 12(3): 367.     CrossRef
  • Aolatg1 and Aolatg13 Regulate Autophagy and Play Different Roles in Conidiation, Trap Formation, and Pathogenicity in the Nematode-Trapping Fungus Arthrobotrys oligospora
    Duanxu Zhou, Yingmei Zhu, Na Bai, Meihua Xie, Ke-Qin Zhang, Jinkui Yang
    Frontiers in Cellular and Infection Microbiology.2022;[Epub]     CrossRef
  • Regulatory Mechanism of Trap Formation in the Nematode-Trapping Fungi
    Mei-Chen Zhu, Xue-Mei Li, Na Zhao, Le Yang, Ke-Qin Zhang, Jin-Kui Yang
    Journal of Fungi.2022; 8(4): 406.     CrossRef
  • Transcriptomic Analysis Reveals That Rho GTPases Regulate Trap Development and Lifestyle Transition of the Nematode-Trapping Fungus Arthrobotrys oligospora
    Le Yang, Xuemei Li, Na Bai, Xuewei Yang, Ke-Qin Zhang, Jinkui Yang, Christina A. Cuomo
    Microbiology Spectrum.2022;[Epub]     CrossRef
  • Prey sensing and response in a nematode-trapping fungus is governed by the MAPK pheromone response pathway
    Sheng-An Chen, Hung-Che Lin, Frank C Schroeder, Yen-Ping Hsueh, A Gladfelter
    Genetics.2021;[Epub]     CrossRef
  • Forward genetic screens identified mutants with defects in trap morphogenesis in the nematode-trapping fungus Arthrobotrys oligospora
    Tsung-Yu Huang, Yi-Yun Lee, Guillermo Vidal-Diez de Ulzurrun, Yen-Ping Hsueh, J Dunlap
    G3 Genes|Genomes|Genetics.2021;[Epub]     CrossRef
  • The NADPH Oxidase A of Verticillium dahliae Is Essential for Pathogenicity, Normal Development, and Stress Tolerance, and It Interacts with Yap1 to Regulate Redox Homeostasis
    Vasileios Vangalis, Ioannis A. Papaioannou, Emmanouil A. Markakis, Michael Knop, Milton A. Typas
    Journal of Fungi.2021; 7(9): 740.     CrossRef
  • DdaSTE12 is involved in trap formation, ring inflation, conidiation, and vegetative growth in the nematode-trapping fungus Drechslerella dactyloides
    Yani Fan, Weiwei Zhang, Yue Chen, Meichun Xiang, Xingzhong Liu
    Applied Microbiology and Biotechnology.2021; 105(19): 7379.     CrossRef
  • Azaphilones biosynthesis complements the defence mechanism of Trichoderma guizhouense against oxidative stress
    Guan Pang, Tingting Sun, Zhenzhong Yu, Tao Yuan, Wei Liu, Hong Zhu, Qi Gao, Dongqing Yang, Christian P. Kubicek, Jian Zhang, Qirong Shen
    Environmental Microbiology.2020; 22(11): 4808.     CrossRef
  • Natural diversity in the predatory behavior facilitates the establishment of a robust model strain for nematode-trapping fungi
    Ching-Ting Yang, Guillermo Vidal-Diez de Ulzurrun, A. Pedro Gonçalves, Hung-Che Lin, Ching-Wen Chang, Tsung-Yu Huang, Sheng-An Chen, Cheng-Kuo Lai, Isheng J. Tsai, Frank C. Schroeder, Jason E. Stajich, Yen-Ping Hsueh
    Proceedings of the National Academy of Sciences.2020; 117(12): 6762.     CrossRef
  • Guttation capsules containing hydrogen peroxide: an evolutionarily conserved NADPH oxidase gains a role in wars between related fungi
    Jian Zhang, Youzhi Miao, Mohammad Javad Rahimi, Hong Zhu, Andrei Steindorff, Sabine Schiessler, Feng Cai, Guan Pang, Komal Chenthamara, Yu Xu, Christian P. Kubicek, Qirong Shen, Irina S. Druzhinina
    Environmental Microbiology.2019; 21(8): 2644.     CrossRef
Research Support, Non-U.S. Gov'ts
Biochemical Properties and Physiological Roles of NADP-Dependent Malic Enzyme in Escherichia coli
Baojuan Wang , Peng Wang , Enxia Zheng , Xiangxian Chen , Hanjun Zhao , Ping Song , Ruirui Su , Xiaoning Li , Guoping Zhu
J. Microbiol. 2011;49(5):797-802.   Published online November 9, 2011
DOI: https://doi.org/10.1007/s12275-011-0487-5
  • 43 View
  • 0 Download
  • 21 Crossref
AbstractAbstract
Malic enzymes catalyze the reversible oxidative decarboxylation of L-malate using NAD(P)+ as a cofactor. NADP-dependent malic enzyme (MaeB) from Escherichia coli MG1655 was expressed and purified as a fusion protein. The molecular weight of MaeB was about 83 kDa, as determined by SDS-PAGE. The recombinant MaeB showed a maximum activity at pH 7.8 and 46°C. MaeB activity was dependent on the presence of Mn2+ but was strongly inhibited by Zn2+. In order to understand the physiological roles, recombinant E. coli strains (icdNADP/ΔmaeB and icdNAD/ΔmaeB) containing NADP-dependent isocitrate dehydrogenase (IDH), or engineered NAD-dependent IDH with the deletion of the maeB gene, were constructed using homologous recombination. During growth on acetate, icdNAD/ΔmaeB grew poorly, having a growth rate only 60% that of the wild-type strain (icdNADP). Furthermore, icdNADP/ΔmaeB exhibited a 2-fold greater adaptability to acetate than icdNAD/ΔmaeB, which may be explained by more NADPH production for biosynthesis in icdNADP/ΔmaeB due to its NADP-dependent IDH. These results indicated that MaeB was important for NADPH production for bacterial growth on acetate. We also observed that MaeB activity was significantly enhanced (7.83-fold) in icdNAD, which was about 3-fold higher than that in icdNADP, when switching from glucose to acetate. The marked increase of MaeB activity was probably induced by the shortage of NADPH in icdNAD. Evidently, MaeB contributed to the NADPH generation needed for bacterial growth on two carbon compounds.

Citations

Citations to this article as recorded by  
  • TA-Cloning for Diabetes Treatment: Expressing Corynebacterium Malic Enzyme Gene in E. coli
    Somayeh Farahmand, Saber SamadiAfshar, Ladan Hosseini
    Current Microbiology.2024;[Epub]     CrossRef
  • Recent advances, challenges and metabolic engineering strategies in the biosynthesis of 3‐hydroxypropionic acid
    Bo Liang, Guannan Sun, Xinping Zhang, Qingjuan Nie, Yukun Zhao, Jianming Yang
    Biotechnology and Bioengineering.2022; 119(10): 2639.     CrossRef
  • Metabolic engineering of Halomonas elongata: Ectoine secretion is increased by demand and supply driven approaches
    Karina Hobmeier, Martin Oppermann, Natalie Stasinski, Andreas Kremling, Katharina Pflüger-Grau, Hans Jörg Kunte, Alberto Marin-Sanguino
    Frontiers in Microbiology.2022;[Epub]     CrossRef
  • Improved production of 2′-fucosyllactose in engineered Saccharomyces cerevisiae expressing a putative α-1, 2-fucosyltransferase from Bacillus cereus
    Mingyuan Xu, Xiangfeng Meng, Weixin Zhang, Yu Shen, Weifeng Liu
    Microbial Cell Factories.2021;[Epub]     CrossRef
  • One stone two birds: Biosynthesis of 3-hydroxypropionic acid from CO2 and syngas-derived acetic acid in Escherichia coli
    Ningyu Lai, Yuanchan Luo, Peng Fei, Peng Hu, Hui Wu
    Synthetic and Systems Biotechnology.2021; 6(3): 144.     CrossRef
  • Transcriptomics and Methylomics Study on the Effect of Iodine-Containing Drug FS-1 on Escherichia Coli ATCC BAA-196
    Ilya S Korotetskiy, Ardak B Jumagaziyeva, Sergey V Shilov, Tatyana V Kuznetsova, Auyes N Myrzabayeva, Zhanar A Iskakbayeva, Aleksandr I Ilin, Monique Joubert, Setshaba Taukobong, Oleg N Reva
    Future Microbiology.2021; 16(14): 1063.     CrossRef
  • Enzymatic characterization of blood lymphocytes in various clinical and pathogenetic variants of respiratory allergy
    A. M. Lazareva, O. A. Kolenchukova, S. V. Smirnova
    Medical Immunology (Russia).2021; 23(1): 107.     CrossRef
  • The Protein-Protein Interaction Network Reveals a Novel Role of the Signal Transduction Protein PII in the Control of c-di-GMP Homeostasis in Azospirillum brasilense
    Edileusa C. M. Gerhardt, Erick Parize, Fernanda Gravina, Flávia L. D. Pontes, Adrian R. S. Santos, Gillize A. T. Araújo, Ana C. Goedert, Alysson H. Urbanski, Maria B. R. Steffens, Leda S. Chubatsu, Fabio O. Pedrosa, Emanuel M. Souza, Karl Forchhammer, Ele
    mSystems.2020;[Epub]     CrossRef
  • Metabolic changes in peripheral blood lymphocytes from children with recurrent respiratory infections
    L. M. Kurtasova, N. A. Shakina, T. V. Lubnina
    Russian Journal of Infection and Immunity.2020; 10(3): 515.     CrossRef
  • The NADP-dependent malic enzyme MaeB is a central metabolic hub controlled by the acetyl-CoA to CoASH ratio
    Luciano F. Huergo, Gillize A.T. Araújo, Adrian S.R. Santos, Edileusa C.M. Gerhardt, Fabio O. Pedrosa, Emanuel M. Souza, Karl Forchhammer
    Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics.2020; 1868(9): 140462.     CrossRef
  • Rediscovering Acetate Metabolism: Its Potential Sources and Utilization for Biobased Transformation into Value-Added Chemicals
    Hyun Gyu Lim, Ji Hoon Lee, Myung Hyun Noh, Gyoo Yeol Jung
    Journal of Agricultural and Food Chemistry.2018; 66(16): 3998.     CrossRef
  • Enhanced performance of the methylerythritol phosphate pathway by manipulation of redox reactions relevant to IspC, IspG, and IspH
    Jia Zhou, Liyang Yang, Chonglong Wang, Eui-Sung Choi, Seon-Won Kim
    Journal of Biotechnology.2017; 248: 1.     CrossRef
  • Rational design of a synthetic Entner–Doudoroff pathway for improved and controllable NADPH regeneration
    Chiam Yu Ng, Iman Farasat, Costas D. Maranas, Howard M. Salis
    Metabolic Engineering.2015; 29: 86.     CrossRef
  • Metabolic network capacity of Escherichia coli for Krebs cycle-dependent proline hydroxylation
    Eleni Theodosiou, Oliver Frick, Bruno Bühler, Andreas Schmid
    Microbial Cell Factories.2015;[Epub]     CrossRef
  • NADPH-generating systems in bacteria and archaea
    Sebastiaan K. Spaans, Ruud A. Weusthuis, John van der Oost, Servé W. M. Kengen
    Frontiers in Microbiology.2015;[Epub]     CrossRef
  • Central metabolic responses to the overproduction of fatty acids in Escherichia coli based on 13C‐metabolic flux analysis
    Lian He, Yi Xiao, Nikodimos Gebreselassie, Fuzhong Zhang, Maciek R. Antoniewicz, Yinjie J. Tang, Lifeng Peng
    Biotechnology and Bioengineering.2014; 111(3): 575.     CrossRef
  • Optimal cofactor swapping can increase the theoretical yield for chemical production in Escherichia coli and Saccharomyces cerevisiae
    Zachary A. King, Adam M. Feist
    Metabolic Engineering.2014; 24: 117.     CrossRef
  • Engineering of NADPH regenerators in Escherichia coli for enhanced biotransformation
    Won-Heong Lee, Myoung-Dong Kim, Yong-Su Jin, Jin-Ho Seo
    Applied Microbiology and Biotechnology.2013; 97(7): 2761.     CrossRef
  • Expression characteristics of the maeA and maeB genes by extracellular malate and pyruvate in Escherichia coli
    Irisappan Ganesh, Sambandam Ravikumar, Si Jae Park, Seung Hwan Lee, Soon Ho Hong
    Korean Journal of Chemical Engineering.2013; 30(7): 1443.     CrossRef
  • Optimizing Cofactor Specificity of Oxidoreductase Enzymes for the Generation of Microbial Production Strains—OptSwap
    Zachary A. King, Adam M. Feist
    Industrial Biotechnology.2013; 9(4): 236.     CrossRef
  • Investigating the effects of perturbations to pgi and eno gene expression on central carbon metabolism in Escherichia coli using 13 C metabolic flux analysis
    Yuki Usui, Takashi Hirasawa, Chikara Furusawa, Tomokazu Shirai, Natsuko Yamamoto, Hirotada Mori, Hiroshi Shimizu
    Microbial Cell Factories.2012;[Epub]     CrossRef
Characterization of Deinococcus radiophilus Thioredoxin Reductase Active with Both NADH and NADPH
Hee-Jeong Seo , Young Nam Lee
J. Microbiol. 2010;48(5):637-643.   Published online November 3, 2010
DOI: https://doi.org/10.1007/s12275-010-0283-7
  • 36 View
  • 0 Download
  • 4 Scopus
AbstractAbstract
Thioredoxin reductase (TrxR, EC 1.6.4.5) of Deinococcus radiophilus was purified by steps of sonication, ammonium sulfate fractionation, 2'5' ADP Sepharose 4B affinity chromatography, and Sephadex G-100 gel filtration. The purified TrxR, which was active with both NADPH and NADH, gave a 368 U/mg protein of specific activity with 478-fold purification and 18% recovery from the cell-free extract. An isoelectric point of the purified enzymes was ca. 4.5. The molecular weights of the purified TrxR estimated by PAGE and gel filtration were about 63.1 and 72.2 kDa, respectively. The molecular mass of a TrxR subunit is 37 kDa. This suggests that TrxR definitely belongs to low molecular weight TrxR (L-TrxR). The Km and Vmax of TrxR for NADPH are 12.5 μM and 25 μM/min, whereas those for NADH are 30.2 μM and 192 μ M/min. The Km and Vmax for 5, 5'-dithio-bis-2-nitrobenzoic acid (DTNB, a substituted substrate for thioredoxin) are 463 μM and 756 μM/min, respectively. The presence of FAD in TrxR was confirmed with the absorbance peaks at 385 and 460 nm. The purified TrxR was quite stable from pH 3 to 9, and was thermo-stable up to 70°C. TrxR activity was drastically reduced (ca. 70%) by Cu2+, Zn2+, Hg2+, and Cd2+, but moderately reduced (ca. 50%) by Ag+. A significant inhibition of TrxR by N ethylmaleimide suggests an occurrence of cysteine at its active sites. Amino acid sequences at the N-terminus of purified TrxR are H2N-Ser-Glu-Gln-Ala-Gln-Met-Tyr-Asp-Val-Ile-Ile-Val-Gly-Gly-Gly-Pro-Ala-Gly-Leu-Thr-Ala-COOH. These sequences show high similarity with TrxRs reported in Archaea, such as Methanosarcina mazei, Archaeoglobus fulgidus etc.
NtrC-Sensed Nitrogen Availability Is Important for Oxidative Stress Defense in Pseudomonas putida KT2440
Sujin Yeom , Jinki Yeom , Woojun Park
J. Microbiol. 2010;48(2):153-159.   Published online May 1, 2010
DOI: https://doi.org/10.1007/s12275-010-0075-0
  • 35 View
  • 0 Download
  • 15 Scopus
AbstractAbstract
The zwf, which encodes glucose-6-phosphate dehydrogenase, is repressed by NtrC under nitrogen-limited condition. Previously, we demonstrated that induction of zwf-1 is required for protecting Pseudomonas putida cells under oxidative stress, which could be possible probably because of derepression of HexR on the zwf-1 gene under oxidative stress. These findings led us investigate that NtrC still represses the zwf-1 under nitrogen-limited oxidative stress condition, which makes cells more sensitive under such condition. Interestingly, deletion of the ntrC gene significantly reduces growth rate, but renders cells more resistant to oxidative stress, under nitrogen limited condition in P. putida. More vitality of the ntrC mutant under oxidative stress condition was also confirmed by the fluorogenic redox dye using flow cytometry. The results of transcriptome analysis demonstrated that the derepression of several oxidative stress genes along with the zwf-1 gene might confer high resistance to oxidative stress in the ntrC mutant. Here, we presented the data for the first time, showing that different sets of genes are involved in nitrogen-rich and nitrogen-limited oxidative stress conditions and NtrC-sensed nitrogen availability is one of the most important prerequisite for full cellular defense against oxidative stress in P. putida.
Occurrence of Thioredoxin Reductase in Deinococcus Species, the UV resistant Bacteria
Hee Jeong Seo , Young Nam Lee
J. Microbiol. 2006;44(4):461-465.
DOI: https://doi.org/2404 [pii]
  • 35 View
  • 0 Download
AbstractAbstract
The occurrence of thioredoxin reductase (NAD(P)H: oxidized-thioredoxin reductase, EC 1.6.4.5, TrxR) in five mesophilic species of Deinococcus was investigated by PAGE. Each species possessed a unique TrxR pattern, for example, a single TrxR characterized D. radiopugnans while multiple forms of TrxR occurred in other Deinococcal spp. Most of TrxRs occurring in Deinococcus showed dual cofactor specificity, active with either NADH or NADPH, although the NADPH specific-TrxR was observed in D. radiophilus and D.proteolyticus.
Regulation of fpr Gene encoding NADPH :Ferredoxin oxidoreductase by the soxRS locus in escherichia coli
Koh, Young Sang , Chouh, Jenny , Roe, Jung Hye
J. Microbiol. 1996;34(2):137-143.
  • 32 View
  • 0 Download
AbstractAbstract
We isolated a promoter inducible by paraquat, a superoxide-generating agent, from Escherichia coli using a promoter-probing plasmid pRS415. From sequence analysis we found out the promoter is for fpr ENCODING nadph : ferredoxin oxidoreductase. We constructed on operon fusion of lacZ gene with fpr promoter to monitor the expression of the gene in the single-copy state. LacZ expression generators, menadione and plumbagin, also induced the expression of β-galactosidase in the fusion strain. On the other hand, no significant induction was observed by treatment with hydrogen peroxide, ethanol, and heat shock. Induction of β-galactosidase was significantly reduced by introducing a Δsox 8 :: cat of soxS3 :: Tn10 mutation into the fusion strain, indicating that fpr gene is a member of the soxRS regulon. The transcriptional start site was determined by primer extension analysis. Possible roles of fpr induction in superoxide stress were discussed.

Journal of Microbiology : Journal of Microbiology
TOP