29Th Steenbock Symposium at the UW-Madison Biochemistry Department
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Kohen Curriculum Vitae
Curriculum Vitae Amnon Kohen Department of Chemistry Tel: (319) 335-0234 University of Iowa FAX: (319) 335-1270 Iowa City, IA 52242 [email protected] EDUCATION AND PROFESSIONAL HISTORY Education D.Sc., Chemistry 1989-1994 Technion – Israel Institute of Technology, Haifa, Israel Advisor: Professor T. Baasov Topic: Mechanistic Studies of the Enzyme KDO8P Synthase B.Sc., Chemistry (with Honors) 1986-1989 Hebrew University, Jerusalem, Israel Positions Professor 2010-Present Department of Chemistry, University of Iowa, Iowa City, IA and Molecular and Cellular Biology Program, and MSTP faculty member Associate Professor 2005-2010 Department of Chemistry, University of Iowa, Iowa City, IA and Molecular and Cellular Biology Program Assistant Professor 1999-2005 Department of Chemistry, University of Iowa, Iowa City, IA Postgraduate Researcher 1997-1999 With Professor Judith Klinman Department of Chemistry, University of California, Berkeley Topic: Hydrogen Tunneling in Biology: Alcohol Dehydrogenases Postgraduate Fellow 1995-1997 With Professor Judith Klinman Department of Chemistry, University of California, Berkeley Topic: Hydrogen Tunneling in Biology: Glucose Oxidase Visiting Scholar Fall 1994 With Professor Karen S. Anderson Department of Pharmacology, Yale Medical School, New Haven, CT Kohen, A. Affiliations American Society for Biochemistry and Molecular Biology (ASBMB, 2013 - present) Center for Biocatalysis and Bioprocessing (CBB) University of Iowa (2000-Present) The Interdisciplinary Graduate Program in Molecular Biology, University of Iowa (2003- Present) American Association for the Advancement of Science (AAAS, 2011-present) American Chemical Society (1995-Present) Divisions: Organic Chemistry, Physical Chemistry, Biochemistry Sigma Xi (1997-Present) Protein Society (1996-1998) Honors and Awards • Career Development Award (University of Iowa- 2015-2016) • Graduate College Outstanding Faculty Mentor Award (2015). -
Proteomic Analysis of Mycelial Proteins from Magnaporthe Oryzae Under Nitrogen Starvation
Proteomic analysis of mycelial proteins from Magnaporthe oryzae under nitrogen starvation X.-G. Zhou1,2, P. Yu 2, C. Dong2, C.-X. Yao2, Y.-M. Ding2, N. Tao2 and Z.-W. Zhao1 1State Key Laboratory for Conservation and Utilization of Bio-Resources in Yunnan, Yunnan University, Kunming, China 2Key Laboratory of Southwestern Crop Gene Resources and Germplasm Innovation, Ministry of Agriculture and Yunnan Provincial Key Laboratory of Agricultural Biotechnology, Biotechnology and Germplasm Resources Institute, Yunnan Academy of Agricultural Sciences, Kunming, China Corresponding author: Z.W. Zhao E-mail: [email protected] Genet. Mol. Res. 15 (2): gmr.15028637 Received March 23, 2016 Accepted April 11, 2016 Published May 13, 2016 DOI http://dx.doi.org/10.4238/gmr.15028637 ABSTRACT. Magnaporthe oryzae is an important model system in studies of plant pathogenic fungi, and nitrogen is a key nutrient source affecting microbial growth and development. In order to understand how nitrogen stress causes changes in mycelial proteins, we analyzed differentially expressed mycelial proteins from the M. oryzae virulent strain CH-63 using two-dimensional electrophoresis and mass spectrometry in complete medium or under nitrogen starvation conditions. A total of 975 ± 70 and 1169 ± 90 protein spots were detected in complete medium and under nitrogen starvation conditions, respectively. Forty-nine protein spots exhibited at least 2-fold up- regulation or down-regulation at the protein level according to PDQuest7.4. Moreover, 43 protein spots were successfully identified by matrix-assisted laser desorption/ionization-time-of-flight/time-of-flight mass spectrometry. Among these spots, 6 proteins were functionally unknown and 37 proteins were categorized into 5 groups according to Genetics and Molecular Research 15 (2): gmr.15028637 ©FUNPEC-RP www.funpecrp.com.br X.-G. -
Cloning, Biochemical Characterization and Inhibition of Alanine Racemase from Streptococcus Iniae
bioRxiv preprint doi: https://doi.org/10.1101/611251; this version posted April 16, 2019. The copyright holder for this preprint (which was not certified by peer review) is the author/funder. All rights reserved. No reuse allowed without permission. Cloning, Biochemical Characterization and Inhibition of Alanine racemase from Streptococcus iniae Murtala Muhammad, Yangyang Li, Siyu Gong, Yanmin Shi, Jiansong Ju, Baohua Zhao*, Dong Liu* College of Life Science, Hebei Normal University, Shijiazhuang 050024, China; *Correspondence: Baohua Zhao and Dong Liu; E-mail: [email protected], [email protected]; College of Life Science, Hebei Normal University, Shijiazhuang 050024, China. Running Title: Inhibitors of alanine racemase Summary statement: Antimicrobial target 1 bioRxiv preprint doi: https://doi.org/10.1101/611251; this version posted April 16, 2019. The copyright holder for this preprint (which was not certified by peer review) is the author/funder. All rights reserved. No reuse allowed without permission. ABSTRACT Streptococcus iniae is a pathogenic and zoonotic bacteria that impacted high mortality to many fish species, as well as capable of causing serious disease to humans. Alanine racemase (Alr, EC 5.1.1.1) is a pyridoxal-5′-phosphate (PLP)-containing homodimeric enzyme that catalyzes the racemization of L-alanine and D-alanine. In this study, we purified alanine racemase from the pathogenic strain of S. iniae, determined its biochemical characteristics and inhibitors. The alr gene has an open reading frame (ORF) of 1107 bp, encoding a protein of 369 amino acids, which has a molecular mass of 40 kDa. The optimal enzyme activity occurred at 35°C and a pH of 9.5. -
Oxdc Antibody Rabbit Polyclonal Antibody Catalog # ABV11223
10320 Camino Santa Fe, Suite G San Diego, CA 92121 Tel: 858.875.1900 Fax: 858.622.0609 OxdC Antibody Rabbit Polyclonal Antibody Catalog # ABV11223 Specification OxdC Antibody - Product Information Application WB Primary Accession O34714 Reactivity Human Host Rabbit Clonality Polyclonal Isotype Rabbit IgG Calculated MW 43566 OxdC Antibody - Additional Information Gene ID 938620 Positive Control Western Blot: Recombinant protein Application & Usage Western blot: 1-4 Western blot of Oxalate decarboxylase µg/ml. antibody. Lane 1: rb- Oxalate decarboxylase - Other Names 10 ng. Lane 2: rb- Oxalate decarboxylase - 50 YvrK ng Target/Specificity OxdC OxdC Antibody - Background Antibody Form Oxalate decarboxylase (OxdC, EC4.1.1.2) is a Liquid manganese-containing enzyme, which decomposes oxalic acid and oxalate. With Appearance OxdC catalysis, oxalate is split into formate Colorless liquid and CO2. This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which Formulation 100 µg (0.5 mg/ml) of antibody in PBS pH cleave carbon-carbon bonds. The systematic 7.2 containing 0.01 % BSA, 0.01 % name of this enzyme class is oxalate thimerosal, and 50 % glycerol. carboxy-lyase (formate-forming). This enzyme is also called oxalate carboxy-lyase. The Handling enzyme is composed of two cupin domains, The antibody solution should be gently each of which contains a Mn (II) ion. This mixed before use. enzyme participates in glyoxylate and dicarboxylate metabolism. This enzyme has Reconstitution & Storage been recognized for diagnostics in diverse -20 °C biotechnological applications such as the clinical assay of oxalate in blood and urine, Background Descriptions therapeutics, process industry, and agriculture to lower oxalate levels in foods and the environment. -
Proteo-Metabolomic Investigation of Transgenic Rice Unravels Metabolic
www.nature.com/scientificreports OPEN Proteo-metabolomic investigation of transgenic rice unravels metabolic alterations and Received: 27 November 2018 Accepted: 24 June 2019 accumulation of novel proteins Published: xx xx xxxx potentially involved in defence against Rhizoctonia solani Subhasis Karmakar1, Karabi Datta1, Kutubuddin Ali Molla2,3, Dipak Gayen4, Kaushik Das1, Sailendra Nath Sarkar1 & Swapan K. Datta1 The generation of sheath blight (ShB)-resistant transgenic rice plants through the expression of Arabidopsis NPR1 gene is a signifcant development for research in the feld of biotic stress. However, to our knowledge, regulation of the proteomic and metabolic networks in the ShB-resistant transgenic rice plants has not been studied. In the present investigation, the relative proteome and metabolome profles of the non–transformed wild-type and the AtNPR1-transgenic rice lines prior to and subsequent to the R. solani infection were investigated. Total proteins from wild type and transgenic plants were investigated using two-dimensional gel electrophoresis (2-DE) followed by mass spectrometry (MS). The metabolomics study indicated an increased abundance of various metabolites, which draws parallels with the proteomic analysis. Furthermore, the proteome data was cross-examined using network analysis which identifed modules that were rich in known as well as novel immunity-related prognostic proteins, particularly the mitogen-activated protein kinase 6, probable protein phosphatase 2C1, probable trehalose-phosphate phosphatase 2 and heat shock protein. A novel protein, 14–3– 3GF14f was observed to be upregulated in the leaves of the transgenic rice plants after ShB infection, and the possible mechanistic role of this protein in ShB resistance may be investigated further. -
Effect of Pyrroloquinoline Quinone Disodium in Female Rats During
Downloaded from British Journal of Nutrition (2019), 121, 818–830 doi:10.1017/S0007114519000047 © The Authors 2019 https://www.cambridge.org/core Effect of pyrroloquinoline quinone disodium in female rats during gestating and lactating on reproductive performance and the intestinal barrier functions in the progeny . IP address: Boru Zhang, Wei Yang, Hongyun Zhang, Shiqi He, Qingwei Meng, Zhihui Chen and Anshan Shan* Institute of Animal Nutrition, Northeast Agricultural University, Harbin 150030, People’s Republic of China 170.106.202.226 (Submitted 26 September 2018 – Final revision received 21 December 2018 – Accepted 28 December 2018 – First published online 28 January 2019) , on Abstract 30 Sep 2021 at 19:42:41 The objective of this study was to investigate the effects of dietary pyrroloquinoline quinone disodium (PQQ·Na2) supplementation on the reproductive performance and intestinal barrier functions of gestating and lactating female Sprague–Dawley (SD) rats and their offspring. Dietary supplementation with PQQ·Na2 increased the number of implanted embryos per litter during gestation and lactation at GD 20 and increased the number of viable fetuses per litter, and the weight of uterine horns with fetuses increased at 1 d of newborn. The mRNA expression levels of catalase (CAT), glutathione peroxidase (GPx2), superoxide dismutase (SOD1), solute carrier family 2 member 1 (Slc2a1) · and solute carrier family 2 member 3 (Slc2a3) in the placenta were increased with dietary PQQ Na2 supplementation. Dietary , subject to the Cambridge Core terms of use, available at supplementation with PQQ·Na2 in gestating and lactating rats increased the CAT, SOD and GPx activities of the jejunal mucosa of weaned rats on PD 21. -
Annotation Guidelines for Experimental Procedures
Annotation Guidelines for Experimental Procedures Developed By Mohammed Alliheedi Robert Mercer Version 1 April 14th, 2018 1- Introduction and background information What is rhetorical move? A rhetorical move can be defined as a text fragment that conveys a distinct communicative goal, in other words, a sentence that implies an author’s specific purpose to readers. What are the types of rhetorical moves? There are several types of rhetorical moves. However, we are interested in 4 rhetorical moves that are common in the method section of a scientific article that follows the Introduction Methods Results and Discussion (IMRaD) structure. 1- Description of a method: It is concerned with a sentence(s) that describes experimental events (e.g., “Beads with bound proteins were washed six times (for 10 min under rotation at 4°C) with pulldown buffer and proteins harvested in SDS-sample buffer, separated by SDS-PAGE, and analyzed by autoradiography.” (Ester & Uetz, 2008)). 2- Appeal to authority: It is concerned with a sentence(s) that discusses the use of standard methods, protocols, and procedures. There are two types of this move: - A reference to a well-established “standard” method (e.g., the use of a method like “PCR” or “electrophoresis”). - A reference to a method that was previously described in the literature (e.g., “Protein was determined using fluorescamine assay [41].” (Larsen, Frandesn and Treiman, 2001)). 3- Source of materials: It is concerned with a sentence(s) that lists the source of biological materials that are used in the experiment (e.g., “All microalgal strains used in this study are available at the Elizabeth Aidar Microalgae Culture Collection, Department of Marine Biology, Federal Fluminense University, Brazil.” (Larsen, Frandesn and Treiman, 2001)). -
Mechanism of Reconstitution/Activation of the Soluble PQQ-Dependent Glucose Dehydrogenase from Acinetobacter Calcoaceticus
Mechanism of reconstitution/activation of the soluble PQQ-dependent glucose dehydrogenase from Acinetobacter calcoaceticus: a comprehensive study Claire Stines-Chaumeil, François Mavré, Brice Kauffmann, Nicolas Mano, Benoit Limoges To cite this version: Claire Stines-Chaumeil, François Mavré, Brice Kauffmann, Nicolas Mano, Benoit Limoges. Mecha- nism of reconstitution/activation of the soluble PQQ-dependent glucose dehydrogenase from Acine- tobacter calcoaceticus: a comprehensive study. ACS Omega, ACS Publications, 2020, 10.1021/ac- somega.9b04034. hal-02457126 HAL Id: hal-02457126 https://hal.archives-ouvertes.fr/hal-02457126 Submitted on 27 Jan 2020 HAL is a multi-disciplinary open access L’archive ouverte pluridisciplinaire HAL, est archive for the deposit and dissemination of sci- destinée au dépôt et à la diffusion de documents entific research documents, whether they are pub- scientifiques de niveau recherche, publiés ou non, lished or not. The documents may come from émanant des établissements d’enseignement et de teaching and research institutions in France or recherche français ou étrangers, des laboratoires abroad, or from public or private research centers. publics ou privés. Mechanism of reconstitution/activation of the soluble PQQ-dependent glucose dehydrogenase from Acinetobacter calcoaceticus: a comprehensive study Claire Stines-Chaumeil,*,a Francois Mavré,b Brice Kauffmann,c Nicolas Mano,a and Benoit Limoges*,b a CNRS, Université de Bordeaux, CRPP, UMR5031, 115 Avenue Schweitzer, F-33600 Pessac, France. b Université de Paris, Laboratoire d'Electrochimie Moléculaire, UMR 7591, CNRS, F-75013 Paris, France. c CNRS UMS3033, INSERM US001, Université de Bordeaux, IECB, 2, Rue Robert Escarpit, F- 33607 Pessac, France. KEYWORDS: pyrroloquinoline quinone, enzyme reconstitution, enzyme cofactor, apoenzyme, glucose dehydrogenase. -
The Clinical Significance of the Organic Acids Test
The Clinical Significance of the Organic Acids Test The Organic Acids Test (OAT) provides an accurate metabolic snapshot of what is going on in the body. Besides offering the most complete and accurate evaluation of intestinal yeast and bacteria, it also provides information on important neurotransmitters, nutritional markers, glutathione status, oxalate metabolism, and much more. The test includes 76 urinary metabolite markers that can be very useful for discovering underlying causes of chronic illness. Patients and physicians report that treating yeast and bacterial abnormalities reduces fatigue, increases alertness and energy, improves sleep, normalizes bowel function, and reduces hyperactivity and abdominal pain. The OAT Assists in Evaluating: ■ Krebs Cycle Abnormalities ■ Neurotransmitter Levels ■ Nutritional Deficiencies ■ Antioxidant Deficiencies ■ Yeast and Clostridia Overgrowth ■ Fatty Acid Metabolism ■ Oxalate Levels ■ And More! The OAT Pairs Well with the Following Tests: ■ GPL-TOX: Toxic Non-Metal Chemical Profile ■ IgG Food Allergy + Candida ■ MycoTOX Profile ■ Phospholipase A2 Activity Test Learn how to better integrate the OAT into your practice, along with our other top tests by attending one of our GPL Academy Practitioner Workshops! Visit www.GPLWorkshops.com for workshop dates and locations. The following pages list the 76 metabolite markers of the Organic Acids Test. Included is the name of the metabolic marker, its clinical significance, and usual initial treatment. INTESTINAL MICROBIAL OVERGROWTH Yeast and Fungal Markers Elevated citramalic acid is produced mainly by Saccharomyces species or Propionibacteria Citramalic Acid overgrowth. High-potency, multi-strain probiotics may help rebalance GI flora. A metabolite produced by Aspergillus and possibly other fungal species in the GI tract. 5-Hydroxy-methyl- Prescription or natural antifungals, along with high-potency, multi-strain probiotics, furoic Acid may reduce overgrowth levels. -
(Helianthus Annuus L.) Plastidial Lipoyl Synthases Genes Expression In
Impact of sunflower (Helianthus annuus L.) plastidial lipoyl synthases genes expression in glycerolipids composition of transgenic Arabidopsis plants Raquel Martins-Noguerol, Antonio Javier Moreno-Pérez, Acket Sebastien, Manuel Adrián Troncoso-Ponce, Rafael Garcés, Brigitte Thomasset, Joaquín Salas, Enrique Martínez-Force To cite this version: Raquel Martins-Noguerol, Antonio Javier Moreno-Pérez, Acket Sebastien, Manuel Adrián Troncoso- Ponce, Rafael Garcés, et al.. Impact of sunflower (Helianthus annuus L.) plastidial lipoyl synthases genes expression in glycerolipids composition of transgenic Arabidopsis plants. Scientific Reports, Nature Publishing Group, 2020, 10, pp.3749. 10.1038/s41598-020-60686-z. hal-02881038 HAL Id: hal-02881038 https://hal.archives-ouvertes.fr/hal-02881038 Submitted on 25 Jun 2020 HAL is a multi-disciplinary open access L’archive ouverte pluridisciplinaire HAL, est archive for the deposit and dissemination of sci- destinée au dépôt et à la diffusion de documents entific research documents, whether they are pub- scientifiques de niveau recherche, publiés ou non, lished or not. The documents may come from émanant des établissements d’enseignement et de teaching and research institutions in France or recherche français ou étrangers, des laboratoires abroad, or from public or private research centers. publics ou privés. www.nature.com/scientificreports OPEN Impact of sunfower (Helianthus annuus L.) plastidial lipoyl synthases genes expression in glycerolipids composition of transgenic Arabidopsis plants Raquel Martins-Noguerol1,2, Antonio Javier Moreno-Pérez 1,2, Acket Sebastien2, Manuel Adrián Troncoso-Ponce2, Rafael Garcés1, Brigitte Thomasset2, Joaquín J. Salas1 & Enrique Martínez-Force 1* Lipoyl synthases are key enzymes in lipoic acid biosynthesis, a co-factor of several enzyme complexes involved in central metabolism. -
Curriculum Vitae Natalie G. Ahn
Natalie G. Ahn Curriculum Vitae Natalie G. Ahn ADDRESS: Department of Biochemistry Jennie Smoly Caruthers Biotechnology Building 3415 Colorado Avenue, 596 UCB University of Colorado at Boulder Boulder, CO 80309-0596 Phone: (303) 492-4799 (Phone) Email: [email protected] I. ACADEMICS EDUCATION Postdoctoral Fellow, 1988-1990, Department of Pharmacology, Univ. of Washington, Seattle Research advisor: Edwin G. Krebs Postdoctoral Fellow, 1985-1987, Department of Medicine, Univ of Washington, Seattle Research advisor: Christoph de Haën Ph.D.,1985, Department of Chemistry University of California, Berkeley Thesis advisor: Judith P. Klinman 1979-1981 Teaching Assistant, undergraduate chemistry, Dept. of Chemistry 1981-1985 Research Assistant, Dept. of Chemistry B.S., 1979, Department of Chemistry, University of Washington, Seattle Undergraduate senior thesis advisor: Lyle H. Jensen, Department of Biological Structure Undergraduate research advisor: David C. Teller, Department of Biochemistry APPOINTMENTS 2018-present Distinguished Professor, University of Colorado 2003-present Associate Director, BioFrontiers Institute, Univ. Colorado, Boulder 1994-2014 Investigator, Howard Hughes Medical Institute (1994-2002 Assistant Investigator; 2003-2004 Associate Investigator; 2005-2014 Investigator) 1993-present Member, UCHSC Cancer Center, Univ. Colorado Health Sciences Center, Denver 1992-2018 Professor, Department of Chemistry and Biochemistry, Univ. Colorado, Boulder (1992-1998 Assistant Professor; 1998-2003 Associate Professor; 2003-present Professor) 1990-1992 Research Assistant Professor, Department of Biochemistry, Univ. Washington, Seattle 3 Natalie G. Ahn II. HONORS 2018 Distinguished Professor, University of Colorado 2018 Member, National Academy of Sciences 2018 Member, American Academy of Arts and Sciences 2016-2018 President, American Society of Biochemistry and Molecular Biology 2012 Professor of Distinction, College of Arts & Sciences, U. -
Crystallographic Snapshots of Sulfur Insertion by Lipoyl Synthase
Crystallographic snapshots of sulfur insertion by lipoyl synthase Martin I. McLaughlina,b,1, Nicholas D. Lanzc, Peter J. Goldmana, Kyung-Hoon Leeb, Squire J. Bookerb,c,d, and Catherine L. Drennana,e,f,2 aDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139; bDepartment of Chemistry, The Pennsylvania State University, University Park, PA 16802; cDepartment of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, PA 16802; dHoward Hughes Medical Institute, The Pennsylvania State University, University Park, PA 16802; eDepartment of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139; and fHoward Hughes Medical Institute, Massachusetts Institute of Technology, Cambridge, MA 02139 Edited by Vern L. Schramm, Albert Einstein College of Medicine, Bronx, NY, and approved July 5, 2016 (received for review March 8, 2016) Lipoyl synthase (LipA) catalyzes the insertion of two sulfur atoms substrate and at an intermediate stage in the reaction, just after at the unactivated C6 and C8 positions of a protein-bound octanoyl insertion of the C6 sulfur atom but before sulfur insertion at C8. chain to produce the lipoyl cofactor. To activate its substrate for sulfur insertion, LipA uses a [4Fe-4S] cluster and S-adenosylmethio- Results nine (AdoMet) radical chemistry; the remainder of the reaction The crystal structure of LipA from M. tuberculosis was de- mechanism, especially the source of the sulfur, has been less clear. termined to 1.64-Å resolution by iron multiwavelength anoma- One controversial proposal involves the removal of sulfur from a lous dispersion phasing (Table S1). The overall fold of LipA consists second (auxiliary) [4Fe-4S] cluster on the enzyme, resulting in de- of a (β/α)6 partial barrel common to most AdoMet radical enzymes struction of the cluster during each round of catalysis.