Pyruvate Ferredoxin Oxidoreductase from the Hyperthermophilic
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Characterization of a Microsomal Retinol Dehydrogenase Gene from Amphioxus: Retinoid Metabolism Before Vertebrates
Chemico-Biological Interactions 130–132 (2001) 359–370 www.elsevier.com/locate/chembiont Characterization of a microsomal retinol dehydrogenase gene from amphioxus: retinoid metabolism before vertebrates Diana Dalfo´, Cristian Can˜estro, Ricard Albalat, Roser Gonza`lez-Duarte * Departament de Gene`tica, Facultat de Biologia, Uni6ersitat de Barcelona, A6. Diagonal, 645, E-08028, Barcelona, Spain Abstract Amphioxus, a member of the subphylum Cephalochordata, is thought to be the closest living relative to vertebrates. Although these animals have a vertebrate-like response to retinoic acid, the pathway of retinoid metabolism remains unknown. Two different enzyme systems — the short chain dehydrogenase/reductases and the cytosolic medium-chain alcohol dehydrogenases (ADHs) — have been postulated in vertebrates. Nevertheless, recent data show that the vertebrate-ADH1 and ADH4 retinol-active forms originated after the divergence of cephalochordates and vertebrates. Moreover, no data has been gathered in support of medium-chain retinol active forms in amphioxus. Then, if the cytosolic ADH system is absent and these animals use retinol, the microsomal retinol dehydrogenases could be involved in retinol oxidation. We have identified the genomic region and cDNA of an amphioxus Rdh gene as a preliminary step for functional characterization. Besides, phyloge- netic analysis supports the ancestral position of amphioxus Rdh in relation to the vertebrate forms. © 2001 Elsevier Science Ireland Ltd. All rights reserved. Keywords: Retinol dehydrogenase; Retinoid metabolism; Amphioxus * Corresponding author. Fax: +34-93-4110969. E-mail address: [email protected] (R. Gonza`lez-Duarte). 0009-2797/01/$ - see front matter © 2001 Elsevier Science Ireland Ltd. All rights reserved. PII: S0009-2797(00)00261-1 360 D. -
Electron Flow and Management in Living Systems: Advancing Understanding of Electron Transfer to Nitrogenase
Utah State University DigitalCommons@USU All Graduate Theses and Dissertations Graduate Studies 8-2018 Electron Flow and Management in Living Systems: Advancing Understanding of Electron Transfer to Nitrogenase Rhesa N. Ledbetter Utah State University Follow this and additional works at: https://digitalcommons.usu.edu/etd Part of the Biochemistry Commons Recommended Citation Ledbetter, Rhesa N., "Electron Flow and Management in Living Systems: Advancing Understanding of Electron Transfer to Nitrogenase" (2018). All Graduate Theses and Dissertations. 7197. https://digitalcommons.usu.edu/etd/7197 This Dissertation is brought to you for free and open access by the Graduate Studies at DigitalCommons@USU. It has been accepted for inclusion in All Graduate Theses and Dissertations by an authorized administrator of DigitalCommons@USU. For more information, please contact [email protected]. ELECTRON FLOW AND MANAGEMENT IN LIVING SYSTEMS: ADVANCING UNDERSTANDING OF ELECTRON TRANSFER TO NITROGENASE by Rhesa N. Ledbetter A dissertation submitted in partial fulfillment of the requirements for the degree of DOCTOR OF PHILOSOPHY in Biochemistry Approved: ______________________ ______________________ Lance C. Seefeldt, Ph.D. Scott A. Ensign, Ph.D. Biochemistry Biochemistry Major Professor Committee Member ______________________ ______________________ Bruce Bugbee, Ph.D. Sean J. Johnson, Ph.D. Plant Physiology Biochemistry Committee Member Committee Member ______________________ ______________________ Nicholas E. Dickenson, Ph.D. Mark R. McLellan, Ph.D. Biochemistry Vice President for Research and Committee Member Dean of the School of Graduate Studies UTAH STATE UNIVERSITY Logan, Utah 2018 ii Copyright © Rhesa N. Ledbetter 2018 All Rights Reserved iii ABSTRACT Electron Flow and Management in Living Systems: Advancing Understanding of Electron Transfer to Nitrogenase by Rhesa N. -
Methionine Sulfoxide Reductase a Is a Stereospecific Methionine Oxidase
Methionine sulfoxide reductase A is a stereospecific methionine oxidase Jung Chae Lim, Zheng You, Geumsoo Kim, and Rodney L. Levine1 Laboratory of Biochemistry, National Heart, Lung, and Blood Institute, Bethesda, MD 20892-8012 Edited by Irwin Fridovich, Duke University Medical Center, Durham, NC, and approved May 10, 2011 (received for review February 10, 2011) Methionine sulfoxide reductase A (MsrA) catalyzes the reduction Results of methionine sulfoxide to methionine and is specific for the S epi- Stoichiometry. Branlant and coworkers have studied in careful mer of methionine sulfoxide. The enzyme participates in defense detail the mechanism of the MsrA reaction in bacteria (17, 18). against oxidative stresses by reducing methionine sulfoxide resi- In the absence of reducing agents, each molecule of MsrA dues in proteins back to methionine. Because oxidation of methio- reduces two molecules of MetO. Reduction of the first MetO nine residues is reversible, this covalent modification could also generates a sulfenic acid at the active site cysteine, and it is function as a mechanism for cellular regulation, provided there reduced back to the thiol by a fast reaction, which generates a exists a stereospecific methionine oxidase. We show that MsrA disulfide bond in the resolving domain of the protein. The second itself is a stereospecific methionine oxidase, producing S-methio- MetO is then reduced and again generates a sulfenic acid at the nine sulfoxide as its product. MsrA catalyzes its own autooxidation active site. Because the resolving domain cysteines have already as well as oxidation of free methionine and methionine residues formed a disulfide, no further reaction forms. -
Emerging Regulatory Roles of Mitochondrial Sirtuins on Pyruvate Dehydrogenase Complex and the Related Metabolic Diseases: Review
Biomedical Research and Therapy, 7(2):3645-3658 Open Access Full Text Article Review Emerging regulatory roles of mitochondrial sirtuins on pyruvate dehydrogenase complex and the related metabolic diseases: Review Abolfazl Nasiri1,2, Masoud Sadeghi3, Asad Vaisi-Raygani2,4, Sara Kiani3, Zahra Aghelan1,2, Reza Khodarahmi3,5,* ABSTRACT The pyruvate dehydrogenase complex (PDC) is a multi-enzyme complex of the mitochondria that provides a link between glycolysis and the Krebs cycle. PDC plays an essential role in producing Use your smartphone to scan this acetyl-CoA from glucose and the regulation of fuel consumption. In general, PDC enzyme is reg- QR code and download this article ulated in two different ways, end-product inhibition and posttranslational modifications (moreex- tensive phosphorylation and dephosphorylation subunit E1). Posttranslational modifications of this enzyme are regulated by various factors. Sirtuins are the class III of histone deacylatases that catalyze 1Students Research Committee, protein posttranslational modifications, including deacetylation, adenosine diphosphate ribosyla- Kermanshah University of Medical tion, and deacylation. Sirt3, Sirt4, and Sirt5 are mitochondrial sirtuins that control the posttrans- Sciences, Kermanshah, Iran lational modifications of mitochondrial protein. Considering the comprehensive role of sirtuins in post-translational modifications and regulation of metabolic processes, the aim of this review isto 2 Department of Clinical Biochemistry, explore the role of mitochondrial sirtuins in the regulation of the PDC. PDC deficiency is a com- School of Medicine, Kermanshah mon metabolic disorder that causes pyruvate to be converted to lactate and alanine rather than to University of Medical Sciences, Kermanshah, Iran acetyl-CoA. because this enzyme is in the gateway of complete oxidation, glucose products enter- ing the Krebs cycle and resulting in physiological and structural changes in the organs. -
Elevation of Cardiac Glycolysis Reduces Pyruvate Dehydrogenase but Increases Glucose Oxidation
University of Louisville ThinkIR: The University of Louisville's Institutional Repository Electronic Theses and Dissertations 5-2011 Elevation of cardiac glycolysis reduces pyruvate dehydrogenase but increases glucose oxidation. Qianwen Wang University of Louisville Follow this and additional works at: https://ir.library.louisville.edu/etd Recommended Citation Wang, Qianwen, "Elevation of cardiac glycolysis reduces pyruvate dehydrogenase but increases glucose oxidation." (2011). Electronic Theses and Dissertations. Paper 1519. https://doi.org/10.18297/etd/1519 This Doctoral Dissertation is brought to you for free and open access by ThinkIR: The University of Louisville's Institutional Repository. It has been accepted for inclusion in Electronic Theses and Dissertations by an authorized administrator of ThinkIR: The University of Louisville's Institutional Repository. This title appears here courtesy of the author, who has retained all other copyrights. For more information, please contact [email protected]. ELEVATION OF CARDIAC GLYCOLYSIS REDUCES PYRUVATE DEHYDROGENASE BUT INCREASES GLUCOSE OXIDATION By Qianwen Wang B.S., Guangdong Medical College of China, 1999 M.S., University of Louisville, 2006 A Dissertaion Submitted to the Faculty of the Graduate School of the University of Louisville In Partial Fulfillment of the Requirements for the Degree of Doctor of Philosophy Department of Physiology and Biophysics University of Louisville, School of Medicine Louisville, Kentucky May 2011 ELEVATION OF CARDIAC GLYCOLYSIS REDUCES PYRUVATE DEHYDROGENASE BUT INCREASES GLUCOSE OXIDATION By Qianwen Wang B.S., Guangdong Medical College of China, 1999 M.S., University of Louisville, 2006 A Dissertation Approved on March 28, 2011 by the following Dissertation Committee: Dissertation Director-Paul N. Epstein, Ph.D. William B. -
Cluster Characterization in Iron-Sulfur Proteins by Magnetic Circular Dichroism (Spectroscopic Probes/Ferredoxins) P
Proc. Natl. Acad. Sci. USA Vol. 75, No. 11, pp. 5273-5275, November 1978 Biochemistry Cluster characterization in iron-sulfur proteins by magnetic circular dichroism (spectroscopic probes/ferredoxins) P. J. STEPHENS*, A. J. THOMSON*t, T. A. KEIDERLING*t, J. RAWLINGS*§, K. K. RAOT, AND D. 0. HALLS * Department of Chemistry, University of Southern California, Los Angeles, California 90007; and ISchool of Biological Sciences, University of London King's College, 68 Half Moon Lane, London, England Communicated by Martin D. Kamen, August 2,1978- ABSTRACT We report magnetic circular dichroism (MCD) respect to the number of 4-Fe clusters). Ac values are normal- spectra of 4-Fe iron-sulfur clusters in the iron-sulfur proteins ized to a magnetic field of 10 kilogauss. Chromatium high-potential iron protein (HIPIP), Bacillus 1-3 MCD and stearothernophilus ferredoxin and Clostridium pasteurianum Figs. display absorption spectra for clusters ferredoxin. The MCD is found to vary significantly with cluster in the C2-, C3-, and Cl- states, respectively. The absorption oxidation state but is relatively insensitive to the nature of the spectra are typical of 4-Fe clusters, exhibiting few distinct protein. The spectra obtained are compared with the corre- features"l; for a given oxidation state the spectra are insensitive sponding spectra of iron-sulfur proteins containing 2-Fe clus- to the specific protein under study. By comparison, the MCD ters. It is concluded that MCD is useful for the characterization spectra are appreciably more structured than the absorption of iron-sulfur cluster type and oxidation state in iron-sulfur spectra but retain the insensitivity to the nature of the proteins and is superior for this purpose to absorption and nat- associated ural circular dichroism spectroscopy. -
Cellular Respiration
Cellular Respiration Glucose is the preferred carbohydrate of cells. In solution, it can change from a linear chain to a ring. Energy is stored in the bonds of the carbohydrates. Breaking these bonds releases that energy. Crushing sugar crystals creates tiny electrical fields that give off invisible ultraviolet light. The wintergreen chemical (methyl salicylate) gets excited by these excited electrons and fluoresces in a visible blue wavelength. This phenomenon is called triboluminescence. Contents 1 Glycolysis 2 Fermentation 3 The Preparatory Reaction 4 Mitochondria 5 Aerobic Respiration 6 Metabolic Pool Glycolysis Glucose is the preferred carbohydrate of cells. Glycolysis (glyco – sugar; lysis – splitting) is a universal process of all cells that occurs in the cytosol whereby the glucose (a 6-carbon sugar) is split into two pyruvate (a 3-carbon molecule) molecules to generate ATP and reduced NADH. ATP (adenosine triphosphate) is the energy currency of the cell that stores chemical energy in 3 high energy phosphate bonds. NADH (reduced nicotinamide adenine dinucleotide) is a high energy electron carrier that acts as a coenzyme in reactions and as a rechargeable battery of sorts. The uncharged state that is not carrying high energy electrons is called NAD+. CC-BY-NC-SA | Jeremy Seto | New York City College of Technology | 1 Cellular Respiration Glycolysis is the splitting of glucose into 2 pyruvate molecules to generate 2 NADH and 2ATP molecules. ATP contains 3 high energy phosphates and acts as cellular energy currency. NADH is the reduced form of NAD+. The High energy electrons associated with the reduced form come with a H atom. -
CELLULAR RESPIRATION Applied Medical Chemistry II Course
CELLULAR RESPIRATION Applied Medical Chemistry II Course Aim of the lecture This lecture discuss the steps of cellular respiration and its regulation Maye M. Ragab Super Visor / Dr. Neveen Introduction individual enzymic reactions were analyzed in an effort to explain the mechanisms of catalysis. However, in cells, these reactions rarely occur in isolation, but rather are organized into multistep sequences called pathways). In a pathway, the product of one reaction serves as the substrate of the subsequent reaction. Different pathways can also intersect, forming an integrated and purposeful network of chemical reactions. These are collectively called metabolism, which is the sum of all the chemical changes occurring in a cell, a tissue, or the body. Most pathways can be classified as either catabolic (degradative) or anabolic (synthetic). Anabolic pathways • form complex end products from simple precursors, for example, the synthesis of the polysaccharide, glycogen, from glucose. • Anabolic reactions require energy (are endergonic), which is generally provided by the breakdown of ATP to (ADP) and inorganic phosphate (Pi). • Anabolic reactions often involve chemical reductions in which the reducing power is most frequently provided by the electron donor NADPH . Catabolic reactions • break down complex molecules, such as proteins, polysaccharides, and lipids, to a few simple molecules, for example, CO2, NH3 (ammonia), and water. • Catabolic reactions serve to capture chemical energy in the form of (ATP) from the degradation of energy-rich fuel molecules. Energy generation by degradation of complex molecules occurs in three stages as in the following figure : [Note: Catabolic pathways are typically oxidative, and require coenzymes such as NAD+.] [Note: Pathways that regenerate a component are called cycles.] 1 2 Overview Of Glycolysis : • The glycolytic pathway is employed by all tissues for the breakdown of glucose to provide energy (in the form of ATP) and intermediates for other metabolic pathways. -
Electron Transfer Partners of Cytochrome P450
4 Electron Transfer Partners of Cytochrome P450 Mark J.l. Paine, Nigel S. Scrutton, Andrew W. Munro, Aldo Gutierrez, Gordon C.K. Roberts, and C. Roland Wolf 1. Introduction Although P450 redox partners are usually expressed independently, "self-sufficient" P450 monooxygenase systems have also evolved through Cytochromes P450 contain a heme center the fusion of P450 and CPR genes. These fusion where the activation of molecular oxygen occurs, molecules are found in bacteria and fungi, the best- resulting in the insertion of a single atom of known example being P450 BM3, a fatty acid oxygen into an organic substrate with the con (0-2 hydroxylase from Bacillus megaterium, which comitant reduction of the other atom to water. The comprises a soluble P450 with a fiised carboxyl- monooxygenation reaction requires a coupled and terminal CPR module (recently reviewed by stepwise supply of electrons, which are derived Munro^). BM3 has the highest catalytic activity from NAD(P)H and supplied via a redox partner. known for a P450 monooxygenase^ and was for P450s are generally divided into two major classes many years the only naturally occurring ftised sys (Class I and Class II) according to the different tem known until the identification of a eukaryotic types of electron transfer systems they use. P450s membrane-bound equivalent fatty acid hydroxy in the Class I family include bacterial and mito lase, CYP505A1, from the phytopathogenic fungus chondrial P450s, which use a two-component Fusarium oxysporurrP. A number of novel P450 sys shuttle system consisting of an iron-sulfur protein tems are starting to emerge from the large numbers (ferredoxin) and ferredoxin reductase (Figure 4.1). -
Containing Aldehyde Ferredoxin Oxidoreductase From
JOURNAL OF BACTERIOLOGY, Aug. 1995, p. 4817–4819 Vol. 177, No. 16 0021-9193/95/$04.0010 Copyright q 1995, American Society for Microbiology Molecular Characterization of the Genes Encoding the Tungsten- Containing Aldehyde Ferredoxin Oxidoreductase from Pyrococcus furiosus and Formaldehyde Ferredoxin Oxidoreductase from Thermococcus litoralis ARNULF KLETZIN,1† SWARNALATHA MUKUND,1 TERRY L. KELLEY-CROUSE,1 2 2 1 MICHAEL K. CHAN, DOUGLAS C. REES, AND MICHAEL W. W. ADAMS * Department of Biochemistry and Molecular Biology and Center for Metalloenzyme Studies, University of Georgia, Athens, Georgia 30602,1 and Division of Chemistry, California Institute of Technology, Pasadena, California 911252 Received 21 February 1995/Accepted 8 June 1995 The hyperthermophilic archaea Pyrococcus furiosus and Thermococcus litoralis contain the tungstoenzymes aldehyde ferredoxin oxidoreductase, a homodimer, and formaldehyde ferredoxin oxidoreductase, a homotet- ramer. Herein we report the cloning and sequencing of the P. furiosus gene aor (605 residues; Mr, 66,630) and the T. litoralis gene for (621 residues; Mr, 68,941). Enzymes containing tungsten (W) are rare in biology, yet the first 169 amino acid residues of a P. furiosus ahc gene encoding hyperthermophilic archaea contain three distinct types, all of an S-adenosylhomocysteine hydrolase; and (iii) a short open which catalyze aldehyde oxidation (6–9). The homodimeric reading frame and a partially sequenced long open reading aldehyde ferredoxin oxidoreductase (AOR) of Pyrococcus fu- frame of unknown function (Fig. 1) (5). riosus (maximum growth temperature [Tmax], 1058C [3]) oxi- The gene for AOR contained 605 codons which correspond dizes a wide range of aliphatic and aromatic, nonphosphory- to a protein with a molecular weight of 66,630 (compared with lated aldehydes (7). -
The PEP–Pyruvate–Oxaloacetate Node As the Switch Point for Carbon flux Distribution in Bacteria
View metadata, citation and similar papers at core.ac.uk brought to you by CORE provided by RERO DOC Digital Library FEMS Microbiology Reviews 29 (2005) 765–794 www.fems-microbiology.org The PEP–pyruvate–oxaloacetate node as the switch point for carbon flux distribution in bacteria Uwe Sauer a, Bernhard J. Eikmanns b,* a Institute of Biotechnology, ETH Zu¨rich, 8093 Zu¨rich, Switzerland b Department of Microbiology and Biotechnology, University of Ulm, 89069 Ulm, Germany Received 18 August 2004; received in revised form 27 October 2004; accepted 1 November 2004 First published online 28 November 2004 We dedicate this paper to Rudolf K. Thauer, Director of the Max-Planck-Institute for Terrestrial Microbiology in Marburg, Germany, on the occasion of his 65th birthday Abstract In many organisms, metabolite interconversion at the phosphoenolpyruvate (PEP)–pyruvate–oxaloacetate node involves a struc- turally entangled set of reactions that interconnects the major pathways of carbon metabolism and thus, is responsible for the dis- tribution of the carbon flux among catabolism, anabolism and energy supply of the cell. While sugar catabolism proceeds mainly via oxidative or non-oxidative decarboxylation of pyruvate to acetyl-CoA, anaplerosis and the initial steps of gluconeogenesis are accomplished by C3- (PEP- and/or pyruvate-) carboxylation and C4- (oxaloacetate- and/or malate-) decarboxylation, respectively. In contrast to the relatively uniform central metabolic pathways in bacteria, the set of enzymes at the PEP–pyruvate–oxaloacetate node represents a surprising diversity of reactions. Variable combinations are used in different bacteria and the question of the sig- nificance of all these reactions for growth and for biotechnological fermentation processes arises. -
A Brief Guide to Enzyme Classification and Nomenclature Rev AM
A Brief Guide to Enzyme Nomenclature and Classification Keith Tipton and Andrew McDonald 1) Introduction NC-IUBMB Enzyme List, or, to give it its full title, “Recommendations of the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology on the Nomenclature and Classification of Enzymes by the Reactions they Catalyse,1 is a functional system, based solely on the substrates transformed and products formed by an enzyme. The basic layout of the classification for each enzyme is described below with some indication of the guidelines followed. More detailed rules for enzyme nomenclature and classification are available online.2 Further details of the principles governing the nomenclature of individual enzyme classes are given in the following sections. 2. Basic Concepts 2.1. EC numbers Enzymes are identified by EC (Enzyme Commission) numbers. These are also valuable for relating the information to other databases. They were divided into 6 major classes according to the type of reaction catalysed and a seventh, the translocases, was added in 2018.3 These are shown in Table 1. Table 1. Enzyme classes Name Reaction catalysed 1 Oxidoreductases *AH2 + B = A +BH2 2 Transferases AX + B = BX + A 3 Hydrolases A-B + H2O = AH + BOH 4 Lyases A=B + X-Y = A-B ç ç X Y 5 Isomerases A = B 6 LiGases †A + B + NTP = A-B + NDP + P (or NMP + PP) 7 Translocases AX + B çç = A + X + ççB (side 1) (side 2) *Where nicotinamide-adenine dinucleotides are the acceptors, NAD+ and NADH + H+ are used, by convention. †NTP = nucleoside triphosphate. The EC number is made up of four components separated by full stops.