Enzyme Relationships Ina Sorbitol Pathway That Bypasses Glycolysis

Total Page:16

File Type:pdf, Size:1020Kb

Enzyme Relationships Ina Sorbitol Pathway That Bypasses Glycolysis Proc. Nati. Acad. Sci. USA Vol. 80, pp. 901-905, Februarv 1983 Biochemistry Enzyme relationships in a sorbitol pathway that bypasses glycolysis and pentose phosphates in glucose metabolism (isozymes/diabetes/alcohol dehydrogenase/reductases/alcoholism) JONATHAN JEFFERY* AND HANS JORNVALLt *Department of Biochemistry, University ofAberdeen, Marischal College, Aberdeen, AB9 lAS Scotland, United Kingdom; and tDepartment of Chemistry I, Karolinska Institutet, S-104 01 Stockholm 60, Sweden Communicated by Sune Bergstr6m, September 17, 1982 ABSTRACT A pathway from glucose via sorbitol bypasses the fructose (8). Increased operation ofthe glycerol phosphate shut- control points of hexokinase and phosphofructokinase in glucose tle could also mediate the effect (9). metabolism. It also may produce glycerol, linking the bypass to The structural relationships, the diverse and unrelated met- lipid synthesis. Utilization of this bypass is favored by a plentiful abolic suggestions, the apparent associations of some interme- supply of glucose-hence, conditions under which glycolysis also diate compounds, and the possible convergent relationships is active. The bypass further involves oxidation of NADPH, so the motivate a search for unifying explanations, detailing the sor- pentose phosphate pathway and the bypass are mutually facilita- bitol pathway and its consequences. tive. Possible consequences in different organs under normal and pathological, especially diabetic, conditions are detailed. Enzymes with related structures (for example, sorbitol dehydrogenase and MATERIALS AND METHODS alcohol dehydrogenase, and possibly, aldehyde reductase and al- Glucose Metabolism via a Five-Step Sorbitol Pathway By- dose reductase, respectively) are linked functionally by this passing the scheme. Some enzymes of the bypass also feature in glycolysis Regulatory Steps of Glycolysis. In glucose metab- (aldolase and alcohol dehydrogenase), and these enzymes, with the olism, flux through the glycolytic and pentose phosphate path- reductases involved, are proteins known to occur in different ways is regulated at phosphofructokinase (10) and glucose-6- classes or multiple isozyme forms. Two of the enzymes (aldolase phosphate dehydrogenase (11). Hexokinase is generally also a and alcohol dehydrogenase) both involve classes with and without control point, though the effect in liver is overcome at high a catalytic metal (zinc). The existence ofparallel pathways and the glucose concentrations by glucokinase. However, as shown in occurrence of similar enzymic steps in one pathway may help to Fig. 1, a complete pathway similar to glycolysis but fully by- explain the abundance and multiplicity ofenzymes such as reduc- passing the hexokinase and phosphofructokinase steps also is tases, aldolases, and alcohol dehydrogenases. possible. It involves oxidation of one or two molecules of NADPH, thus favoring operation of the pentose phosphate Although alcohol dehydrogenase is widespread in nature, is pathway, and is linked to lipid synthesis via glycerol formation common in liver, and has been structurally characterized from (Fig. 1). several sources (1), its exact role in mammalian organs generally The first step of the pathway is conversion of glucose into has remained unclear. In addition to ethanol oxidation, func- sorbitol by aldose reductase and NADPH. Oxidation ofsorbitol tions in bile acid formation, fatty acid degradation, vitamin A by sorbitol dehydrogenase and NAD' then yields fructose. metabolism, a hydroxysteroid reaction, and other areas of me- Fructose is not a substrate for glucokinase, but in some circum- tabolism have been considered (2). Different and multiple func- stances hexokinase and ATP could convert it into fructose 6- tions of alcohol dehydrogenase would be consistent with the phosphate, leading into glycolysis at the phosphofructokinase considerable species variations and extensive evolutionary reaction. This loop via sorbitol then would serve as a transhy- changes found. drogenase function (reduction of NAD+ and oxidation of Recently, another common liver enzyme, sorbitol dehydro- NADPH). Alternatively, fructokinase and ATP could convert genase, was shown to be structurally, mechanistically, and an- fructose into fructose 1-phosphate. This compound can be cestrally related to alcohol dehydrogenase (3). The substrates of cleaved by aldolase B to give dihydroxyacetone phosphate and sorbitol dehydrogenase, fructose and sorbitol, are considered glyceraldehyde. Glyceraldehyde 3-phosphate results from the important in special organs, such as male sexual organs (4), or action oftriosephosphate isomerase on dihydroxyacetone phos- special disease states, such as hyperglycemic cataract formation phate or oftriokinase on glyceraldehyde. Entry at this stage into (5) and possibly diabetic neuropathy (6) and glomerulosclerosis glycolysis via glyceraldehyde 3-phosphate bypasses the hexo- (7), but a more general metabolic significance that is compatible kinase and phosphofructokinase reactions. Conversion of glyc- with the structural similarity of these enzymes has not been clear. eraldehyde to glycerol is an alternative to phosphorylation. The The structural link between alcohol and polyol dehydroge- reduction can be effected by alcohol dehydrogenase and NADH nases showed a type ofparallel or convergent evolution ofa sec- or by aldehyde reductase and NADPH. ond, different enzyme in each case with related specificity (3). Occurrence of the individual enzymes of the pathway is de- Enhancement of alcohol metabolism by fructose gave one as- scribed in relation to the organs mentioned below. The initial sociation between the substrates for sorbitol and alcohol dehy- steps of the pathway, with the glucose-fructose conversion drogenases. This effect may stem from avoidance of the rate- (sometimes also called the "sorbitol pathway"), have been dis- limiting NADH dissociation off alcohol dehydrogenase by an cussed further in relation to diabetes or insulin effects (12), but in situ coenzyme reoxidation with glyceraldehyde formed from usually not the associated, later combination into glycolysis or lipogenesis. The publication costs ofthis article were defrayed in part by page charge In summary, the essential steps providing the bypass are payment. This article must therefore be hereby marked "advertise- those leading via sorbitol and fructose 1-phosphate to glycer- ment" in accordance with 18 U. S. C. §1734 solely to indicate this fact. aldehyde 3-phosphate and linking, among other enzymes, sor- 901 Downloaded by guest on September 30, 2021 902 Biochemistry: Jeffery and Jbrnvall Proc. Natl. Acad. Sci. USA 80 (1983) bitol dehydrogenase and alcohol dehydrogenase with various ofthe aldose reductase type (that is, NADPH-linked aldehyde reductases and aldolases. reductases) have little (15) activity towards glucose, and much hepatic sorbitol dehydrogenase is present. These aspects sug- RESULTS AND DISCUSSION gest that liver may not be the main functional site ofthe entire Normal Occurrence. The scheme in Fig. 1 and the enzymes bypass for energy production but rather for permitting metab- shown demonstrate that the bypass or parts ofit may be offunc- olism of important compounds in any ratios. tional significance. In this respect, five tissues or organs appear Pancreas. Sorbitol is present in pancreas and glucose-induced of special interest in normal conditions. They are, on the one insulin release evidently requires both NADPH and aldose re- hand, the liver, pancreas, and placenta, where some com- ductase activity within the f3 cells (12). Reduction ofglucose to pounds ofthe scheme may have special roles, and, on the other sorbitol possibly primes or activates an element in the insulin hand, the brain and the reproductive system, where the bypass release mechanism (12). Therefore, it appears possible that in appears capable of having a more general metabolic role. the pancreas, the initial steps ofthe scheme in Fig. 1 may have Liver. As the main processorofingestedcompounds, the liver special functions. As in the liver, they may not be ofenergetic might be expected to encounter sorbitol. However, orally in- value in an entire bypass ofglycolysis but serve other functions, gested sorbitol is poorly absorbed in man and animals, and prod- which in the case of pancreas may be metabolic regulation via ucts ofits metabolism by intestinal microorganisms, rather than insulin release. sorbitol itself, are absorbed (13, 14). Nevertheless, sorbitol en- Placenta. Glucose is converted into fructose by the aldose tering the livercould be oxidized byhepatic sorbitol dehydroge- reductase and sorbitol dehydrogenase of normal placenta (16) nase in the same way that ethanol is oxidized by alcohol dehy- and umbilical cord (17) in species including man. High concen- drogenase. trations offructose in the fetal blood ofungulates (for example, Most important, liver deals with high postprandial concen- sheep and pig) apparently result from nonutilization offructose trations of glucose. Accumulation of sorbitol formed from glu- by their fetuses (18). Because fructose is not an important fetal cose within the liver then would be disadvantageous, raising the energy source in these cases, the loop from glucose to fructose osmotic pressure of the cells. Significantly, the liver enzymes may have an osmoregulatory role or serve a transhydrogenase Glucose aldose hexokinase (Iglucokinase) Glucose-6-P sorbi tol dehydrogenase Fructose I11 Fructose-6-P phospho- fructokinase fructokinase Fructose-l-P Fructose-1,6-bisP
Recommended publications
  • Characterization of Flavin-Containing Opine Dehydrogenase from Bacteria
    RESEARCH ARTICLE Characterization of Flavin-Containing Opine Dehydrogenase from Bacteria Seiya Watanabe1,2*, Rui Sueda1, Fumiyasu Fukumori3, Yasuo Watanabe1 1 Faculty of Agriculture, Ehime University, Matsuyama, Ehime, Japan, 2 Center for Marine Environmental Studies, Ehime University, Matsuyama, Ehime, Japan, 3 Faculty of Food and Nutritional Sciences, Toyo University, Itakura-machi, Gunma, Japan * [email protected] Abstract Opines, in particular nopaline and octopine, are specific compounds found in crown gall tumor tissues induced by infections with Agrobacterium species, and are synthesized by well-studied NAD(P)H-dependent dehydrogenases (synthases), which catalyze the reduc- tive condensation of α-ketoglutarate or pyruvate with L-arginine. The corresponding genes are transferred into plant cells via a tumor-inducing (Ti) plasmid. In addition to the reverse OPEN ACCESS oxidative reaction(s), the genes noxB-noxA and ooxB-ooxA are considered to be involved Citation: Watanabe S, Sueda R, Fukumori F, in opine catabolism as (membrane-associated) oxidases; however, their properties have Watanabe Y (2015) Characterization of Flavin- not yet been elucidated in detail due to the difficulties associated with purification (and pres- Containing Opine Dehydrogenase from Bacteria. ervation). We herein successfully expressed Nox/Oox-like genes from Pseudomonas PLoS ONE 10(9): e0138434. doi:10.1371/journal. putida in P. putida cells. The purified protein consisted of different α-, β-, and γ-subunits pone.0138434 encoded by the OdhA, OdhB, and OdhC genes, which were arranged in tandem on the Editor: Eric Cascales, Centre National de la chromosome (OdhB-C-A), and exhibited dehydrogenase (but not oxidase) activity toward Recherche Scientifique, Aix-Marseille Université, FRANCE nopaline in the presence of artificial electron acceptors such as 2,6-dichloroindophenol.
    [Show full text]
  • Amino Acids Biosynthesis and Nitrogen
    Guedes et al. BMC Genomics 2011, 12(Suppl 4):S2 http://www.biomedcentral.com/1471-2164/12/S4/S2 PROCEEDINGS Open Access Amino acids biosynthesis and nitrogen assimilation pathways: a great genomic deletion during eukaryotes evolution RLM Guedes1, F Prosdocimi2,3, GR Fernandes1,2, LK Moura2, HAL Ribeiro1, JM Ortega1* From 6th International Conference of the Brazilian Association for Bioinformatics and Computational Biology (X-meeting 2010) Ouro Preto, Brazil. 15-18 November 2010 Abstract Background: Besides being building blocks for proteins, amino acids are also key metabolic intermediates in living cells. Surprisingly a variety of organisms are incapable of synthesizing some of them, thus named Essential Amino Acids (EAAs). How certain ancestral organisms successfully competed for survival after losing key genes involved in amino acids anabolism remains an open question. Comparative genomics searches on current protein databases including sequences from both complete and incomplete genomes among diverse taxonomic groups help us to understand amino acids auxotrophy distribution. Results: Here, we applied a methodology based on clustering of homologous genes to seed sequences from autotrophic organisms Saccharomyces cerevisiae (yeast) and Arabidopsis thaliana (plant). Thus we depict evidences of presence/absence of EAA biosynthetic and nitrogen assimilation enzymes at phyla level. Results show broad loss of the phenotype of EAAs biosynthesis in several groups of eukaryotes, followed by multiple secondary gene losses. A subsequent inability for nitrogen assimilation is observed in derived metazoans. Conclusions: A Great Deletion model is proposed here as a broad phenomenon generating the phenotype of amino acids essentiality followed, in metazoans, by organic nitrogen dependency. This phenomenon is probably associated to a relaxed selective pressure conferred by heterotrophy and, taking advantage of available homologous clustering tools, a complete and updated picture of it is provided.
    [Show full text]
  • Energy Metabolism in the Tropical Abalone, Haliotis Asinina Linné: Comparisons with Temperate Abalone Species ⁎ J
    Journal of Experimental Marine Biology and Ecology 342 (2007) 213–225 www.elsevier.com/locate/jembe Energy metabolism in the tropical abalone, Haliotis asinina Linné: Comparisons with temperate abalone species ⁎ J. Baldwin a, , J.P. Elias a, R.M.G. Wells b, D.A. Donovan c a School of Biological Sciences, Monash University, Clayton, Victoria 3800, Australia b School of Biological Sciences, The University of Auckland, Private Bag 92019, Auckland, New Zealand c Department of Biology, MS 9160, Western Washington University, Bellingham, WA 98225, USA Received 15 March 2006; received in revised form 14 July 2006; accepted 12 September 2006 Abstract The abalone, Haliotis asinina, is a large, highly active tropical abalone that feeds at night on shallow coral reefs where oxygen levels of the water may be low and the animals can be exposed to air. It is capable of more prolonged and rapid exercise than has been reported for temperate abalone. These unusual behaviours raised the question of whether H. asinina possesses enhanced capacities for aerobic or anaerobic metabolism. The blood oxygen transport system of H. asinina resembles that of temperate abalone in terms of a large hemolymph volume, similar hemocyanin concentrations, and in most hemocyanin oxygen binding properties; however, absence of a Root effect appears confined to hemocyanin from H. asinina and may assist oxygen uptake when hemolymph pH falls during exercise or environmental hypoxia. During exposure to air, H. asinina reduces oxygen uptake by at least 20-fold relative to animals at rest in aerated seawater, and there is no significant ATP production from anaerobic glycolysis or phosphagen hydrolysis in the foot or adductor muscles.
    [Show full text]
  • A Structural and Kinetic Analysis of a New Functional Class of Opine
    ARTICLE cro Staphylopine, pseudopaline, and yersinopine dehydrogenases: A structural and kinetic analysis of a new functional class of opine dehydrogenase Received for publication, January 19, 2018, and in revised form, April 3, 2018 Published, Papers in Press, April 4, 2018, DOI 10.1074/jbc.RA118.002007 Jeffrey S. McFarlane‡, Cara L. Davis§, and X Audrey L. Lamb‡§1 From the Departments of ‡Molecular Biosciences and §Chemistry, University of Kansas, Lawrence, Kansas 66045 Edited by F. Peter Guengerich Opine dehydrogenases (ODHs) from the bacterial pathogens densation of an ␣ or ␻ amino group from an amino acid with an Staphylococcus aureus, Pseudomonas aeruginosa, and Yersinia ␣-keto acid followed by reduction with NAD(P)H, producing a pestis perform the final enzymatic step in the biosynthesis of a family of products known as N-(carboxyalkyl) amino acids or new class of opine metallophores, which includes staphylopine, opines (Fig. 1)(1). Opines are composed of a variety ␣-keto acid Downloaded from pseudopaline, and yersinopine, respectively. Growing evidence and amino acid substrates and have diverse functional roles. indicates an important role for this pathway in metal acquisition Octopine, isolated from octopus muscle by Morizawa in 1927, and virulence, including in lung and burn-wound infections was the first described opine, composed of pyruvate and argi- (P. aeruginosa) and in blood and heart infections (S. aureus). nine (2). ODHs are widespread in cephalopods and mollusks, Here, we present kinetic and structural characterizations of such as Pecten maximus, the king scallop, where they allow the http://www.jbc.org/ these three opine dehydrogenases. A steady-state kinetic analy- continuation of glycolysis under anaerobic conditions by sis revealed that the three enzymes differ in ␣-keto acid and shunting pyruvate into opine products and regenerating NADϩ NAD(P)H substrate specificity and nicotianamine-like sub- (3).
    [Show full text]
  • Metabolic Responses of the Estuarine Gastropod Thais Haemastoma to Hypoxia (Energy Charge, Opine Dehydrogenase,Survival, Adaptation, Respiration)
    Louisiana State University LSU Digital Commons LSU Historical Dissertations and Theses Graduate School 1985 Metabolic Responses of the Estuarine Gastropod Thais Haemastoma to Hypoxia (Energy Charge, Opine Dehydrogenase,survival, Adaptation, Respiration). Martin A. Kapper Louisiana State University and Agricultural & Mechanical College Follow this and additional works at: https://digitalcommons.lsu.edu/gradschool_disstheses Recommended Citation Kapper, Martin A., "Metabolic Responses of the Estuarine Gastropod Thais Haemastoma to Hypoxia (Energy Charge, Opine Dehydrogenase,survival, Adaptation, Respiration)." (1985). LSU Historical Dissertations and Theses. 4095. https://digitalcommons.lsu.edu/gradschool_disstheses/4095 This Dissertation is brought to you for free and open access by the Graduate School at LSU Digital Commons. It has been accepted for inclusion in LSU Historical Dissertations and Theses by an authorized administrator of LSU Digital Commons. For more information, please contact [email protected]. INFORMATION TO USERS This reproduction was made from a copy of a document sent to us for microfilming. While the most advanced technology has been used to photograph and reproduce this document, the quality of the reproduction is heavily dependent upon the quality of the material submitted. The following explanation of techniques is provided to help clarify markings or notations which may appear on this reproduction. 1.The sign or “target" for pages apparently lacking from the document photographed is “Missing Page(s)”. If it was possible to obtain the missing page(s) or section, they are spliced into the film along with adjacent pages. This may have necessitated cutting through an image and duplicating adjacent pages to assure complete continuity. 2. When an image on the film is obliterated with a round black mark, it is an indication of either blurred copy because of movement during exposure, duplicate copy, or copyrighted materials that should not have been filmed.
    [Show full text]
  • Stereoselective Synthesis of Opine-Type Secondary Amine Carboxylic Acids by a New Enzyme Opine Dehydrogenase Use of Recombinant Enzymes
    ELSEVIER Journal of Molecular Catalysis B: Enzymatic I (I 996) I5 I- 160 Stereoselective synthesis of opine-type secondary amine carboxylic acids by a new enzyme opine dehydrogenase Use of recombinant enzymes Yasuo Kato, Hideaki Yamada, Yasuhisa Asano * Biotechrrology Research Center, Faculty of Engineering, Toyma Prefectural Unif~ersity,5180 Kurokawn, Kosugi. Towma 939-03, Japm Received 12 September 1995; accepted 19 October 1995 Abstract The substrate specificity of the recently discovered enzyme, opine dehydrogenase (ODH) from Arthrohucter sp. strain IC for amino donors in the reaction that forms secondary amines using pyruvate as a fixed amino acceptor is examined. The enzyme was active toward short-chain aliphatic @)-amino acids and those substituted with acyloxy, phosphonooxy, and halogen groups. The enzyme was named N-[ 1-(R)-(carboxyl)ethyl]-(S)-norvaline: NAD+ oxidoreductase (L-norvaline forming). Other substrates for the enzyme were 3-aminobutyric acid and (S)-phenylalaninol. Optically pure opine-type secondary amine carboxylic acids were synthesized from amino acids and their analogs such as (S)-methionine, (S)-iso- leucine, (S)-leucine. (S)-valine, (S)-phenylalanine, (S)-alanine, (S)-threonine, (S)-serine, and (S)-phenylalaninol, and cu-keto acids such as glyoxylate, pyruvate, and 2-oxobutyrate using the enzyme, with regeneration of NADH by formate dehydrogenase (FDH) from Moruxellu sp. C-l. The absolute configuration of the nascent asymmetric center of the opines was of the (R) stereochemistry with > 99.9% e.e. One-pot synthesis of N-[ 1-( R)-(carboxyl)ethyl]-(S)-phenylalanine from phenylpyruvate and pyruvate by using ODH, FDH, and phenylalanine dehydrogenase (PheDH) from Bacillus sphaericus. is also described.
    [Show full text]
  • Purification and Characterization of Tauropine Dehydrogenase from the Marine Sponge Halichondria Japonica Kadota (Demospongia)*1
    Fisheries Science 63(3), 414-420 (1997) Purification and Characterization of Tauropine Dehydrogenase from the Marine Sponge Halichondria japonica Kadota (Demospongia)*1 Nobuhiro Kan-no,*2,•õ Minoru Sato,*3 Eizoh Nagahisa,*2 and Yoshikazu Sato*2 *2School of Fisheries Sciences , Kitasato University, Sanriku, Iwate 022-01, Japan *3Faculty of Agriculture , Tohoku University, Sendai, Miyagi 981, Japan (Received July 8, 1996) Tauropine dehydrogenase (tauropine: NAD oxidoreductase) was purified to homogeneity from the sponge Halichondria japonica Kadota (colony). Relative molecular masses of this enzyme in its native form and in its denatured form were 36,500 and 37,000, respectively, indicating a monomeric structure. The maximum rate in the tauropine-biosynthetic reaction was observed at pH 6.8, and that in the tauro pine-catabolic reaction at pH 9.0. Pyruvate and taurine were the preferred substrates. The enzyme showed significant activity for oxalacetate as a substitute for pyruvate but much lower activities for other keto acids and amino acids. The tauropine-biosynthetic reaction was strongly inhibited by the substrate pyruvate. The optimal concentration of pyruvate was 0.25-0.35 mm and the inhibitory concen tration giving half-maximal rate was 3.2 mm. The tauropine-catabolic reaction was inhibited by the sub strate tauropine: the optimal concentration was 2.5-5.0 mm. Apparent K,,, values determined using con stant cosubstrate concentrations were 37.0 mm for taurine, 0.068 mm for pyruvate, and 0.036 mm for NADH in the tauropine-biosynthetic reaction; and 0.39 mm for tauropine and 0.16 mm for NAD+ in the tauropine-catabolic reaction.
    [Show full text]
  • 12) United States Patent (10
    US007635572B2 (12) UnitedO States Patent (10) Patent No.: US 7,635,572 B2 Zhou et al. (45) Date of Patent: Dec. 22, 2009 (54) METHODS FOR CONDUCTING ASSAYS FOR 5,506,121 A 4/1996 Skerra et al. ENZYME ACTIVITY ON PROTEIN 5,510,270 A 4/1996 Fodor et al. MICROARRAYS 5,512,492 A 4/1996 Herron et al. 5,516,635 A 5/1996 Ekins et al. (75) Inventors: Fang X. Zhou, New Haven, CT (US); 5,532,128 A 7/1996 Eggers Barry Schweitzer, Cheshire, CT (US) 5,538,897 A 7/1996 Yates, III et al. s s 5,541,070 A 7/1996 Kauvar (73) Assignee: Life Technologies Corporation, .. S.E. al Carlsbad, CA (US) 5,585,069 A 12/1996 Zanzucchi et al. 5,585,639 A 12/1996 Dorsel et al. (*) Notice: Subject to any disclaimer, the term of this 5,593,838 A 1/1997 Zanzucchi et al. patent is extended or adjusted under 35 5,605,662 A 2f1997 Heller et al. U.S.C. 154(b) by 0 days. 5,620,850 A 4/1997 Bamdad et al. 5,624,711 A 4/1997 Sundberg et al. (21) Appl. No.: 10/865,431 5,627,369 A 5/1997 Vestal et al. 5,629,213 A 5/1997 Kornguth et al. (22) Filed: Jun. 9, 2004 (Continued) (65) Prior Publication Data FOREIGN PATENT DOCUMENTS US 2005/O118665 A1 Jun. 2, 2005 EP 596421 10, 1993 EP 0619321 12/1994 (51) Int. Cl. EP O664452 7, 1995 CI2O 1/50 (2006.01) EP O818467 1, 1998 (52) U.S.
    [Show full text]
  • All Enzymes in BRENDA™ the Comprehensive Enzyme Information System
    All enzymes in BRENDA™ The Comprehensive Enzyme Information System http://www.brenda-enzymes.org/index.php4?page=information/all_enzymes.php4 1.1.1.1 alcohol dehydrogenase 1.1.1.B1 D-arabitol-phosphate dehydrogenase 1.1.1.2 alcohol dehydrogenase (NADP+) 1.1.1.B3 (S)-specific secondary alcohol dehydrogenase 1.1.1.3 homoserine dehydrogenase 1.1.1.B4 (R)-specific secondary alcohol dehydrogenase 1.1.1.4 (R,R)-butanediol dehydrogenase 1.1.1.5 acetoin dehydrogenase 1.1.1.B5 NADP-retinol dehydrogenase 1.1.1.6 glycerol dehydrogenase 1.1.1.7 propanediol-phosphate dehydrogenase 1.1.1.8 glycerol-3-phosphate dehydrogenase (NAD+) 1.1.1.9 D-xylulose reductase 1.1.1.10 L-xylulose reductase 1.1.1.11 D-arabinitol 4-dehydrogenase 1.1.1.12 L-arabinitol 4-dehydrogenase 1.1.1.13 L-arabinitol 2-dehydrogenase 1.1.1.14 L-iditol 2-dehydrogenase 1.1.1.15 D-iditol 2-dehydrogenase 1.1.1.16 galactitol 2-dehydrogenase 1.1.1.17 mannitol-1-phosphate 5-dehydrogenase 1.1.1.18 inositol 2-dehydrogenase 1.1.1.19 glucuronate reductase 1.1.1.20 glucuronolactone reductase 1.1.1.21 aldehyde reductase 1.1.1.22 UDP-glucose 6-dehydrogenase 1.1.1.23 histidinol dehydrogenase 1.1.1.24 quinate dehydrogenase 1.1.1.25 shikimate dehydrogenase 1.1.1.26 glyoxylate reductase 1.1.1.27 L-lactate dehydrogenase 1.1.1.28 D-lactate dehydrogenase 1.1.1.29 glycerate dehydrogenase 1.1.1.30 3-hydroxybutyrate dehydrogenase 1.1.1.31 3-hydroxyisobutyrate dehydrogenase 1.1.1.32 mevaldate reductase 1.1.1.33 mevaldate reductase (NADPH) 1.1.1.34 hydroxymethylglutaryl-CoA reductase (NADPH) 1.1.1.35 3-hydroxyacyl-CoA
    [Show full text]
  • (12) Patent Application Publication (10) Pub. No.: US 2015/0240226A1 Mathur Et Al
    US 20150240226A1 (19) United States (12) Patent Application Publication (10) Pub. No.: US 2015/0240226A1 Mathur et al. (43) Pub. Date: Aug. 27, 2015 (54) NUCLEICACIDS AND PROTEINS AND CI2N 9/16 (2006.01) METHODS FOR MAKING AND USING THEMI CI2N 9/02 (2006.01) CI2N 9/78 (2006.01) (71) Applicant: BP Corporation North America Inc., CI2N 9/12 (2006.01) Naperville, IL (US) CI2N 9/24 (2006.01) CI2O 1/02 (2006.01) (72) Inventors: Eric J. Mathur, San Diego, CA (US); CI2N 9/42 (2006.01) Cathy Chang, San Marcos, CA (US) (52) U.S. Cl. CPC. CI2N 9/88 (2013.01); C12O 1/02 (2013.01); (21) Appl. No.: 14/630,006 CI2O I/04 (2013.01): CI2N 9/80 (2013.01); CI2N 9/241.1 (2013.01); C12N 9/0065 (22) Filed: Feb. 24, 2015 (2013.01); C12N 9/2437 (2013.01); C12N 9/14 Related U.S. Application Data (2013.01); C12N 9/16 (2013.01); C12N 9/0061 (2013.01); C12N 9/78 (2013.01); C12N 9/0071 (62) Division of application No. 13/400,365, filed on Feb. (2013.01); C12N 9/1241 (2013.01): CI2N 20, 2012, now Pat. No. 8,962,800, which is a division 9/2482 (2013.01); C07K 2/00 (2013.01); C12Y of application No. 1 1/817,403, filed on May 7, 2008, 305/01004 (2013.01); C12Y 1 1 1/01016 now Pat. No. 8,119,385, filed as application No. PCT/ (2013.01); C12Y302/01004 (2013.01); C12Y US2006/007642 on Mar. 3, 2006.
    [Show full text]
  • Simple Rules Govern the Diversity of Bacterial Nicotianamine-Like Metallophores
    bioRxiv preprint doi: https://doi.org/10.1101/641969; this version posted May 19, 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. 1 Simple rules govern the diversity of bacterial nicotianamine-like metallophores 2 Clémentine Laffont1, Catherine Brutesco1, Christine Hajjar1, Gregorio Cullia2, Roberto Fanelli2, 3 Laurent Ouerdane3, Florine Cavelier2, Pascal Arnoux1,* 4 1Aix Marseille Univ, CEA, CNRS, BIAM, Saint Paul-Lez-Durance, France F-13108. 5 2Institut des Biomolécules Max Mousseron, IBMM, UMR-5247, CNRS, Université Montpellier, 6 ENSCM , Place Eugène Bataillon, 34095 Montpellier cedex 5, France. 7 3CNRS-UPPA, Laboratoire de Chimie Analytique Bio-inorganique et Environnement, UMR 5254, 8 Hélioparc, 2, Av. Angot 64053 Pau, France. 9 *Correspondance: Pascal Arnoux, Aix Marseille Univ, CEA, CNRS, BIAM, Saint Paul-Lez- 10 Durance, France F-13108; [email protected]; Tel. 04-42-25-35-70 11 Keywords: opine/opaline dehydrogenase, CntM, nicotianamine-like metallophore, bacillopaline 12 13 ABSTRACT 14 In metal-scarce environments, some pathogenic bacteria produce opine-type metallophores 15 mainly to face the host’s nutritional immunity. This is the case of staphylopine, pseudopaline and 16 yersinopine, identified in Staphylococcus aureus, Pseudomonas aeruginosa and Yersinia pestis 17 respectively. These metallophores are synthesized by two (CntLM) or three enzymes (CntKLM), 18 CntM catalyzing the last step of biosynthesis using diverse substrates (pyruvate or α-ketoglutarate), 19 pathway intermediates (xNA or yNA) and cofactors (NADH or NADPH), depending on the species. 20 Here, we explored substrate specificity of CntM by combining bioinformatics and structural analysis 21 with chemical synthesis and enzymatic studies.
    [Show full text]
  • Simple Rules Govern the Diversity of Bacterial Nicotianamine-Like Metallophores
    Simple rules govern the diversity of bacterial nicotianamine-like metallophores Clémentine Laffont, Catherine Brutesco, Christine Hajjar, Gregorio Cullia, Roberto Fanelli, Laurent Ouerdane, Florine Cavelier, Pascal Arnoux To cite this version: Clémentine Laffont, Catherine Brutesco, Christine Hajjar, Gregorio Cullia, Roberto Fanelli, etal.. Simple rules govern the diversity of bacterial nicotianamine-like metallophores. Biochemical Journal, Portland Press, 2019, 476 (15), pp.2221-2233. 10.1042/bcj20190384. cea-02275929 HAL Id: cea-02275929 https://hal-cea.archives-ouvertes.fr/cea-02275929 Submitted on 3 Sep 2019 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. 1 Simple rules govern the diversity of bacterial nicotianamine-like metallophores 2 Clémentine Laffont1, Catherine Brutesco1, Christine Hajjar1, Gregorio Cullia2, Roberto Fanelli2, 3 Laurent Ouerdane3, Florine Cavelier2, Pascal Arnoux1,* 4 1Aix Marseille Univ, CEA, CNRS, BIAM, Saint Paul-Lez-Durance, France F-13108. 5 2Institut des Biomolécules Max Mousseron, IBMM, UMR-5247, CNRS, Université Montpellier, 6 ENSCM , Place Eugène Bataillon, 34095 Montpellier cedex 5, France. 7 3CNRS-UPPA, Laboratoire de Chimie Analytique Bio-inorganique et Environnement, UMR 5254, 8 Hélioparc, 2, Av. Angot 64053 Pau, France. 9 *Correspondance: Pascal Arnoux, Aix Marseille Univ, CEA, CNRS, BIAM, Saint Paul-Lez- 10 Durance, France F-13108; [email protected]; Tel.
    [Show full text]