The Importance of L-Rhamnose Sugar
Total Page:16
File Type:pdf, Size:1020Kb
Load more
Recommended publications
-
Adaptive Laboratory Evolution Enhances Methanol Tolerance and Conversion in Engineered Corynebacterium Glutamicum
ARTICLE https://doi.org/10.1038/s42003-020-0954-9 OPEN Adaptive laboratory evolution enhances methanol tolerance and conversion in engineered Corynebacterium glutamicum Yu Wang 1, Liwen Fan1,2, Philibert Tuyishime1, Jiao Liu1, Kun Zhang1,3, Ning Gao1,3, Zhihui Zhang1,3, ✉ ✉ 1234567890():,; Xiaomeng Ni1, Jinhui Feng1, Qianqian Yuan1, Hongwu Ma1, Ping Zheng1,2,3 , Jibin Sun1,3 & Yanhe Ma1 Synthetic methylotrophy has recently been intensively studied to achieve methanol-based biomanufacturing of fuels and chemicals. However, attempts to engineer platform micro- organisms to utilize methanol mainly focus on enzyme and pathway engineering. Herein, we enhanced methanol bioconversion of synthetic methylotrophs by improving cellular tolerance to methanol. A previously engineered methanol-dependent Corynebacterium glutamicum is subjected to adaptive laboratory evolution with elevated methanol content. Unexpectedly, the evolved strain not only tolerates higher concentrations of methanol but also shows improved growth and methanol utilization. Transcriptome analysis suggests increased methanol con- centrations rebalance methylotrophic metabolism by down-regulating glycolysis and up- regulating amino acid biosynthesis, oxidative phosphorylation, ribosome biosynthesis, and parts of TCA cycle. Mutations in the O-acetyl-L-homoserine sulfhydrylase Cgl0653 catalyzing formation of L-methionine analog from methanol and methanol-induced membrane-bound transporter Cgl0833 are proven crucial for methanol tolerance. This study demonstrates the importance of -
Contig Protein Description Symbol Anterior Posterior Ratio
Table S2. List of proteins detected in anterior and posterior intestine pooled samples. Data on protein expression are mean ± SEM of 4 pools fed the experimental diets. The number of the contig in the Sea Bream Database (http://nutrigroup-iats.org/seabreamdb) is indicated. Contig Protein Description Symbol Anterior Posterior Ratio Ant/Pos C2_6629 1,4-alpha-glucan-branching enzyme GBE1 0.88±0.1 0.91±0.03 0.98 C2_4764 116 kDa U5 small nuclear ribonucleoprotein component EFTUD2 0.74±0.09 0.71±0.05 1.03 C2_299 14-3-3 protein beta/alpha-1 YWHAB 1.45±0.23 2.18±0.09 0.67 C2_268 14-3-3 protein epsilon YWHAE 1.28±0.2 2.01±0.13 0.63 C2_2474 14-3-3 protein gamma-1 YWHAG 1.8±0.41 2.72±0.09 0.66 C2_1017 14-3-3 protein zeta YWHAZ 1.33±0.14 4.41±0.38 0.30 C2_34474 14-3-3-like protein 2 YWHAQ 1.3±0.11 1.85±0.13 0.70 C2_4902 17-beta-hydroxysteroid dehydrogenase 14 HSD17B14 0.93±0.05 2.33±0.09 0.40 C2_3100 1-acylglycerol-3-phosphate O-acyltransferase ABHD5 ABHD5 0.85±0.07 0.78±0.13 1.10 C2_15440 1-phosphatidylinositol phosphodiesterase PLCD1 0.65±0.12 0.4±0.06 1.65 C2_12986 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-1 PLCD1 0.76±0.08 1.15±0.16 0.66 C2_4412 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase gamma-2 PLCG2 1.13±0.08 2.08±0.27 0.54 C2_3170 2,4-dienoyl-CoA reductase, mitochondrial DECR1 1.16±0.1 0.83±0.03 1.39 C2_1520 26S protease regulatory subunit 10B PSMC6 1.37±0.21 1.43±0.04 0.96 C2_4264 26S protease regulatory subunit 4 PSMC1 1.2±0.2 1.78±0.08 0.68 C2_1666 26S protease regulatory subunit 6A PSMC3 1.44±0.24 1.61±0.08 -
Hypoglycemic Activity and Mechanism of the Sulfated Rhamnose Polysaccharides Chromium(III) Complex in Type 2 Diabetic Mice
Bioorganic Chemistry 88 (2019) 102942 Contents lists available at ScienceDirect Bioorganic Chemistry journal homepage: www.elsevier.com/locate/bioorg Hypoglycemic activity and mechanism of the sulfated rhamnose T polysaccharides chromium(III) complex in type 2 diabetic mice Han Yea, Zhaopeng Shenb, Jiefen Cuia, Yujie Zhua, Yuanyuan Lia, Yongzhou Chia, ⁎ Jingfeng Wanga, Peng Wanga, a College of Food Science and Engineering, Ocean University of China, Qingdao 266003, PR China b College of Medicine and Pharmacy, Ocean University of China, Qingdao 266003, PR China ARTICLE INFO ABSTRACT Keywords: The sulfated rhamnose polysaccharides found in Enteromorpha prolifera belong to a class of unique polyanionic Chromium polysaccharides with high chelation capacity. In this study, a complex of sulfated rhamnose polysaccharides with Glucose metabolism chromium(III) (SRPC) was synthesized, and its effect on type 2 diabetes mellitus (T2DM) in mice fed a high-fat, Hypoglycemic high-sucrose diet was investigated. The molecular weight of SRPC is 4.57 kDa, and its chromium content is Mice 28 μg/mg. Results indicated that mice treated by oral administration of SRPC (10 mg/kg and 30 mg/kg body Sulfated rhamnose polysaccharides mass per day) for 11 weeks showed significantly improved oral glucose tolerance, decreased body mass gain, reduced serum insulin levels, and increased tissue glycogen content relative to T2DM mice (p < 0.01). SRPC treatment improved glucose metabolism via activation of the IR/IRS-2/PI3K/PKB/GSK-3β signaling pathway (which is related to glycogen synthesis) and enhanced glucose transport through insulin signaling casca- de–induced GLUT4 translocation. Because of its effectiveness and stability, SRPC could be used as a therapeutic agent for blood glucose control and a promising nutraceutical for T2DM treatment. -
Biosynthèse De Nouveaux Dérivés De L'alpha-Bisabolol Par Une Approche
THÈSE En vue de l’obtention du DOCTORAT DE L’UNIVERSITÉ DE TOULOUSE Délivré par l'Institut National des Sciences Appliquées de Toulouse Présentée et soutenue par Arthur SARRADE-LOUCHEUR Le 30 juin 2020 Biosynthèse de nouveaux dérivés de l'α-bisabolol par une approche de biologie synthèse Ecole doctorale : SEVAB - Sciences Ecologiques, Vétérinaires, Agronomiques et Bioingenieries Spécialité : Ingénieries microbienne et enzymatique Unité de recherche : TBI - Toulouse Biotechnology Institute, Bio & Chemical Engineering Thèse dirigée par Gilles TRUAN et Magali REMAUD-SIMEON Jury Mme Véronique DE BERARDINIS, Rapporteure, Chercheur CEA M. Jean-Etienne BASSARD, Rapporteur, Chargé de Recherche, CNRS Mme Danièle WERCK-REICHHART, Examinatrice, Directeur de Recherche Emérite, CNRS M. Gilles TRUAN, Directeur de thèse, Directeur de Recherche, CNRS Mme Magali REMAUD-SIMEON, Co-directrice de thèse, Professeur des Universités, INSA Mme Fayza DABOUSSI, Présidente, Directeur de Recherche INRAE 2 Author: Arthur Sarrade-Loucheur Year: 2020 Biosynthesis of new α-bisabolol derivatives through a synthetic biology approach The rise of synthetic biology now enables the production of new to nature molecules. In the frame of this thesis we focused on the diversification of the (+)-epi-α-bisabolol scaffold. This molecule coming from the plant Lippia dulcis belongs to the vast family of sesquiterpenes. While sesquiterpenes possess diverse biological activities, (+)-epi-α- bisabolol is the precursor of hernandulcin, an intense sweetener. However, the last oxidative step(s) of the hernandulcin biosynthetic pathway remain elusive. Rather than seeking the native oxidase responsible for hernandulcin synthesis among L. dulcis enzymes we turned our choice towards oxidative enzymes known to be promiscuous and that could functionalize (+)-epi-α-bisabolol in order to i) generate diversity from (+)-epi-α-bisabolol; ii) hopefully identify an oxidative enzyme catalyzing hernandulcin synthesis. -
Structure of L-Rhamnose Isomerase in Complex with L
View metadata, citation and similar papers at core.ac.uk brought to you by CORE provided by Elsevier - Publisher Connector FEBS Open Bio 3 (2013) 35–40 journal homepage: www.elsevier.com/locate/febsopenbio Structure of l-rhamnose isomerase in complex with l-rhamnopyranose demonstrates the sugar-ring opening mechanism and the role of a substrate sub-binding site Hiromi Yoshidaa, Akihide Yoshiharab, Misa Teraokaa, Satoshi Yamashitaa, Ken Izumorib, Shigehiro Kamitoria,* aLife Science Research Center and Faculty of Medicine, Kagawa University, 1750-1 Ikenobe, Miki-cho, Kita-gun, Kagawa 761-0793, Japan bRare Sugar Research Center and Faculty of Agriculture, Kagawa University, Miki-cho, Kagawa 761-0795, Japan article info abstract Article history: L-Rhamnose isomerase (L-RhI) catalyzes the reversible isomerization of L-rhamnose to L-rhamnulose. Received 27 November 2012 Previously determined X-ray structures of L-RhI showed a hydride-shift mechanism for the isomeriza- Accepted 30 November 2012 tion of substrates in a linear form, but the mechanism for opening of the sugar-ring is still unclear. To elucidate this mechanism, we determined X-ray structures of a mutant L-RhI in complex with L- Keywords: rhamnopyranose and D-allopyranose. Results suggest that a catalytic water molecule, which acts as an l-Rhamnose isomerase acid/base catalyst in the isomerization reaction, is likely to be involved in pyranose-ring opening, and Pseudomonas stutzeri Sugar-ring opening mechanism that a newly found substrate sub-binding site in the vicinity of the catalytic site may recognize different Rare sugar anomers of substrates. X-ray structure C 2012 The Authors. -
58. Cross-Induction of the L-Fucose System by L-Rhamnose In
JOURNAL OF BACTERIOLOGY, Aug. 1987, p. 3712-3719 Vol. 169, No. 8 0021-9193/87/083712-08$02.00/0 Copyright © 1987, American Society for Microbiology Cross-Induction of the L-Fucose System by L-Rhamnose in Escherichia coli Y.-M. CHEN,1 J. F. TOBIN,2 Y. ZHU,' R. F. SCHLEIF,2 AND E. C. C. LIN'* Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, Massachusetts 02115,1 and Department ofBiochemistry, Brandeis University, Waltham, Massachusetts 022542 Received 6 January 1987/Accepted 21 May 1987 Dissimilation of L-fucose as a carbon and energy source by Escherichia coli involves a permease, an isomerase, a kinase, and an aldolase encoded by the fuc regulon at minute 60.2. Utilization of L-rhamnose involves a similar set of proteins encoded by the rha operon at minute 87.7. Both pathways lead to the formation of L-lactaldehyde and dihydroxyacetone phosphate. A common NAD-linked oxidoreductase encoded by fucO serves to reduce L-lactaldehyde to L-1,2-propanediol under anaerobic growth conditions, irrespective of whether the aldehyde is derived from fucose or rhamnose. In this study it was shown that anaerobic growth on rhamnose induces expression of not only thefucO gene but also the entirefuc regulon. Rhamnose is unable to induce the fuc genes in mutants defective in rhaA (encoding L-rhamnose isomerase), rhaB (encoding L-rhamnulose kinase), rhaD (encoding L-rhamnulose 1-phosphate aldolase), rhaR (encoding the positive regulator for the rha structural genes), or fucR (encoding the positive regulator for the fuc regulon). Thus, cross-induction of the L-fucose enzymes by rhamnose requires formation of L-lactaldehyde; either the aldehyde itself or the L-fuculose 1-phosphate (known to be an effector) formed from it then interacts with the fucR-encoded protein to induce the fuc regulon. -
Genomic Analysis of Thermophilicbacillus Coagulans
OPEN Genomic analysis of thermophilic Bacillus SUBJECT AREAS: coagulans strains: efficient producers for COMPARATIVE GENOMICS platform bio-chemicals BACTERIAL GENOMICS Fei Su & Ping Xu Received 17 September 2013 State Key Laboratory of Microbial Metabolism, and School of Life Sciences & Biotechnology, Shanghai Jiao Tong University, Shanghai 200240, P. R. China. Accepted 14 January 2014 Microbial strains with high substrate efficiency and excellent environmental tolerance are urgently needed Published for the production of platform bio-chemicals. Bacillus coagulans has these merits; however, little genetic 29 January 2014 information is available about this species. Here, we determined the genome sequences of five B. coagulans strains, and used a comparative genomic approach to reconstruct the central carbon metabolism of this species to explain their fermentation features. A novel xylose isomerase in the xylose utilization pathway was identified in these strains. Based on a genome-wide positive selection scan, the selection pressure on amino Correspondence and acid metabolism may have played a significant role in the thermal adaptation. We also researched the requests for materials immune systems of B. coagulans strains, which provide them with acquired resistance to phages and mobile should be addressed to genetic elements. Our genomic analysis provides comprehensive insights into the genetic characteristics of P.X. ([email protected]. B. coagulans and paves the way for improving and extending the uses of this species. cn) hite biotechnology, the clean industrial technology supported by several predominant political move- ments, will comprise no less than 20% of the chemical industry sales in the United States in 20201.To attempt to meet the dramatic future demands for these materials, researchers have used microbial W 2 strains to produce platform bio-chemicals . -
Capsular Polysaccharide of Azotobacter Agilis' Gary H
JOURNAL OF BACTERIOLOGY Vol. 88, No. 6, p. 1695-1699 Decemnber, 1964 Copyright © 1964 American Society for Microbiology Printed in U.S.A. CAPSULAR POLYSACCHARIDE OF AZOTOBACTER AGILIS' GARY H. COHEN2 AND DONALD B. JOHNSTONE Department of Agricultural Biochemistry, University of Vermont, Burlington, Vermont Received for publication 19 June 1964 ABSTRACT is confined to well-defined capsules. To our COHEN, GARY H. (University of Vermont, Bur- knowledge, no reports have appeared in the lington), AND DONALD B. JOHNSTONE. Capsular literature concerning the chemistry of the extra- polysaccharide of Azotobacter agilis. J. Bacteriol. cellular polysaccharide of A. agilis. 88:1695-1699. 1964.-Capsular polysaccharide from Azotobacter agilis strain 132 was recovered from MATERIALS AND METHODS washed cells by alkaline digestion. The polysac- Growth of the organisms. A. agilis (ATCC charide was purified by centrifugation, repeated 12838) used alcohol precipitation, Sevag deproteinization, and throughout this study was originally treatment with ribonuclease and charcoal-cellu- isolated in this laboratory from water (Johnstone, lose. Methods of isolation and purification ap- 1957) and designated in subsequent reports as peared to provide a polymer showing no evidence strain 132 (Johnstone, Pfeffer, and Blanchard, of heterogeneity when examined by chemical and 1959; Johnstone, 1962b). Burk's nitrogen-free physical methods. Colorimetric, paper chromato- broth (Wilson and Knight, 1952) at pH 7.0 graphic, and enzymatic analyses on both intact supplemented with 2% sucrose was inoculated and acid-hydrolyzed polysaccharide indicated with cells growing in the logarithmic phase. that the polymer contained galactose and rham- Cultures were incubated at 31 C in 7.5-liter New nose at a molar ratio of approximately 1.0:0.7. -
The Immunomodulatory Properties of L-Rhamnose
The Immunomodulatory Properties of L-Rhamnose Mimmi Lundahl M.Sc. Immunology Supervisors: Prof. Ed Lavelle and Prof. Eoin Scanlan Report prepared for the degree of Doctor of Philosophy, Immunology School of Biochemistry and Immunology, School of Chemistry Trinity Biomedical Sciences Institute Trinity College Dublin 2020 I hereby certify that this report is entirely my own work, and that the contents have not been published elsewhere in paper or electronic form unless indicated through referencing. i Abstract L-Rhamnose is a non-mammalian monosaccharide ubiquitously found on the surface of both commensal and pathogenic bacteria. Previous publications had identified that L-rhamnose-rich Mycobacterium tuberculosis glycolipids, and their structural derivatives, pHBADs, were able to aid this pathogen’s ability to escape immune elimination by repressing protective immune responses. A key immune cell for combatting M. tuberculosis is the macrophage, an innate immune cell present in essentially all tissues. A distinguishing feature of macrophages is their polarisation combined with plasticity; the ability to adopt distinct phenotypes. These are simplified into the pro-inflammatory and bactericidal, “classically activated” M1 macrophages and the “alternatively activated” Th2-promoting and anti-inflammatory M2 macrophages. To combat M. tuberculosis, M1 macrophage activation is critical. In the research presented herein, it is demonstrated that L-rhamnose skews macrophage polarisation away from a bactericidal phenotype and enhances M2 characteristics. Furthermore, it is revealed that L-rhamnose is capable of inducing macrophage innate memory, causing responses elicited by subsequent stimuli, a week after L-rhamnose incubation, to yield a more anti-inflammatory and anti-bactericidal profile. This is presented both as induction of the regulatory cytokine IL-10, as well as reduced expression of iNOS mRNA. -
Generate Metabolic Map Poster
Authors: Pallavi Subhraveti Ron Caspi Quang Ong Peter D Karp An online version of this diagram is available at BioCyc.org. Biosynthetic pathways are positioned in the left of the cytoplasm, degradative pathways on the right, and reactions not assigned to any pathway are in the far right of the cytoplasm. Transporters and membrane proteins are shown on the membrane. Ingrid Keseler Periplasmic (where appropriate) and extracellular reactions and proteins may also be shown. Pathways are colored according to their cellular function. Gcf_900114035Cyc: Amycolatopsis sacchari DSM 44468 Cellular Overview Connections between pathways are omitted for legibility. -
WO 2014/207087 Al 31 December 2014 (31.12.2014) P O P C T
(12) INTERNATIONAL APPLICATION PUBLISHED UNDER THE PATENT COOPERATION TREATY (PCT) (19) World Intellectual Property Organization International Bureau (10) International Publication Number (43) International Publication Date WO 2014/207087 Al 31 December 2014 (31.12.2014) P O P C T (51) International Patent Classification: Seville (ES). GUTIERREZ GOMEZ, Pablo; Campus C12N 9/00 (2006.01) C12N 9/90 (2006.01) Palmas Altas, Calle Energia Solar 1, E-41014 Seville (ES). C12N 9/02 (2006.01) C12P 5/02 (2006.01) (74) Agent: NEDERLANDSCH OCTROOIBUREAU; J.W. C12N 9/10 (2006.01) C12P 7/76 (2006.01) Frisolaan 13, NL-2517 JS The Hague (NL). C12N 9/12 (2006.01) C12P 7/64 (2006.01) C12N 9/88 (2006.01) C12N 1/1 9 (2006.01) (81) Designated States (unless otherwise indicated, for every kind of national protection available): AE, AG, AL, AM, (21) International Application Number: AO, AT, AU, AZ, BA, BB, BG, BH, BN, BR, BW, BY, PCT/EP2014/063484 BZ, CA, CH, CL, CN, CO, CR, CU, CZ, DE, DK, DM, (22) International Filing Date: DO, DZ, EC, EE, EG, ES, FI, GB, GD, GE, GH, GM, GT, 26 June 2014 (26.06.2014) HN, HR, HU, ID, IL, IN, IR, IS, JP, KE, KG, KN, KP, KR, KZ, LA, LC, LK, LR, LS, LT, LU, LY, MA, MD, ME, (25) Filing Language: English MG, MK, MN, MW, MX, MY, MZ, NA, NG, NI, NO, NZ, (26) Publication Language: English OM, PA, PE, PG, PH, PL, PT, QA, RO, RS, RU, RW, SA, SC, SD, SE, SG, SK, SL, SM, ST, SV, SY, TH, TJ, TM, (30) Priority Data: TN, TR, TT, TZ, UA, UG, US, UZ, VC, VN, ZA, ZM, 13382241 .1 26 June 2013 (26.06.2013) EP ZW. -
Characterization of Ribose-5-Phosphate Isomerase B from Newly Isolated Strain Ochrobactrum Sp
J. Microbiol. Biotechnol. (2018), 28(7), 1122–1132 https://doi.org/10.4014/jmb.1802.02021 Research Article Review jmb Characterization of Ribose-5-Phosphate Isomerase B from Newly Isolated Strain Ochrobactrum sp. CSL1 Producing L-Rhamnulose from L-Rhamnose Min Shen1†, Xin Ju1†, Xinqi Xu2, Xuemei Yao1, Liangzhi Li1*, Jiajia Chen1, Cuiying Hu1, Jiaolong Fu1, and Lishi Yan1 1School of Chemistry, Biology, and Material Engineering, Suzhou University of Science and Technology, Suzhou 215009, P.R. China 2Fujian Key Laboratory of Marine Enzyme Engineering, Fuzhou University, Fujian 350116, P.R. China Received: February 14, 2018 Revised: April 12, 2018 In this study, we attempted to find new and efficient microbial enzymes for producing rare Accepted: April 13, 2018 sugars. A ribose-5-phosphate isomerase B (OsRpiB) was cloned, overexpressed, and First published online preliminarily purified successfully from a newly screened Ochrobactrum sp. CSL1, which could May 8, 2018 catalyze the isomerization reaction of rare sugars. A study of its substrate specificity showed *Corresponding author that the cloned isomerase (OsRpiB) could effectively catalyze the conversion of L-rhamnose to Phone: +86-512-68056493; L-rhamnulose, which was unconventional for RpiB. The optimal reaction conditions (50oC, Fax: +86-512-68418431; 2+ E-mail: [email protected] pH 8.0, and 1 mM Ca ) were obtained to maximize the potential of OsRpiB in preparing L-rhamnulose. The catalytic properties of OsRpiB, including Km, kcat, and catalytic efficiency † These authors contributed (k /K ), were determined as 43.47 mM, 129.4 sec-1, and 2.98 mM/sec. The highest conversion equally to this work.