DOCSLIB.ORG

(12) Patent Application Publication (10) Pub. No.: US 2013/0089535 A1 Yamashiro Et Al

Total Page：16

File Type：pdf, Size：1020Kb

Download full-text PDF Read full-text
(12) Patent Application Publication (10) Pub. No.: US 2013/0089535 A1 Yamashiro Et Al US 2013 0089535A1 (19) United States (12) Patent Application Publication (10) Pub. No.: US 2013/0089535 A1 Yamashiro et al. (43) Pub. Date: Apr. 11, 2013 (54) AGENT FOR REDUCING ACETALDEHYDE Publication Classification NORAL CAVITY (51) Int. Cl. (75) Inventors: Kan Yamashiro, Kakamigahara-shi (JP); A68/66 (2006.01) Takahumi Koyama, Kakamigahara-shi A638/51 (2006.01) (JP) A61O 11/00 (2006.01) A638/44 (2006.01) Assignee: AMANOENZYME INC., Nagoya-shi (52) U.S. Cl. (73) CPC. A61K 8/66 (2013.01); A61K 38/44 (2013.01); (JP) A61 K38/51 (2013.01); A61O II/00 (2013.01) (21) Appl. No.: 13/703,451 USPC .......... 424/94.4; 424/94.5; 435/191: 435/232 (22) PCT Fled: Jun. 7, 2011 (57) ABSTRACT Disclosed herein is a novel enzymatic agent effective in (86) PCT NO.: PCT/UP2011/062991 reducing acetaldehyde in the oral cavity. It has been found S371 (c)(1), that an aldehyde dehydrogenase derived from a microorgan (2), (4) Date: Dec. 11, 2012 ism belonging to the genus Saccharomyces and a threonine aldolase derived from Escherichia coli are effective in reduc (30) Foreign Application Priority Data ing low concentrations of acetaldehyde. Therefore, an agent for reducing acetaldehyde in the oral cavity is provided, Jun. 19, 2010 (JP) ................................. 2010-140O26 which contains these enzymes as active ingredients. Patent Application Publication Apr. 11, 2013 Sheet 1 of 2 US 2013/0089535 A1 FIG 1) 10.5 1 0 9.9.5 8. 5 CONTROL TA AD (BSA) ENZYME Patent Application Publication Apr. 11, 2013 Sheet 2 of 2 US 2013/0089535 A1 FIG 2) 110 the CONTROL (BSA) 100 354. 0.0O O 2 4 6 8 10 2 14 16 18 20 TIME (min) US 2013/0O89535 A1 Apr. 11, 2013 AGENT FOR REDUCING ACETALDEHYDE lizes the property of L-cysteine to bind to acetaldehyde. How NORAL CAVITY ever, this reaction is a reversible reaction, and therefore there is a possibility that acetaldehyde is again liberated. Further, TECHNICAL FIELD L-cysteine itself has a distinctive smell, which makes it dif ficult to apply L-cysteine to oral care products. On the other 0001. The present invention relates to an agent for reduc hand, the aldehyde oxidase derived from a microorganism is ing acetaldehyde in the oral cavity. More specifically, the advantageous in that it does not require a coenzyme, but there present invention relates to an agent that reduces acetalde is a problem that hazardous hydrogen peroxide is generated hyde in the oral cavity by an acetaldehyde-degrading enzyme by a reaction involving the aldehyde oxidase. Further, the and a use thereof. This application is based upon and claims reported aldehyde oxidase derived from a microorganism the benefit of priority from prior Japanese Patent Application exhibits activity under acidic conditions (at around pH 3.5), No. 2010-140026 filed on Jun. 19, 2010 in Japan, the entire but its reactivity under physiological conditions is unknown. contents of which are incorporated herein by reference. Furthermore, the confirmed reactivity of the enzyme is noth ing more than reactivity only toward relatively high concen BACKGROUND ART trations (in the order of mM) of substrate. The concentration 0002. In recent years, it has been reported that acetalde of acetaldehyde contained in saliva is usually in the order of hyde in saliva not only causes bad breath but also increases uM, but the reactivity of an enzymatic reaction is lowered the risk of diseases Such as upper digestive system cancers. when the concentration of a substrate is Kim or less. There Acetaldehyde in saliva is derived from various sources, but in fore, there is a demand for development of an enzyme that has recent years, acetaldehyde resulting from alcohol metabolism Sufficientactivity against low concentrations of substrate. It is during alcohol drinking or from Smoking or acetaldehyde to be noted that it has been reported that a superoxide dismu derived from periodontal pathogens in the mouth has been tase derived from a microorganism belonging to the genus known as a typical example and regarded as a problem. Gluconobacter exhibits acetaldehyde-degrading activity 0003. Among them, acetaldehyde produced as a metabolic (Patent Document 2). product in the course of alcoholysis accumulates in Saliva during alcohol drinking, which constitutes a risk factor for PRIOR ART DOCUMENTS esophageal cancer and stomach cancer. Particularly, it has been reported that in the case of flushers (people whose Patent Documents genome type of aldehyde dehydrogenase is AG or GG), the 0008 Patent Document 1: JP 2010-57482 A concentration of acetaldehyde in Saliva is increased up to almost 100 uM by alcohol drinking. 0009 Patent Document 2: JP 2010-110248 A 0004. It is also known that the concentration of acetalde Non-Patent Document hyde in saliva is increased by Smoking. It is considered that one of its causes is acetaldehyde contained in tobacco Smoke 0.010 Non-Patent Document 1: Salaspuro V. Hietala J, (Filtration of tobacco smoke (written by OtaniY), The history Kaihovaara P. et al., Int J. Cancer. 2002 Jan. 20; 97(3): of smoking research: 1996-2005, edited by Misu Y. Agari I, 361-4. Ohwada H. Nakao K, and Itani S, Smoking Research Foun dation, 2007). SUMMARY OF THE INVENTION 0005. A research group of Tokyo University has reported that drinking of one or more cans of beer per day and Smoking Problems to be Solved by the Invention makes the risk of esophageal cancer for flushers up to 190 0011. As has been described above, it has been found that times higher than that for people who are not flushers and do acetaldehyde in the oral cavity (in the mouth) poses a risk for not drink alcohol and smoke (Cui R, Kamatani Y, et. al. health problems, and therefore there is a demand for devel Functional variants in ADH1B and ALDH2 coupled with opment of oral care products that can degrade and remove alcohol and Smoking synergistically enhance esophageal can such acetaldehyde. It is therefore an object of the present cer risk. Gastroenterology 137:1768-1775 (2009)). invention to provide a novel enzyme preparation effective in 0006. It has been found by epidemiological studies that reducing acetaldehyde in the oral cavity. Some bacteria present in the mouth synthesize acetaldehyde and acetaldehyde derived from such bacteria is a cause of bad Means for Solving the Problems breath or a risk factor for upper digestive system cancers such as esophageal cancer and stomach cancer (which was 0012. The present inventors have intensively studied using reported at the annual meeting of the Japanese Cancer Asso artificial saliva to find enzymes effective in reducing acetal ciation in 2009). According to the results of an epidemiologi dehyde in the oral cavity. As a result, the present inventors cal study performed by Aichi Cancer Center Research Insti have found that an aldehyde dehydrogenase and a threonine tute (in Nagoya City) on about 3,800 people, people who aldolase exhibit excellent activity at low substrate concentra brush teeth twice or more a day have a lower risk for oral tions, which has led to the completion of the present inven cancer or esophageal cancer by 30% than people who brush tion. The present invention includes the following (1) to (10). teeth once a day. It is considered that the reason for this is that 0013 (1) An agent for reducing acetaldehyde in an oral oral bacteria that produce acetaldehyde and produced acetal cavity, including an aldehyde dehydrogenase or a threonine dehyde are washed away by tooth brushing. aldolase. 0007 Meanwhile, as means for removing acetaldehyde in 0014 (2) The agent for reducing acetaldehyde in an oral saliva or foods, one using L-cysteine (Non-Patent Document cavity according to (1), wherein the aldehyde dehydrogenase 1) and one using an aldehyde oxidase derived from a micro is derived from a microorganism belonging to the genus Sac organism (Patent Document 1) are known. The former uti charomyces. US 2013/0O89535 A1 Apr. 11, 2013 00.15 (3) The agent for reducing acetaldehyde in an oral Escherichia coli (see, for example, Eur. J. Biochem, 255, cavity according to (2), wherein the microorganism belong 220-226 (1998)) is preferably used. ing to the genus Saccharomyces is Saccharomyces cerevisiae. 0028. The concentration of acetaldehyde (substrate) at 0016 (4) The agent for reducing acetaldehyde in an oral which the acetaldehyde-reducing agent according to the cavity according to (1), wherein the threonine aldolase is present invention can act is not particularly limited, but is derived from Escherichia coli. preferably in the range of 1 uM to 1 mM, more preferably in 0017 (5) The agent for reducing acetaldehyde in an oral the range of 1 uM to 100 uM. It is to be noted that the strength cavity according to any one of (1) to (4), which exhibits (degree) of activity of the acetaldehyde-reducing agent degradation activity against acetaldehyde at a substrate con according to the present invention is not particularly limited. centration of 1 uM to 1 mM. 0029. The acetaldehyde-reducing agent according to the 0018 (6) The agent for reducing acetaldehyde in an oral present invention may contain, in addition to the active ingre cavity according to any one of (1) to (4), which exhibits dient (the aldehyde dehydrogenase or the threonine aldolase), degradation activity against acetaldehyde at a substrate con an excipient, a buffering agent, a suspension agent, a stabi centration of 1 uM to 100 uM. lizer, a pH adjuster, a preservative, an antiseptic, a perfume, a 0019 (7) An oral composition including the agent for thickener, fat and oil, a gloss agent, a binder, a binder rein reducing acetaldehyde in an oral cavity according to any one forcement, an emulsion stabilizer, a normal Saline solution, of (1) to (6).
Load more

Recommended publications
  • Organic & Biomolecular Chemistry
    Organic & Biomolecular Chemistry Accepted Manuscript This is an Accepted Manuscript, which has been through the Royal Society of Chemistry peer review process and has been accepted for publication. Accepted Manuscripts are published online shortly after acceptance, before technical editing, formatting and proof reading. Using this free service, authors can make their results available to the community, in citable form, before we publish the edited article. We will replace this Accepted Manuscript with the edited and formatted Advance Article as soon as it is available. You can find more information about Accepted Manuscripts in the Information for Authors. Please note that technical editing may introduce minor changes to the text and/or graphics, which may alter content. The journal’s standard Terms & Conditions and the Ethical guidelines still apply. In no event shall the Royal Society of Chemistry be held responsible for any errors or omissions in this Accepted Manuscript or any consequences arising from the use of any information it contains. www.rsc.org/obc Page 1 of 14 Organic & Biomolecular Chemistry Enantioselective imine reduction catalyzed by imine reductases and artificial metalloenzymes Daniela Gamenara a* , Pablo Domínguez de María b,c* Manuscript a: Organic Chemistry Department. Universidad de la República (UdelaR). Gral. Flores 2124. 11800 Montevideo, Uruguay. b: Institut für Technische und Makromolekulare Chemie (ITMC), Accepted RWTH Aachen University. Worringerweg 1. 52074 Aachen, Germany. c: Present address: Sustainable Momentum . Ap. Correos 3517. 35004, Las Palmas de Gran Canaria; Canary Islands; Spain. Chemistry Biomolecular & * Corresponding Authors: Dr. Daniela Gamenara. Tel.: +598 29247881; Fax: +598 29241906; E-mail: [email protected] ; Dr.
    [Show full text]
  • (12) Patent Application Publication (10) Pub. No.: US 2012/0028333 A1 Piatesi Et Al
    US 20120028333A1 (19) United States (12) Patent Application Publication (10) Pub. No.: US 2012/0028333 A1 Piatesi et al. (43) Pub. Date: Feb. 2, 2012 (54) USE OF ENZYMES TO REDUCE ALDEHYDES (30) Foreign Application Priority Data FROMALDEHYDE-CONTAINING PRODUCTS Apr. 7, 2009 (EP) .................................. O9157522.5 Publication Classification (76) Inventors: Andrea Piatesi, Mannheim (DE); (51) Int. Cl. Tilo Habicher, Speyer (DE); CI2N 9/02 (2006.01) Michael Bischel, Worms (DE); CI2N I/00 (2006.01) Li-Wen Wang, Mannheim (DE): CI2N 15/63 (2006.01) Jirgen Reichert, Limburgerhof A62D 3/02 (2007.01) (DE); Rainer Packe-Wirth, C7H 2L/04 (2006.01) Trostberg (DE); Kai-Uwe (52) U.S. Cl. ... 435/189: 435/262:536/23.2:435/320.1; Baldenius, Heidelberg (DE); Erich 435/243 Kromm, Weisenheim am Sand (57) ABSTRACT (DE); Stefan Häfner, Speyer (DE); Carsten Schwalb. Mannheim (DE); The invention relates to the use of an enzyme preparation Hans Wolfgang Höffken, which catalyzes the degradation of formaldehyde for reduc Ludwigshafen (DE) ing the formaldehyde content in a formaldehyde-containing formulation. In a preferred embodiment, the enzyme prepa ration contains a formaldehyde dismutase from a Pseudomo (21) Appl. No.: 13/262,662 nas putida Strain. Further, the invention refers to a process for reducing the formaldehyde content in cross-linking agents for textile finishing or in polymer dispersions used, e.g. in con (22) PCT Filed: Mar. 31, 2010 struction chemistry. Further the invention relates to the use of an enzyme preparation which catalyzes the degradation of (86). PCT No.: PCT/EP1OAS4284 aldehydes for reducing the formaldehyde content in an alde hyde-containing formulation.
    [Show full text]
  • Supplemental Methods
    Supplemental Methods: Sample Collection Duplicate surface samples were collected from the Amazon River plume aboard the R/V Knorr in June 2010 (4 52.71’N, 51 21.59’W) during a period of high river discharge. The collection site (Station 10, 4° 52.71’N, 51° 21.59’W; S = 21.0; T = 29.6°C), located ~ 500 Km to the north of the Amazon River mouth, was characterized by the presence of coastal diatoms in the top 8 m of the water column. Sampling was conducted between 0700 and 0900 local time by gently impeller pumping (modified Rule 1800 submersible sump pump) surface water through 10 m of tygon tubing (3 cm) to the ship's deck where it then flowed through a 156 µm mesh into 20 L carboys. In the lab, cells were partitioned into two size fractions by sequential filtration (using a Masterflex peristaltic pump) of the pre-filtered seawater through a 2.0 µm pore-size, 142 mm diameter polycarbonate (PCTE) membrane filter (Sterlitech Corporation, Kent, CWA) and a 0.22 µm pore-size, 142 mm diameter Supor membrane filter (Pall, Port Washington, NY). Metagenomic and non-selective metatranscriptomic analyses were conducted on both pore-size filters; poly(A)-selected (eukaryote-dominated) metatranscriptomic analyses were conducted only on the larger pore-size filter (2.0 µm pore-size). All filters were immediately submerged in RNAlater (Applied Biosystems, Austin, TX) in sterile 50 mL conical tubes, incubated at room temperature overnight and then stored at -80oC until extraction. Filtration and stabilization of each sample was completed within 30 min of water collection.
    [Show full text]
  • Supplementary Table S4. FGA Co-Expressed Gene List in LUAD
    Supplementary Table S4. FGA co-expressed gene list in LUAD tumors Symbol R Locus Description FGG 0.919 4q28 fibrinogen gamma chain FGL1 0.635 8p22 fibrinogen-like 1 SLC7A2 0.536 8p22 solute carrier family 7 (cationic amino acid transporter, y+ system), member 2 DUSP4 0.521 8p12-p11 dual specificity phosphatase 4 HAL 0.51 12q22-q24.1histidine ammonia-lyase PDE4D 0.499 5q12 phosphodiesterase 4D, cAMP-specific FURIN 0.497 15q26.1 furin (paired basic amino acid cleaving enzyme) CPS1 0.49 2q35 carbamoyl-phosphate synthase 1, mitochondrial TESC 0.478 12q24.22 tescalcin INHA 0.465 2q35 inhibin, alpha S100P 0.461 4p16 S100 calcium binding protein P VPS37A 0.447 8p22 vacuolar protein sorting 37 homolog A (S. cerevisiae) SLC16A14 0.447 2q36.3 solute carrier family 16, member 14 PPARGC1A 0.443 4p15.1 peroxisome proliferator-activated receptor gamma, coactivator 1 alpha SIK1 0.435 21q22.3 salt-inducible kinase 1 IRS2 0.434 13q34 insulin receptor substrate 2 RND1 0.433 12q12 Rho family GTPase 1 HGD 0.433 3q13.33 homogentisate 1,2-dioxygenase PTP4A1 0.432 6q12 protein tyrosine phosphatase type IVA, member 1 C8orf4 0.428 8p11.2 chromosome 8 open reading frame 4 DDC 0.427 7p12.2 dopa decarboxylase (aromatic L-amino acid decarboxylase) TACC2 0.427 10q26 transforming, acidic coiled-coil containing protein 2 MUC13 0.422 3q21.2 mucin 13, cell surface associated C5 0.412 9q33-q34 complement component 5 NR4A2 0.412 2q22-q23 nuclear receptor subfamily 4, group A, member 2 EYS 0.411 6q12 eyes shut homolog (Drosophila) GPX2 0.406 14q24.1 glutathione peroxidase
    [Show full text]
  • Letters to Nature
    letters to nature Received 7 July; accepted 21 September 1998. 26. Tronrud, D. E. Conjugate-direction minimization: an improved method for the re®nement of macromolecules. Acta Crystallogr. A 48, 912±916 (1992). 1. Dalbey, R. E., Lively, M. O., Bron, S. & van Dijl, J. M. The chemistry and enzymology of the type 1 27. Wolfe, P. B., Wickner, W. & Goodman, J. M. Sequence of the leader peptidase gene of Escherichia coli signal peptidases. Protein Sci. 6, 1129±1138 (1997). and the orientation of leader peptidase in the bacterial envelope. J. Biol. Chem. 258, 12073±12080 2. Kuo, D. W. et al. Escherichia coli leader peptidase: production of an active form lacking a requirement (1983). for detergent and development of peptide substrates. Arch. Biochem. Biophys. 303, 274±280 (1993). 28. Kraulis, P.G. Molscript: a program to produce both detailed and schematic plots of protein structures. 3. Tschantz, W. R. et al. Characterization of a soluble, catalytically active form of Escherichia coli leader J. Appl. Crystallogr. 24, 946±950 (1991). peptidase: requirement of detergent or phospholipid for optimal activity. Biochemistry 34, 3935±3941 29. Nicholls, A., Sharp, K. A. & Honig, B. Protein folding and association: insights from the interfacial and (1995). the thermodynamic properties of hydrocarbons. Proteins Struct. Funct. Genet. 11, 281±296 (1991). 4. Allsop, A. E. et al.inAnti-Infectives, Recent Advances in Chemistry and Structure-Activity Relationships 30. Meritt, E. A. & Bacon, D. J. Raster3D: photorealistic molecular graphics. Methods Enzymol. 277, 505± (eds Bently, P. H. & O'Hanlon, P. J.) 61±72 (R. Soc. Chem., Cambridge, 1997).
    [Show full text]
  • 2021 Code Changes Reference Guide
    Boston University Medical Group 2021 CPT Code Changes Reference Guide Page 1 of 51 Background Current Procedural Terminology (CPT) was created by the American Medical Association (AMA) in 1966. It is designed to be a means of effective and dependable communication among physicians, patients, and third-party payers. CPT provides a uniform coding scheme that accurately describes medical, surgical, and diagnostic services. CPT is used for public and private reimbursement systems; development of guidelines for medical care review; as a basis for local, regional, and national utilization comparisons; and medical education and research. CPT Category I codes describe procedures and services that are consistent with contemporary medical practice. Category I codes are five-digit numeric codes. CPT Category II codes facilitate data collection for certain services and test results that contribute to positive health outcomes and quality patient care. These codes are optional and used for performance management. They are alphanumeric five-digit codes with the alpha character F in the last position. CPT Category III codes represent emerging technologies. They are alphanumeric five-digit codes with the alpha character T in the last position. The CPT Editorial Panel, appointed by the AMA Board of Trustees, is responsible for maintaining and updating the CPT code set. Purpose The AMA makes annual updates to the CPT code set, effective January 1. These updates include deleted codes, revised codes, and new codes. It’s important for providers to understand the code changes and the impact those changes will have to systems, workflow, reimbursement, and RVUs. This document is meant to assist you with this by providing a summary of the changes; a detailed breakdown of this year’s CPT changes by specialty, and HCPCS Updates for your reference.
    [Show full text]
  • Product Sheet Info
    Master Clone List for NR-19279 ® Vibrio cholerae Gateway Clone Set, Recombinant in Escherichia coli, Plates 1-46 Catalog No. NR-19279 Table 1: Vibrio cholerae Gateway® Clones, Plate 1 (NR-19679) Clone ID Well ORF Locus ID Symbol Product Accession Position Length Number 174071 A02 367 VC2271 ribD riboflavin-specific deaminase NP_231902.1 174346 A03 336 VC1877 lpxK tetraacyldisaccharide 4`-kinase NP_231511.1 174354 A04 342 VC0953 holA DNA polymerase III, delta subunit NP_230600.1 174115 A05 388 VC2085 sucC succinyl-CoA synthase, beta subunit NP_231717.1 174310 A06 506 VC2400 murC UDP-N-acetylmuramate--alanine ligase NP_232030.1 174523 A07 132 VC0644 rbfA ribosome-binding factor A NP_230293.2 174632 A08 322 VC0681 ribF riboflavin kinase-FMN adenylyltransferase NP_230330.1 174930 A09 433 VC0720 phoR histidine protein kinase PhoR NP_230369.1 174953 A10 206 VC1178 conserved hypothetical protein NP_230823.1 174976 A11 213 VC2358 hypothetical protein NP_231988.1 174898 A12 369 VC0154 trmA tRNA (uracil-5-)-methyltransferase NP_229811.1 174059 B01 73 VC2098 hypothetical protein NP_231730.1 174075 B02 82 VC0561 rpsP ribosomal protein S16 NP_230212.1 174087 B03 378 VC1843 cydB-1 cytochrome d ubiquinol oxidase, subunit II NP_231477.1 174099 B04 383 VC1798 eha eha protein NP_231433.1 174294 B05 494 VC0763 GTP-binding protein NP_230412.1 174311 B06 314 VC2183 prsA ribose-phosphate pyrophosphokinase NP_231814.1 174603 B07 108 VC0675 thyA thymidylate synthase NP_230324.1 174474 B08 466 VC1297 asnS asparaginyl-tRNA synthetase NP_230942.2 174933 B09 198
    [Show full text]
  • Properties of Formaldehyde Dismutation Catalyzing Enzymeof
    Agric. Biol. Chem., 48 (8), 2017-2023, 1984 2017 Properties of Formaldehyde Dismutation Catalyzing Enzymeof Pseudomonas putida F61 Nobuo Kato, Hisataka Kobayashi, Masayuki Shimao and Chikahiro Sakazawa Department of Environmental Chemistry and Technology, Tottori University, Tottori 680, Japan Received January 9, 1984 Twoforms of formaldehyde dismutase distinguishable on disc-gel electrophoresis were isolated from the cell-free extract of Pseudomonasputida ¥61. The mobilities on SDS-gel electrophoresis and the NH2-terminal amino acids (arginine) of the two enzyme species were identical. The COOH- terminal amino acid sequence was found to be -Ser-Gly-Lys. The enzyme was inhibited by carbonyl, reducing and sulfhydryl reagents. The enzyme catalyzed the cross-dismutation reaction between formaldehyde and an aldehyde, such as propionaldehyde, acrolein, butyraldehyde, isobutyraldehyde and crotonaldehyde. The enzyme also catalyzed a coupled oxidoreduction between an alcohol and an aldehyde (RCH2OH+ R CHO^RCHO+R CH2OH) without addition of an electron acceptor. Aliphatic alcohols and aldehydes of C2 to C4 were utilized in this reaction. In the preceding study,1} we found an en- (E; formaldehyde dismutase, X; unknown zyme, which catalyzed dismutation of form- prosthetic group, and XH2; its reduced form.) aldehyde to form equimolar amounts of meth- Furthermore, we have found that the enzyme anol and formic acid, in Pseudomonas putida catalyzes a unique alcohol: aldehyde oxido- F61. The enzyme, given the trivial name of reduction reaction: formaldehyde dismutase, was purified and RCH2OH+R CHO >RCHO+R CH2OH partially characterized. On the other hand, mammalian alcohol dehydrogenase (EC In this work, we describe more detailed 1.1.1.1) was reported to catalyze formalde- properties of this enzyme and its substrate hyde dismutation on the addition of a cata- specificities in the cross-dismutation and al- lytic amount of NAD+or one of its deriva- cohol: aldehyde oxidoreduction reactions.
    [Show full text]
  • University of Groningen Physiology and Biochemistry of Primary Alcohol
    University of Groningen Physiology and biochemistry of primary alcohol oxidation in the gram-positive bacteria "amycolatopsis methanolica" and "bacillus methanolicus" Hektor, Harm Jan IMPORTANT NOTE: You are advised to consult the publisher's version (publisher's PDF) if you wish to cite from it. Please check the document version below. Document Version Publisher's PDF, also known as Version of record Publication date: 1997 Link to publication in University of Groningen/UMCG research database Citation for published version (APA): Hektor, H. J. (1997). Physiology and biochemistry of primary alcohol oxidation in the gram-positive bacteria "amycolatopsis methanolica" and "bacillus methanolicus". s.n. Copyright Other than for strictly personal use, it is not permitted to download or to forward/distribute the text or part of it without the consent of the author(s) and/or copyright holder(s), unless the work is under an open content license (like Creative Commons). The publication may also be distributed here under the terms of Article 25fa of the Dutch Copyright Act, indicated by the “Taverne” license. More information can be found on the University of Groningen website: https://www.rug.nl/library/open-access/self-archiving-pure/taverne- amendment. Take-down policy If you believe that this document breaches copyright please contact us providing details, and we will remove access to the work immediately and investigate your claim. Downloaded from the University of Groningen/UMCG research database (Pure): http://www.rug.nl/research/portal. For technical reasons the number of authors shown on this cover page is limited to 10 maximum. Download date: 30-09-2021 Chapter 2 Formaldehyde dismutase activities in Gram-positive bacteria oxidizing methanol L.V.
    [Show full text]
  • Fermentation of Acetylene by an Obligate Anaerobe, Pelobacter Acetylenicus Sp
    Archives of Arch Microbiol (1985) 142: 295- 301 Microbiology Springer-Verlag 1985 Fermentation of acetylene by an obligate anaerobe, Pelobacter acetylenicus sp. nov. * Bernhard Schink Fakult/it ffir Biologie, Universit/it Konstanz, Postfach 5560, D-7750 Konstanz, Federal Republic of Germany Abstract. Four strains of strictly anaerobic Gram-negative tion reactions (Schink 1985a). No significant anaerobic rod-shaped non-sporeforming bacteria were enriched and degradation could be observed with ethylene (ethene), the isolated from marine and freshwater sediments with acety- most simple unsaturated hydrocarbon (Schink 1985 a, b). lene (ethine) as sole source of carbon and energy. Acetylene, It was reported recently that also acetylene can be metab- acetoin, ethanolamine, choline, 1,2-propanediol, and glyc- olized in the absence of molecular oxygen (Watanabe and erol were the only substrates utilized for growth, the latter de Guzman 1980). Enrichment cultures with acetylene as two only in the presence of small amounts of acetate. Sub- sole carbon source were obtained in mineral media with strates were fermented by disproportionation to acetate and sulfate as electron acceptor, and acetate could be identified ethanol or the respective higher acids and alcohols. No as an intermediary metabolite (Culbertson et al. 1981). How- cytochromes were detectable; the guanine plus cytosine ever, these enrichment cultures were difficult to maintain, content of the DNA was 57.1 _+ 0.2 tool%. Alcohol dehy- and the acetylene-degrading bacteria could not be identified drogenase, aldehyde dehydrogenase, phosphate acetyl- (C. W. Culbertson and R. S. Oremland, Abstr. 3rd Int. transferase, and acetate kinase were found in high activities Syrup.
    [Show full text]
  • Supplementary Informations SI2. Supplementary Table 1
    Supplementary Informations SI2. Supplementary Table 1. M9, soil, and rhizosphere media composition. LB in Compound Name Exchange Reaction LB in soil LBin M9 rhizosphere H2O EX_cpd00001_e0 -15 -15 -10 O2 EX_cpd00007_e0 -15 -15 -10 Phosphate EX_cpd00009_e0 -15 -15 -10 CO2 EX_cpd00011_e0 -15 -15 0 Ammonia EX_cpd00013_e0 -7.5 -7.5 -10 L-glutamate EX_cpd00023_e0 0 -0.0283302 0 D-glucose EX_cpd00027_e0 -0.61972444 -0.04098397 0 Mn2 EX_cpd00030_e0 -15 -15 -10 Glycine EX_cpd00033_e0 -0.0068175 -0.00693094 0 Zn2 EX_cpd00034_e0 -15 -15 -10 L-alanine EX_cpd00035_e0 -0.02780553 -0.00823049 0 Succinate EX_cpd00036_e0 -0.0056245 -0.12240603 0 L-lysine EX_cpd00039_e0 0 -10 0 L-aspartate EX_cpd00041_e0 0 -0.03205557 0 Sulfate EX_cpd00048_e0 -15 -15 -10 L-arginine EX_cpd00051_e0 -0.0068175 -0.00948672 0 L-serine EX_cpd00054_e0 0 -0.01004986 0 Cu2+ EX_cpd00058_e0 -15 -15 -10 Ca2+ EX_cpd00063_e0 -15 -100 -10 L-ornithine EX_cpd00064_e0 -0.0068175 -0.00831712 0 H+ EX_cpd00067_e0 -15 -15 -10 L-tyrosine EX_cpd00069_e0 -0.0068175 -0.00233919 0 Sucrose EX_cpd00076_e0 0 -0.02049199 0 L-cysteine EX_cpd00084_e0 -0.0068175 0 0 Cl- EX_cpd00099_e0 -15 -15 -10 Glycerol EX_cpd00100_e0 0 0 -10 Biotin EX_cpd00104_e0 -15 -15 0 D-ribose EX_cpd00105_e0 -0.01862144 0 0 L-leucine EX_cpd00107_e0 -0.03596182 -0.00303228 0 D-galactose EX_cpd00108_e0 -0.25290619 -0.18317325 0 L-histidine EX_cpd00119_e0 -0.0068175 -0.00506825 0 L-proline EX_cpd00129_e0 -0.01102953 0 0 L-malate EX_cpd00130_e0 -0.03649016 -0.79413596 0 D-mannose EX_cpd00138_e0 -0.2540567 -0.05436649 0 Co2 EX_cpd00149_e0
    [Show full text]
  • OXPHOS Remodeling in High-Grade Prostate Cancer Involves Mtdna Mutations and Increased Succinate Oxidation
    ARTICLE https://doi.org/10.1038/s41467-020-15237-5 OPEN OXPHOS remodeling in high-grade prostate cancer involves mtDNA mutations and increased succinate oxidation Bernd Schöpf 1, Hansi Weissensteiner 1, Georg Schäfer2, Federica Fazzini1, Pornpimol Charoentong3, Andreas Naschberger1, Bernhard Rupp1, Liane Fendt1, Valesca Bukur4, Irina Giese4, Patrick Sorn4, Ana Carolina Sant’Anna-Silva 5, Javier Iglesias-Gonzalez6, Ugur Sahin4, Florian Kronenberg 1, ✉ Erich Gnaiger 5,6 & Helmut Klocker 7 1234567890():,; Rewiring of energy metabolism and adaptation of mitochondria are considered to impact on prostate cancer development and progression. Here, we report on mitochondrial respiration, DNA mutations and gene expression in paired benign/malignant human prostate tissue samples. Results reveal reduced respiratory capacities with NADH-pathway substrates glu- tamate and malate in malignant tissue and a significant metabolic shift towards higher succinate oxidation, particularly in high-grade tumors. The load of potentially deleterious mitochondrial-DNA mutations is higher in tumors and associated with unfavorable risk factors. High levels of potentially deleterious mutations in mitochondrial Complex I-encoding genes are associated with a 70% reduction in NADH-pathway capacity and compensation by increased succinate-pathway capacity. Structural analyses of these mutations reveal amino acid alterations leading to potentially deleterious effects on Complex I, supporting a causal relationship. A metagene signature extracted from the transcriptome of tumor samples exhibiting a severe mitochondrial phenotype enables identification of tumors with shorter survival times. 1 Institute of Genetic Epidemiology, Department of Genetics and Pharmacology, Medical University Innsbruck, Schöpfstraße 41, A-6020 Innsbruck, Austria. 2 Institute of Pathology, Neuropathology and Molecular Pathology, Medical University Innsbruck, Müllerstraße 44, A-6020 Innsbruck, Austria.
    [Show full text]