DOCSLIB.ORG

Title a Role of Formate Dehydrogenase in the Oxalate Metabolism in the Wood-Destroying Basidiomycete Ceriporiopsis Subvermispora

Total Page：16

File Type：pdf, Size：1020Kb

Download full-text PDF Read full-text
Title a Role of Formate Dehydrogenase in the Oxalate Metabolism in the Wood-Destroying Basidiomycete Ceriporiopsis Subvermispora View metadata, citation and similar papers at core.ac.uk brought to you by CORE provided by Kyoto University Research Information Repository A Role of Formate Dehydrogenase in the Oxalate Metabolism Title in the Wood-destroying Basidiomycete Ceriporiopsis subvermispora WATANABE, Tomoki; SABRINA, Tengku; HATTORI, Author(s) Takefumi; SHIMADA, Mikio Wood research : bulletin of the Wood Research Institute Kyoto Citation University (2003), 90: 7-8 Issue Date 2003-09-30 URL http://hdl.handle.net/2433/53104 Right Type Departmental Bulletin Paper Textversion publisher Kyoto University Preliminary A Role of Formate Dehydrogenase in the Oxalate Metabolism in the Wood-destroying Basidiomycete Ceriporiopsis subvermispora*l Tomoki WATANABE*2, Tengku SABRINA *3, Takefumi HATTORI*2 and Mikio SHIMADA*2 (Received June 7, 2003) Keywords: oxalate metabolism, NAD +-dependent formate dehydrogenase, white-rot fungi, Ceriporiopsis subvermispora metabolism that oxalate decarboxylase (ODO; EO 4.1.1.2) Introduction converts oxalate to formate and carbon dioxide, and the It is a common physiological trait that brown-rot fungi, formate thus produced is converted to carbon dioxide by including Fomitopsis palustris accumulate oxalic acid in large formate dehydrogenase (FDH; EO 1.2.1.2), yielding quantities in the cultures. Oxalic acid serves as an acid NADH. However, recently, Aguilar et al. successfully catalyst for the hydrolytic breakdown of wood purified oxalate oxidase (OXO ; EO 1.2.3.4) from white­ polysaccharides during brown-rot wood decay processes. rot fungus Ceriporiopsis subvermispora and they proposed a Furthermore, F. palustris has been reported to acquire novel pathway in which oxalate is metabolized by OXO to energy for growth by "oxalate-fermentation"l). An carbon dioxide, accompanied with the production of 11 oxalate-producing enzyme, glyoxylate dehydrogenase H 20 2 ) (GLOXDH) linked with oxalate biosynthesis, and Thus, we were motivated to investigate whether C. isocitrate lyase (IOL) as a key enzyme of the glyoxylate subvermispora has the oxalate-metabolizing systems with ll cycle, have been successfully purified and characterized ODO, FDH and OXO ) We report here preliminary from F. palustrii,3). Furthermore, another oxalate­ results for the purification and characterization of FDH producing enzyme, oxaloacetase has been detected from and the detection of ODO activity from C. subvermispora. 4 wood-rotting fungi ). The results are discussed in relation to oxalate metabolism On the contrary, white-rot fungi accumulate much by this fungus. smaller amounts of oxalic acid because they have oxalate­ 5 8 decomposing systems - ). Under the extracellular condi­ Results and Discussion tion, the two biochemical mediators, including veratryl alcohol cation radicals and Mn3 + produced by lignin Ceriporiopsis subvermispora OS 105 that was kindly provided peroxidase and manganese peroxidase, respectively, have from Dr. Vicuna was cultivated at 2rO in the Kirk's basal l2 been reported to catalyze the decomposition of oxalic acid medium ) containing 2.5% glucose as a carbon source, 3.0 to carbon dioxide9,lO). As a result, oxalic acid seemingly mM ammonium tartrate as a nitrogen source, which was inhibits ligninolytic enzymes4). Furthermore, it has been supplemented with 7-fold minerals. We have purified proposed as a general mechanism for intracellular oxalate FDH from C. subvermispora by varIOUS column o Route A !JJr2CO, + H,O, TCA a ~COOH) Isocitrate Glyoxylate NAD+ NADH+H+ cycle V .A 2 CO: "-.HCOOH U CO, ® RouteS @ Figure A possible biochemical mechanism for oxalate metabolism in C. subvermispora. Notes: CD Oxalate oxidase, CV Oxalate decarboxylase, ® Formate dehydrogenase. *1 Laboratory of Biochemical Control, Wood Research Institute, Kyoto University, Uji, Kyoto 611-0011, Japan. *2 North Sumatra University, Indonesia. *3 A part of this work was presented at the 55th Annual Meeting of the Wood Research Society in Fukuoka, March 2003. -7- WOOD RESEARCH No. 90 (2003) chromatographies. The purified FDH was found to be and the role in white-rot wood decay (Figure). electrophoreticallya single band on SDS-PAGE gel. The purified FDH was similar in molecular mass to the FDHs I3 I4 References purified from yeasts ) and plants ) But the K m value for formate was about one twentieth that of the yeast 1) E. MUNIR, J.J. YOON, T. TOKIMATSU, T. HATTORI and M. SHIMADA: Proc. Nat!. Acad. Sci. USA.) 98(20), 11126-11130 enzyme, although the K m value for NAD+ was almost the I3 same ). The enzyme showed greater activities at the (2001). neutral pH range. 2) E. MUNIR, T. HATTORI and M. SHIMADA: Arch. Biochem. Biophys.) 399(2), 225-231 (2002). The optimum temperature for native FDH was at a 3) T. TOKIMATSU, Y. NAGAI, T. HATTORI and M. SHIMADA: room temperature. Formate was the best substrate FEBS Lett.) 437(1-2), 117-121 (1998). among various intermediate organic acids tested. The 4) Y. AKAMATSU, M. TAKAHASHI and M. SHIMADA: Mokuzai FDH activity was inhibited by NADH (60 pM), ATP (10 Gakkaishi) 39, 352-356 (1993). mM), and ADP (10 mM). Interestingly, 2-oxoglutarate 5) H. SHIMAZONO: J. Biolchem.) 42, 321-340 (1955). and oxaloacetate also inhibited the enzymes. These 6) H. SHIMAZONO: Bull. Forest Expt. Station) 33, 393-397 results suggest that these a-ketoacids may control the (1951). enzyme activity intrftcellularly. 7) S. TAKAO: Appl. Microbiol.) 13, 727-732 (1965). The ODe activity was detected from the cell-free 8) M.V. DUTTON, C.S. EVANS, P.T. ATKEY and D.A. WOOD: extracts of C. subvermispora. Thus, the results strongly Appl. Microbiol. Biotechnol.) 39(1), 5-10 (1993). 9) Y. AKAMATSU, D.E. MA, T. HIGUCHI and M. SHIMADA: suggest that C. subvermispora decomposes oxalate to CO2 via formate (Figure, Route B), besides another oxalate FEBS Lett.) 269, 261-263 (1990). metabolizing pathway which was reported by Aguilar et at. 10) D.B. MA, T. HATTORI, Y. AKAMATSU, M. ADACHI and M. (Route A) 11). SHIMADA: Biosci. Biochem. Biotechnol.) 56,1378-1381 (1992). 11) C. AGUILAR, U. URZUA, C. KOENING and R. VICUNA: Arch. We suspect that NADH produced as the results of the Biochem. Biophys.) 366, 275-282 (1999). oxidation of formate may serve as an electron donor for I5 12) T.K. KIRK, E. SCHULTZ, W.]. CONNORS, L.F. LORENZ and ATP generation as in the case ofyeasts ). Alternatively, J.G. ZEICUS: Arch. Microbiol.) 117, 277-285 (1978). NADH may be used as a cosubstrate for several enzymes to 13) T.V. AVILOVA, O.A. EGOROVA, L.S. LOANESYAN and A.M. reduce quinones derived from lignin. It is speculated that EGOROV: Eur. J. Biochem.) 152, 657-662 (1985). white-rot fungi are superior to brown-rot ones in 14) D. PEACOCK and D. BOULTER: Biochem. J.) 120, 763-769 biochemical evolution on conversion of oxalate to an (1970). energy source. However, further research is needed to 15) N. KATO, H. SAHM and F. WANER: Biochim. Biophys. Acta) elucidate the reaction mechanisms for oxalate metabolism 566(1), 12-20 (1979). -8-.
Load more

Recommended publications
  • Harnessing Escherichia Coli for Bio-Based Production of Formate
    bioRxiv preprint doi: https://doi.org/10.1101/2021.01.06.425572; this version posted January 6, 2021. The copyright holder for this preprint (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under aCC-BY 4.0 International license. Harnessing Escherichia coli for bio‐based production of formate under pressurized H2 and CO2 gases. Magali Roger1,2, Tom C. Reed2 and Frank Sargent2* 1 Aix Marseille University, CNRS, Bioenergetics and Protein Engineering (BIP UMR7281), 31 Chemin Joseph Aiguier, CS70071, 13042 Marseille Cedex 09, France. 2 School of Natural and Environmental Sciences, Newcastle University, Newcastle upon Tyne, NE1 7RU, England, UK *For Correspondence: Prof Frank Sargent FRSE, Division of Plant & Microbial Biology, School of Natural & Environmental Sciences, Newcastle University, Devonshire Building, Kensington Terrace, Newcastle upon Tyne NE2 4BF, England, United Kingdom. T: +44 191 20 85138. E: [email protected] 1 bioRxiv preprint doi: https://doi.org/10.1101/2021.01.06.425572; this version posted January 6, 2021. The copyright holder for this preprint (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under aCC-BY 4.0 International license. ABSRACT Escherichia coli is gram‐negative bacterium that is a workhorse of the biotechnology industry. The organism has a flexible metabolism and can perform a mixed‐acid fermentation under anaerobic conditions. Under these conditions E. coli synthesises a formate hydrogenlyase isoenzyme (FHL‐1) that can generate molecular hydrogen and carbon dioxide from formic acid.
    [Show full text]
  • Elb87.Pdf (3.312Mb)
    NONLINEAR CONSTRAINT-BASED MODELING OF THE FUNCTION AND EVOLUTION OF C4 PHOTOSYNTHESIS A Dissertation Presented to the Faculty of the Graduate School of Cornell University in Partial Fulfillment of the Requirements for the Degree of Doctor of Philosophy by Elijah Lane Bogart August 2015 © 2015 Elijah Lane Bogart ALL RIGHTS RESERVED NONLINEAR CONSTRAINT-BASED MODELING OF THE FUNCTION AND EVOLUTION OF C4 PHOTOSYNTHESIS Elijah Lane Bogart, Ph.D. Cornell University 2015 C4 plants, such as maize, concentrate carbon dioxide in a specialized compart- ment surrounding the veins of their leaves to improve the efficiency of carbon dioxide assimilation. The C4 photosynthetic system is a key target of efforts to improve crop yield through biotechnology, and its independent development in dozens of plant species widely separated geographically and phylogenetically is an intriguing example of convergent evolution. The availability of extensive high-throughput experimental data from C4 and non-C4 plants, as well as the origin of the biochemical pathways of C4 photosynthesis in the recruitment of enzymatic reactions already present in the ancestral state, makes it natural to study the development, function and evolu- tion of the C4 system in the context of a plant’s complete metabolic network, but the essentially nonlinear relationship between rates of photosynthesis, rates of photorespiration, and carbon dioxide and oxygen levels prevents the appli- cation of conventional, linear methods for genome-scale metabolic modeling to these questions. I present an approach which incorporates nonlinear constraints on reaction rates arising from enzyme kinetics and diffusion laws into flux balance analysis problems, and software to enable it.
    [Show full text]
  • ( 12 ) Patent Application Publication
    US 20200199632A1 IN (19 ) United States (12 ) Patent Application Publication ( 10 ) Pub . No .: US 2020/0199632 A1 Toivari et al. (43 ) Pub . Date : Jun . 25 , 2020 ( 54 ) IMPROVED PRODUCTION OF C12N 9/14 (2006.01 ) OXALYL - COA , GLYOXYLATE AND /OR C12N 9/00 (2006.01 ) GLYCOLIC ACID C12N 9/88 (2006.01 ) (52 ) U.S. CI. ( 71 ) Applicant : Teknologian Tutkimuskeskus VTT CPC C12P 7/42 (2013.01 ) ; C12P 5/026 Oy , Espoo (FI ) ( 2013.01) ; C12N 9/14 (2013.01 ) ; C12N 9/88 (72 ) Inventors : Mervi Toivari , VTT (FI ) ; Marja ( 2013.01 ) ; C12N 9/93 (2013.01 ) ; C12Y Ilmén , VTT (FI ) ; Merja Penttilä , VTT 604/01001 ( 2013.01 ) ; C12 Y 602/01008 (FI ) ( 2013.01 ) ; C12Y 307/01001 (2013.01 ) (21 ) Appl. No.: 16 /633,608 (57 ) ABSTRACT ( 22 ) PCT Filed : Jul, 27 , 2018 The present invention relates to a method of converting ( 86 ) PCT No .: PCT/ FI2018 / 050557 oxalate to oxalyl - coA and /or oxalyl - coA to glyoxylate in a fungus and to a method of producing glycolic acid . Still , the $ 371 ( c ) ( 1 ) , present invention relates to a genetically modified fungus (2 ) Date : Jan. 24 , 2020 comprising increased enzyme activity associated with oxalyl- CoA . And furthermore , the present invention relates ( 30 ) Foreign Application Priority Data to use of the fungus of the present invention for producing oxalate , oxalyl- CoA , glyoxylate and /or glycolic acid from a Jul. 28 , 2017 (FI ) 20175703 carbon substrate . Still furthermore , the present invention Publication Classification relates to a method of producing specific products and to a (51 ) Int. Ci. method of preparing the genetically modified fungus of the C12P 7/42 ( 2006.01 ) present invention .
    [Show full text]
  • Recent Progress in the Microbial Production of Pyruvic Acid
    fermentation Review Recent Progress in the Microbial Production of Pyruvic Acid Neda Maleki 1 and Mark A. Eiteman 2,* 1 Department of Food Science, Engineering and Technology, University of Tehran, Karaj 31587-77871, Iran; [email protected] 2 School of Chemical, Materials and Biomedical Engineering, University of Georgia, Athens, GA 30602, USA * Correspondence: [email protected]; Tel.: +1-706-542-0833 Academic Editor: Gunnar Lidén Received: 10 January 2017; Accepted: 6 February 2017; Published: 13 February 2017 Abstract: Pyruvic acid (pyruvate) is a cellular metabolite found at the biochemical junction of glycolysis and the tricarboxylic acid cycle. Pyruvate is used in food, cosmetics, pharmaceutical and agricultural applications. Microbial production of pyruvate from either yeast or bacteria relies on restricting the natural catabolism of pyruvate, while also limiting the accumulation of the numerous potential by-products. In this review we describe research to improve pyruvate formation which has targeted both strain development and process development. Strain development requires an understanding of carbohydrate metabolism and the many competing enzymes which use pyruvate as a substrate, and it often combines classical mutation/isolation approaches with modern metabolic engineering strategies. Process development requires an understanding of operational modes and their differing effects on microbial growth and product formation. Keywords: auxotrophy; Candida glabrata; Escherichia coli; fed-batch; metabolic engineering; pyruvate; pyruvate dehydrogenase 1. Introduction Pyruvic acid (pyruvate at neutral pH) is a three carbon oxo-monocarboxylic acid, also known as 2-oxopropanoic acid, 2-ketopropionic acid or acetylformic acid. Pyruvate is biochemically located at the end of glycolysis and entry into the tricarboxylic acid (TCA) cycle (Figure1).
    [Show full text]
  • Fumarate Respiration of Wolinella Succinogenes: Enzymology, Energetics and Coupling Mechanism
    View metadata, citation and similar papers at core.ac.uk brought to you by CORE provided by Elsevier - Publisher Connector Biochimica et Biophysica Acta 1553 (2002) 23^38 www.bba-direct.com Review Fumarate respiration of Wolinella succinogenes: enzymology, energetics and coupling mechanism Achim Kro«ger a;*, Simone Biel a,Jo«rg Simon a, Roland Gross a, Gottfried Unden b, C. Roy D. Lancaster c a Institut fu«r Mikrobiologie, Johann Wolfgang Goethe-Universita«t, Marie-Curie-Str. 9, D-60439 Frankfurt am Main, Germany b Institut fu«r Mikrobiologie und Weinforschung, Johannes Gutenberg-Universita«t, D-55099 Mainz, Germany c Max-Planck-Institut fu«r Biophysik, Heinrich-Ho¡mann-Str. 7, D-60528 Frankfurt am Main, Germany Received 10 May 2001; received in revised form 27 August 2001; accepted 12 October 2001 Abstract Wolinella succinogenes performs oxidative phosphorylation with fumarate instead of O2 as terminal electron acceptor and H2 or formate as electron donors. Fumarate reduction by these donors (`fumarate respiration') is catalyzed by an electron transport chain in the bacterial membrane, and is coupled to the generation of an electrochemical proton potential (vp) across the bacterial membrane. The experimental evidence concerning the electron transport and its coupling to vp generation is reviewed in this article. The electron transport chain consists of fumarate reductase, menaquinone (MK) and either hydrogenase or formate dehydrogenase. Measurements indicate that the vp is generated exclusively by MK reduction with H2 or formate; MKH2 oxidation by fumarate appears to be an electroneutral process. However, evidence derived from the crystal structure of fumarate reductase suggests an electrogenic mechanism for the latter process.
    [Show full text]
  • Enzymatic Mechanism of Oxalate Production in the TCA and Glyoxylate Pathways Using Various Isolates of Antrodia Radiculosa K.M
    AMERICAN WOOD PROTECTION ASSOCIATION Enzymatic Mechanism of Oxalate Production in the TCA and Glyoxylate Pathways using Various Isolates of Antrodia radiculosa K.M. Jenkins S.V. Diehl Mississippi State University Starkville, Mississippi C.A. Clausen F. Green, III USDA-FS Forest Products Laboratory Madison, Wisconsin ABSTRACT Brown-rot fungi produce oxalate in large amounts; however, levels of accumulation and function vary by species. Copper-tolerant fungi, like Antrodia radiculosa, produce and accumulate high levels of oxalate in response to copper. Oxalate biosynthesis in copper-tolerant fungi has been linked to the glyoxylate and tricarboxylic acid (TCA) cycles. Within these two cycles, it has been proposed that oxalate production relies on twelve specific enzymes. In this study, Antrodia radiculosa isolates causing decay of untreated and 1.2% copper citrate treated wood were used to evaluate oxalate concentration and enzyme activity in five of the twelve enzymes. The enzyme activity of fumarase, glyoxylate dehydrogenase, isocitrate lyase, malate synthase, and oxaloacetase, was determined. Future gene expression analysis will determine any variations in enzymatic activity, as well as attempt to establish a pathway involved in the direct production of oxalate. INTRODUCTION Oxalate is a metabolic byproduct of the decay process, and is also a major factor that leads to the tolerance of copper based preservatives (Arango et al. 2009). The role of oxalate tends to vary with the type of copper treatment and species. Most brown-rot fungi produce oxalate regularly; however, copper-tolerant fungi produce it in much higher quantities. Clausen and Green (2003) found that copper-tolerant fungi produce 2-17 times more oxalate in copper treated blocks when compared to untreated controls.
    [Show full text]
  • (12) United States Patent (10) Patent No.: US 7927,859 B2 San Et Al
    USOO7927859B2 (12) United States Patent (10) Patent No.: US 7927,859 B2 San et al. (45) Date of Patent: Apr. 19, 2011 (54) HIGH MOLARSUCCINATEYIELD FOREIGN PATENT DOCUMENTS BACTERIA BY INCREASING THE WO WO99.06532 * 2/1999 INTRACELLULAR NADHAVAILABILITY WO WO 2007 OO1982 1, 2007 OTHER PUBLICATIONS (75) Inventors: Ka-Yiu San, Houston, TX (US); George N. Bennett, Houston, TX (US); Ailen Branden et al. Introduction to Protein Structure, Garland Publishing Inc., New York, p. 247, 1991.* Sánchez, Houston, TX (US) ExPASy. Formate Dehydrogenase.* Vemuri et al. Effects of growth mode and pyruvate carboxylase on (73) Assignee: Rice University, Houston, TX (US) Succinic acid production by metabolically engineered strains of Escherichia coli. Appl Environ Microbiol. Apr. 2002:68(4): 1715 (*) Notice: Subject to any disclaimer, the term of this 27.3 patent is extended or adjusted under 35 Goodbye et al. Cloning and sequence analysis of the fermentative alcohol-dehydrogenase-encoding gene of Escherichia coli. Gene. U.S.C. 154(b) by 791 days. Dec. 21, 1989;85(1):209-14.* Datsenko et al. One-step inactivation of chromosomal genes in (21) Appl. No.: 10/923,635 Escherichia coli K-12 using PCR products. Proc Natl AcadSci USA. Jun. 6, 2000:97(12):6640-5.* (22) Filed: Aug. 20, 2004 Berrios-Rivera et al. Metabolic engineering of Escherichia coli: increase of NADHavailability by overexpressing an NAD(+)-depen (65) Prior Publication Data dent formate dehydrogenase. Metab Eng. Jul. 2002;4(3):217-29.* Gupta et al. Escherichia coli derivatives lacking both alcohol US 2005/OO42736A1 Feb. 24, 2005 dehydrogenase and phosphotransacetylase grow anaerobically by lactate fermentation.
    [Show full text]
  • NAD+-Dependent Formate Dehydrogenase from Plants
    reVIeWS NAD+-dependent Formate Dehydrogenase from Plants A.A. Alekseeva1,2,3, S.S. Savin2,3, V.I. Tishkov1,2,3,* 1Chemistry Department, Lomonosov Moscow State University 2Innovations and High Technologies MSU Ltd 3Bach Institute of Biochemistry, Russian Academy of Sciences *E-mail: [email protected] Received 05.08.2011 Copyright © 2011 Park-media, Ltd. This is an open access article distributed under the Creative Commons Attribution License,which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. ABSTRACT NAD+-dependent formate dehydrogenase (FDH, EC 1.2.1.2) widely occurs in nature. FDH consists of two identical subunits and contains neither prosthetic groups nor metal ions. This type of FDH was found in different microorganisms (including pathogenic ones), such as bacteria, yeasts, fungi, and plants. As opposed to microbiological FDHs functioning in cytoplasm, plant FDHs localize in mitochondria. Formate dehydrogenase activity was first discovered as early as in 1921 in plant; however, until the past decade FDHs from plants had been considerably less studied than the enzymes from microorganisms. This review summarizes the recent results on studying the physiological role, properties, structure, and protein engineering of plant formate dehy- drogenases. KEYWORDS plant formate dehydrogenase; physiological role; properties; structure; expression; Escherichia coli; protein engineering. ABBREVIATIONS FDH – formate dehydrogenase; PseFDH, CboFDH – formate dehydrogenases from
    [Show full text]
  • Prospects for Bioprocess Development Based on Recent Genome Advances in Lignocellulose Degrading Basidiomycetes
    Prospects for Bioprocess Development Based on Recent Genome Advances in Lignocellulose Degrading Basidiomycetes Chiaki Hori and Daniel Cullen 1 Introduction Efficient and complete degradation of woody plant cell walls requires the concerted action of hydrolytic and oxidative systems possessed by a relatively small group of filamentous basidiomycetous fungi. Among these wood decay species, Phanerochaete chrysosporium was the first to be sequenced (Martinez et al. 2004). In the intervening 10 years, over 100 related saprophytes have been sequenced. There genomes have revealed impressive sequence diversity. and recent functional analyses are providing a deeper understanding of their roles in the deconstruction of plant cell walls and the transformation of xenobiotics. Wood cell walls are primarily composed of cellulose, hemicellulose and lignin. Many microbes are capable of hydrolyzing the linkages in cellulose and hemicel­ lulose, even though crystalline regions within cellulose can be rather challenging substrates (reviewed in Baldrian and Lopez-Mondejar 2014; van den Brink and de Vries 2011). In contrast, few microbes possess the oxidative enzymes required to efficiently degrade the recalcitrant lignin, a complex, amorphous, and insoluble phenylpropanoid polymer (Higuchi 1990; Ralph et al. 2004). These unusual wood decay fungi secrete extracellular peroxidases with impressive oxidative potential. Potential applications have focused primarily on lignocellulosic bioconversions to C. Hori, Ph.D. ( ) Riken Biomass Engineering Group, Yokohama, Japan e-mail: [email protected] D. Cullen, Ph.D USDA Forest Products Laboratory, Madison, WI. USA e-mail: [email protected] © Springer International Publishing Switzerland 2016 161 M. Schmoll, C. Dattenböck (eds.). Gene Expression Systems in Fungi: Advancements and Applications, Fungal Biology, DOI 10.1007/978-3-319-27951-0_6 162 C.
    [Show full text]
  • A Global Regulatory Genein Escherichia Coli Mediating
    Proc. Nati. Acad. Sci. USA Vol. 85, pp. 1888-1892, March 1988 Genetics areA (dye), a global regulatory gene in Escherichia coli mediating repression of enzymes in aerobic pathways (global control/anaerobic repression/modulon) S. IUCHI AND E. C. C. LIN* Department of Microbiology and Molecular Genetics, Harvard Medical School, 25 Shattuck Street, Boston, MA 02115 Communicated by Jon Beckwith, December 7, 1987 (receivedfor review October 23, 1987) ABSTRACT In Escherichia coli the levels of numerous genes, including those encoding nitrate, trimethylamine N- enzymes associated with aerobic metabolism are decreased oxide, and fumarate reductases, depends on the pleiotropic during anaerobic growth. In an arcA mutant the anaerobic transcriptional activator encoded by the fnr gene. Aerobic levels of these enzymes are increased. The enzymes, which are repression of this system appears to result from a deficiency encoded by different regulons, include members that belong to of functional Fnr protein (ref. 3; for a review, see ref. 2). In the tricarboxylic acid cycle, the glyoxylate shunt, the pathway the absence of 02, nitrate becomes the dominant electron for fatty acid degradation, several dehydrogenases of the acceptor by inhibiting the induction of fumarate and tri- flavoprotein class, and the cytochrome o oxidase complex. methylamine N-oxide reductases. In this control, nitrate and Transductional crosses placed the arcA gene near min o on the a molybdenum compound act as corepressors (4). The chromosomal map. Complementation tests showed that the apo-repressor may be encoded by the narL gene (5), which arcA gene corresponded to the dye gene, which is also known also acts as an activator for the synthesis of nitrate reductase as fexA, msp, seg, or sfrA because of various phenotypic (6).
    [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]
  • FORMATE DEHYDROGENASE Ph
    Enzymatic Assay of FORMATE DEHYDROGENASE (EC 1.2.1.2) PRINCIPLE: Formate Dehydrogenase Formate + ß-NAD > CO2 + ß-NADH Abbreviations used: ß-NAD = ß-Nicotinamide Adenine Dinucleotide, Oxidized Form ß-NADH = ß-Nicotinamide Adenine Dinucleotide, Reduced Form CONDITIONS: T = 37°C, pH = 7.0, A340nm, Light path = 1 cm METHOD: Continuous Spectrophotometric Rate Determination REAGENTS: A. 200 mM Sodium Phosphate Buffer, pH 7.0 at 37°C (Prepare 100 ml in deionized water using Sodium Phosphate, Monobasic, Anhydrous, Sigma Prod. No. S- 0751. Adjust the pH to 7.0 with 1 M NaOH.) B. 200 mM Sodium Formate Solution (Form) (Prepare 10 ml in deionized water using Formic Acid, Sodium Salt, Sigma Prod. No. F-6502. PREPARE FRESH.) C. 10.5 mM ß-Nicotinamide Adenine Dinucleotide Solution (ß-NAD) (Prepare 3 ml in deionized water using ß-Nicotinamide Adenine Dinucleotide, Sigma Prod. No. N-7004 or dissolve the contents of one 20 mg vial of ß-Nicotinamide Adenine Dinucleotide, Sigma Stock No. 260-120, in the appropriate volume of deionized water. PREPARE FRESH.) D. 1.5 mM ß-Nicotinamide Adenine Dinucleotide Solution (Enzyme Diluent) (Prepare 50 ml in Reagent A using ß-Nicotinamide Adenine Dinucleotide, Sigma Prod. No. N-7004. PREPARE FRESH.) E. Formate Dehydrogenase Enzyme Solution (Immediately before use, prepare a solution containing 0.25 - 0.50 unit/ml of Formate Dehydrogenase in Cold Reagent D.) SPFORM09 Page 1 of 3 Revised: 05/23/96 Enzymatic Assay of FORMATE DEHYDROGENASE (EC 1.2.1.2) PROCEDURE: Pipette (in milliliters) the following reagents into suitable cuvettes: Test Blank Deionized Water 1.10 1.10 Reagent A (Buffer) 0.75 0.75 Reagent B (Form) 0.75 0.75 Mix by inversion and equilibrate to 37°C.
    [Show full text]