Putative Genes Identi Ed in Alkaloids Biosynthesis in Dendrobium O
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Characterization and Phylogeny of the Pfp Gene of Amycolatopsis Methanolica Encoding
JOURNAL OF BACTERIOLOGY, Jan. 1996, p. 149–155 Vol. 178, No. 1 0021-9193/96/$04.0010 Copyright q 1996, American Society for Microbiology Characterization and Phylogeny of the pfp Gene of Amycolatopsis methanolica Encoding PPi-Dependent Phosphofructokinase ALEXANDRA M. C. R. ALVES, WIM G. MEIJER, JAN W. VRIJBLOED, AND LUBBERT DIJKHUIZEN* Department of Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute (GBB), University of Groningen, 9751 NN Haren, The Netherlands Received 28 July 1995/Accepted 2 November 1995 The actinomycete Amycolatopsis methanolica employs a PPi-dependent phosphofructokinase (PPi-PFK) (EC 2.7.1.90) with biochemical characteristics similar to those of both ATP- and PPi-dependent enzymes during growth on glucose. A 2.3-kb PvuII fragment hybridizing to two oligonucleotides based on the amino-terminal amino acid sequence of PPi-PFK was isolated from a genomic library of A. methanolica. Nucleotide sequence analysis of this fragment revealed the presence of an open reading frame encoding a protein of 340 amino acids with a high degree of similarity to PFK proteins. Heterologous expression of this open reading frame in Escherichia coli gave rise to a unique 45-kDa protein displaying a high level of PPi-PFK activity. The open reading frame was therefore designated pfp, encoding the PPi-PFK of A. methanolica. Upstream and transcribed divergently from pfp, a partial open reading frame (aroA) similar to 3-deoxy-D-arabino-heptulosonate-7- phosphate synthase-encoding genes was identified. The partial open reading frame (chiA) downstream from pfp was similar to chitinase genes from Streptomyces species. A phylogenetic analysis of the ATP- and PPi- dependent proteins showed that PPi-PFK enzymes are monophyletic, suggesting that the two types of PFK evolved from a common ancestor. -
ATP-Citrate Lyase Has an Essential Role in Cytosolic Acetyl-Coa Production in Arabidopsis Beth Leann Fatland Iowa State University
Iowa State University Capstones, Theses and Retrospective Theses and Dissertations Dissertations 2002 ATP-citrate lyase has an essential role in cytosolic acetyl-CoA production in Arabidopsis Beth LeAnn Fatland Iowa State University Follow this and additional works at: https://lib.dr.iastate.edu/rtd Part of the Molecular Biology Commons, and the Plant Sciences Commons Recommended Citation Fatland, Beth LeAnn, "ATP-citrate lyase has an essential role in cytosolic acetyl-CoA production in Arabidopsis " (2002). Retrospective Theses and Dissertations. 1218. https://lib.dr.iastate.edu/rtd/1218 This Dissertation is brought to you for free and open access by the Iowa State University Capstones, Theses and Dissertations at Iowa State University Digital Repository. It has been accepted for inclusion in Retrospective Theses and Dissertations by an authorized administrator of Iowa State University Digital Repository. For more information, please contact [email protected]. ATP-citrate lyase has an essential role in cytosolic acetyl-CoA production in Arabidopsis by Beth LeAnn Fatland A dissertation submitted to the graduate faculty in partial fulfillment of the requirements for the degree of DOCTOR OF PHILOSOPHY Major: Plant Physiology Program of Study Committee: Eve Syrkin Wurtele (Major Professor) James Colbert Harry Homer Basil Nikolau Martin Spalding Iowa State University Ames, Iowa 2002 UMI Number: 3158393 INFORMATION TO USERS The quality of this reproduction is dependent upon the quality of the copy submitted. Broken or indistinct print, colored or poor quality illustrations and photographs, print bleed-through, substandard margins, and improper alignment can adversely affect reproduction. In the unlikely event that the author did not send a complete manuscript and there are missing pages, these will be noted. -
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Mechanistic Studies on (S)-Norcoclaurine Synthase and Dimethylallyltryptophan Synthase by Louis Yu Pan Luk B.Sc., The University of British Columbia, 2004 A THESIS SUMBITTED IN PARTIAL FULFILLMENT OF THE REQUIREMENTS FOR THE DEGREE OF DOCTOR OF PHILOSOPHY in THE FACULTY OF GRADUATE STUDIES (Chemistry) The University of British Columbia (Vancouver) September, 2010 © Louis Yu Pan Luk, 2010 ii Abstract In alkaloid biosynthesis, there are a limited number of enzymes that can catalyze an aromatic electrophilic substitution. One example is norcoclaurine synthase, which catalyzes an asymmetric Pictet-Spengler condensation of dopamine and 4-hydroxyphenylacetaldehyde to give (S)-norcoclaurine. This is the first committed step in the biosynthesis of the benzylisoquinoline alkaloids that include morphine and codeine. In this work, the gene encoding for the Thalictrum flavum norcoclaurine synthase is highly overexpressed in Escherichia coli and the His-tagged recombinant enzyme is purified for the first time. A continuous assay based on circular dichroism spectroscopy is developed and used to monitor the kinetics of the enzymatic reaction. Dopamine analogues bearing a methoxy or hydrogen substituent in place of the C-1 phenolic group were readily accepted by the enzyme whereas those bearing the same substituents at C-2 were not. This supports a mechanism involving a two-step cyclization of the putative iminium ion intermediate that does not proceed via a spirocyclic intermediate. The reaction of [3,5,6- 2 H3]-dopamine was found to be slowed by a kinetic isotope effect of 1.7 ± 0.2 on the value of kcat/KM. This is interpreted as showing that the deprotonation step causing re-aromatization is partially rate determining in the overall reaction. -
Pyruvate-Phosphate Dikinase of Oxymonads and Parabasalia and the Evolution of Pyrophosphate-Dependent Glycolysis in Anaerobic Eukaryotes† Claudio H
EUKARYOTIC CELL, Jan. 2006, p. 148–154 Vol. 5, No. 1 1535-9778/06/$08.00ϩ0 doi:10.1128/EC.5.1.148–154.2006 Copyright © 2006, American Society for Microbiology. All Rights Reserved. Pyruvate-Phosphate Dikinase of Oxymonads and Parabasalia and the Evolution of Pyrophosphate-Dependent Glycolysis in Anaerobic Eukaryotes† Claudio H. Slamovits and Patrick J. Keeling* Canadian Institute for Advanced Research, Botany Department, University of British Columbia, 3529-6270 University Boulevard, Vancouver, British Columbia V6T 1Z4, Canada Received 29 September 2005/Accepted 8 November 2005 In pyrophosphate-dependent glycolysis, the ATP/ADP-dependent enzymes phosphofructokinase (PFK) and pyruvate kinase are replaced by the pyrophosphate-dependent PFK and pyruvate phosphate dikinase (PPDK), respectively. This variant of glycolysis is widespread among bacteria, but it also occurs in a few parasitic anaerobic eukaryotes such as Giardia and Entamoeba spp. We sequenced two genes for PPDK from the amitochondriate oxymonad Streblomastix strix and found evidence for PPDK in Trichomonas vaginalis and other parabasalia, where this enzyme was thought to be absent. The Streblomastix and Giardia genes may be related to one another, but those of Entamoeba and perhaps Trichomonas are distinct and more closely related to bacterial homologues. These findings suggest that pyrophosphate-dependent glycolysis is more widespread in eukaryotes than previously thought, enzymes from the pathway coexists with ATP-dependent more often than previously thought and may be spread by lateral transfer of genes for pyrophosphate-dependent enzymes from bacteria. Adaptation to anaerobic metabolism is a complex process (PPDK), respectively (for a comparison of these reactions, see involving changes to many proteins and pathways of critical reference 21). -
Multi-Enzymatic Cascades in the Synthesis of Modified Nucleosides
biomolecules Article Multi-Enzymatic Cascades in the Synthesis of Modified Nucleosides: Comparison of the Thermophilic and Mesophilic Pathways Ilja V. Fateev , Maria A. Kostromina, Yuliya A. Abramchik, Barbara Z. Eletskaya , Olga O. Mikheeva, Dmitry D. Lukoshin, Evgeniy A. Zayats , Maria Ya. Berzina, Elena V. Dorofeeva, Alexander S. Paramonov , Alexey L. Kayushin, Irina D. Konstantinova * and Roman S. Esipov Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry RAS, Miklukho-Maklaya 16/10, 117997 GSP, B-437 Moscow, Russia; [email protected] (I.V.F.); [email protected] (M.A.K.); [email protected] (Y.A.A.); [email protected] (B.Z.E.); [email protected] (O.O.M.); [email protected] (D.D.L.); [email protected] (E.A.Z.); [email protected] (M.Y.B.); [email protected] (E.V.D.); [email protected] (A.S.P.); [email protected] (A.L.K.); [email protected] (R.S.E.) * Correspondence: [email protected]; Tel.: +7-905-791-1719 ! Abstract: A comparative study of the possibilities of using ribokinase phosphopentomutase ! nucleoside phosphorylase cascades in the synthesis of modified nucleosides was carried out. Citation: Fateev, I.V.; Kostromina, Recombinant phosphopentomutase from Thermus thermophilus HB27 was obtained for the first time: M.A.; Abramchik, Y.A.; Eletskaya, a strain producing a soluble form of the enzyme was created, and a method for its isolation and B.Z.; Mikheeva, O.O.; Lukoshin, D.D.; chromatographic purification was developed. It was shown that cascade syntheses of modified nu- Zayats, E.A.; Berzina, M.Y..; cleosides can be carried out both by the mesophilic and thermophilic routes from D-pentoses: ribose, Dorofeeva, E.V.; Paramonov, A.S.; 2-deoxyribose, arabinose, xylose, and 2-deoxy-2-fluoroarabinose. -
LAP3, a Novel Plant Protein Required for Pollen Development, Is Essential for Proper Exine Formation Anna A
View metadata, citation and similar papers at core.ac.uk brought to you by CORE provided by Valparaiso University Valparaiso University ValpoScholar Biology Faculty Publications Department of Biology 2009 LAP3, a novel plant protein required for pollen development, is essential for proper exine formation Anna A. Dobritsa University of Chicago Shuh-Ichi Nishikawa Nagoya University Daphne Preuss University of Chicago Ewa Urbanczyk-Wochniak Samuel Roberts Noble Foundation Lloyd W. Sumner Samuel Roberts Noble Foundation See next page for additional authors Follow this and additional works at: http://scholar.valpo.edu/bio_fac_pub Part of the Biology Commons Recommended Citation Dobritsa, A. A., Nishikawa, S. I., Preuss, D., Urbanczyk-Wochniak, E., Sumner, L. W., Hammond, A., Carlson, A. L. & Swanson, R. J. 2009 LAP3, a novel plant protein required for pollen development, is essential for proper exine formation. Sexual Plant Reproduction 22: 167-177. This Article is brought to you for free and open access by the Department of Biology at ValpoScholar. It has been accepted for inclusion in Biology Faculty Publications by an authorized administrator of ValpoScholar. For more information, please contact a ValpoScholar staff member at [email protected]. Authors Anna A. Dobritsa, Shuh-Ichi Nishikawa, Daphne Preuss, Ewa Urbanczyk-Wochniak, Lloyd W. Sumner, Adam Hammond, Ann L. Carlson, and Rob Swanson This article is available at ValpoScholar: http://scholar.valpo.edu/bio_fac_pub/13 Sex Plant Reprod (2009) 22:167–177 DOI 10.1007/s00497-009-0101-8 ORIGINAL ARTICLE LAP3, a novel plant protein required for pollen development, is essential for proper exine formation Anna A. Dobritsa Æ Shuh-Ichi Nishikawa Æ Daphne Preuss Æ Ewa Urbanczyk-Wochniak Æ Lloyd W. -
Deploying Microbial Synthesis for Halogenating and Diversifying Medicinal Alkaloid Scaffolds
Downloaded from orbit.dtu.dk on: Sep 28, 2021 Deploying Microbial Synthesis for Halogenating and Diversifying Medicinal Alkaloid Scaffolds Bradley, Samuel Alan; Zhang, Jie; Jensen, Michael Krogh Published in: Frontiers in Bioengineering and Biotechnology Link to article, DOI: 10.3389/fbioe.2020.594126 Publication date: 2020 Document Version Publisher's PDF, also known as Version of record Link back to DTU Orbit Citation (APA): Bradley, S. A., Zhang, J., & Jensen, M. K. (2020). Deploying Microbial Synthesis for Halogenating and Diversifying Medicinal Alkaloid Scaffolds. Frontiers in Bioengineering and Biotechnology, 8, [594126]. https://doi.org/10.3389/fbioe.2020.594126 General rights Copyright and moral rights for the publications made accessible in the public portal are retained by the authors and/or other copyright owners and it is a condition of accessing publications that users recognise and abide by the legal requirements associated with these rights. Users may download and print one copy of any publication from the public portal for the purpose of private study or research. You may not further distribute the material or use it for any profit-making activity or commercial gain You may freely distribute the URL identifying the publication in the public portal 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. fbioe-08-594126 October 19, 2020 Time: 19:15 # 1 REVIEW published: 23 October 2020 doi: 10.3389/fbioe.2020.594126 Deploying Microbial Synthesis for Halogenating and Diversifying Medicinal Alkaloid Scaffolds Samuel A. Bradley, Jie Zhang and Michael K. -
Divergent Camptothecin Biosynthetic Pathway in Ophiorrhiza Pumila
Yang et al. BMC Biology (2021) 19:122 https://doi.org/10.1186/s12915-021-01051-y RESEARCH ARTICLE Open Access Divergent camptothecin biosynthetic pathway in Ophiorrhiza pumila Mengquan Yang2†, Qiang Wang1,3†, Yining Liu2, Xiaolong Hao1, Can Wang1, Yuchen Liang2, Jianbo Chen3, Youli Xiao2ˆ and Guoyin Kai1* Abstract Background: The anticancer drug camptothecin (CPT), first isolated from Camptotheca acuminata, was subsequently discovered in unrelated plants, including Ophiorrhiza pumila. Unlike known monoterpene indole alkaloids, CPT in C. acuminata is biosynthesized via the key intermediate strictosidinic acid, but how O. pumila synthesizes CPT has not been determined. Results: In this study, we used nontargeted metabolite profiling to show that 3α-(S)-strictosidine and 3-(S), 21-(S)- strictosidinic acid coexist in O. pumila. After identifying the enzymes OpLAMT, OpSLS, and OpSTR as participants in CPT biosynthesis, we compared these enzymes to their homologues from two other representative CPT-producing plants, C. acuminata and Nothapodytes nimmoniana, to elucidate their phylogenetic relationship. Finally, using labelled intermediates to resolve the CPT biosynthesis pathway in O. pumila,weshowedthat3α-(S)-strictosidine, not 3-(S), 21- (S)-strictosidinic acid, is the exclusive intermediate in CPT biosynthesis. Conclusions: In our study, we found that O. pumila, another representative CPT-producing plant, exhibits metabolite diversity in its central intermediates consisting of both 3-(S), 21-(S)-strictosidinic acid and 3α-(S)-strictosidine and utilizes 3α-(S)-strictosidine as the exclusive intermediate in the CPT biosynthetic pathway, which differs from C. acuminata.Our results show that enzymes likely to be involved in CPT biosynthesis in O. pumila, C. acuminata,andN. -
Characterisation of the ATP-Dependent Phosphofructokinase Gene Family from Arabidopsis Thaliana
View metadata, citation and similar papers at core.ac.uk brought to you by CORE provided by Elsevier - Publisher Connector FEBS Letters 581 (2007) 2401–2410 Characterisation of the ATP-dependent phosphofructokinase gene family from Arabidopsis thaliana Angelika Mustropha,1, Uwe Sonnewaldb, Sophia Biemeltb,* a Humboldt-University Berlin, Institute of Biology, AG Plant Physiology, Philippstrasse 13, 10115 Berlin, Germany b Friedrich-Alexander University Erlangen-Nuremberg, Department of Biochemistry, Staudtstrasse 5, 91058 Erlangen, Germany Received 1 March 2007; revised 15 April 2007; accepted 16 April 2007 Available online 30 April 2007 Edited by Mark Stitt addition to the widely distributed ATP-dependent phospho- Abstract Plants possess two different types of phosphofructo- kinases, an ATP-dependent (PFK) and a pyrophosphate-depen- fructokinase (PFK, EC 2.7.1.11), in plants and a number of dent form (PFP). While plant PFPs have been investigated in prokaryotes a second type of phosphofructokinase is present detail, cDNA clones coding for PFK have not been identified using pyrophosphate (PPi) instead of ATP as phosphoryl in Arabidopsis thaliana. Searching the A. thaliana genome re- donor (pyrophosphate-fructose-6-phosphate-phosphotransfer- vealed 11 putative members of a phosphofructokinase gene fam- ase, PFP, EC 2.7.1.90). Phosphorylation of Fru6P catalyzed by ily. Among those, four sequences showed high homology to the PFK is virtually irreversible in vivo, while PFP reacts near alpha- or beta-subunits of plant PFPs. Seven cDNAs resulted equilibrium and catalyzes the reaction in both directions. In in elevated PFK, but not PFP activity after transient expression addition a third, ADP-dependent phosphofructokinase has in tobacco leaves suggesting that they encode Arabidopsis PFKs. -
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Inclusion of Low Amounts of Fructose With an Intraduodenal Glucose Load Markedly Reduces Postprandial Hyperglycemia and Hyperinsulinemia in the Conscious Dog Masakazu Shiota,1 Mary Courtney Moore,1 Pietro Galassetti,1 Michael Monohan,1 Doss W. Neal,1 Gerald I. Shulman,2 and Alan D. Cherrington1 ؎ Intraportal infusion of small amounts of fructose mark- (12 2%), net glycogen deposition (3.68 mmol glucose edly augmented net hepatic glucose uptake (NHGU) equivalent/kg body wt), net hepatic lactate production during hyperglycemic hyperinsulinemia in conscious (3.27 mmol/kg), and glycogen synthesis via the direct dogs. In this study, we examined whether the inclusion pathway (68%) were significantly higher (P < 0.05) of catalytic amounts of fructose with a glucose load compared to that in the absence of fructose. The in- ؎ reduces postprandial hyperglycemia and the pancreatic creases in arterial blood glucose (from 4.4 ؎ 0.1 to 6.4 -cell response to a glucose load in conscious 42-h– 0.2 mmol/l at 30 min) and arterial plasma insulin (from fasted dogs. Each study consisted of an equilibration 48 ؎ 6to126؎ 30 pmol/l at 30 min) were significantly ؊140 to ؊40 min), control (؊40 to 0 min), and test smaller (P < 0.05). In summary, the inclusion of small) period (0–240 min). During the latter period, glucose amounts of fructose with a glucose load augmented mol ⅐ kg؊1 ⅐ min؊1) was continuously given NHGU, increased hepatic glycogen synthesis via the 44.4) intraduodenally with (2.22 mol ⅐ kg؊1 ⅐ min؊1)or direct pathway, and augmented hepatic glycolysis. As a without fructose. -
Supplementary. Table S1 a Total of Degs Detected in This Study (Gm) No
Supplementary. Table S1 A total of DEGs detected in this study (Gm) No. genename significance in annotation 1 At1g01020 D2 ARV1__expressed protein, similar to hypothetical protein DDB0188786 [Dictyostelium discoideum] (GB:EAL62332.1); contains InterPro domain Arv1-like protein (InterPro:IPR007290) 2 At1g01100 D2 60S acidic ribosomal protein P1 (RPP1A), similar to 60S ACIDIC RIBOSOMAL PROTEIN P1 GB:O23095 from (Arabidopsis thaliana) 3 At1g01120 D2, Dm KCS1__fatty acid elongase 3-ketoacyl-CoA synthase 1 (KCS1), nearly identical to GB:AAC99312 GI:4091810 from (Arabidopsis thaliana) 4 At1g01160 D1, D2, Dm GIF2__SSXT protein-related / transcription co-activator-related, similar to SYT/SSX4 fusion protein (GI:11127695) (Homo sapiens); supporting cDNA gi:21539891:gb:AY102640.1:; contains Pfam profile PF05030: SSXT protein (N-terminal region) 5 At1g01170 D2 ozone-responsive stress-related protein, putative, similar to stress-related ozone-induced protein AtOZI1 (GI:790583) (Arabidopsis thaliana); contains 1 predicted transmembrane domain; 6 At1g01240 D1, D2, Dm expressed protein 7 At1g01300 D2, Dm aspartyl protease family protein, contains Pfam domain, PF00026: eukaryotic aspartyl protease 8 At1g01320 D2 tetratricopeptide repeat (TPR)-containing protein, low similarity to SP:P46825 Kinesin light chain (KLC) {Loligo pealeii}; contains Pfam profile PF00515: TPR Domain 9 At1g01430 D2, Dm expressed protein, similar to hypothetical protein GB:CAB80917 GI:7267605 from (Arabidopsis thaliana) 10 At1g01470 D1, D2, Dm LEA14_LSR3__late embryogenesis abundant -
Characteristics of Carbohydrate Metabolism in Sweet Corn (Sugary-I) Endosperms
Reprints from Vol. 118(5), September 1993 Journal of the American Society for Horticultural Science 1071 J. AMER. Soc. HaRT. SCI. 118(5):661-666. 1993. Characteristics of Carbohydrate Metabolism in Sweet Corn (sugary-I) Endosperms Douglas C. Doehlertl and Tsung Min Kuo U.S. Department of Agriculture, Agricultural Research Service, National Center for Agricultural Utilization Research, Phytoproducts Research Unit, 1815 North University Street, Peoria, IL 61604 John A. Juvik Department ofHorticulture, University ofIllinois, 1201 West Gregory Avenue, Urbana, IL 61801 Eric P. Beers and Stanley H. Duke Department ofAgronomy, University ofWisconsin, 1575 Linden Drive, Madison, WI 53706 Additional index words. Zea mays, phytoglycogen, gene dosage Abstract. Metabolic characteristics ofdeveloping sugary-! maize (Zea mays L.) endosperms were investigated. In the later stages ofdevelopment (>30 days postpollination), sugary-! kernels maintained higher levels ofmany enzyme activities and retained more moisture than normal kernels. Higher enzyme activities were attributed to moisture retention and were not associated with any increase in dry weight accumulation. Ofenzyme activities measured at 20 days postpollination, that ofADP-glucose pyrophosphorylase was higher in sugary-! kernels than in normal, whereas total amylase, a-amylase, and pullulanase activities were lower. Experiments testing the effects of zero, one, two, and three doses of the sugary-! gene in OH43 endosperms indicated that the sugary-! phenotype was not expressed until three doses ofthe sugary-! gene were present. Decreased activities of amylases, but not of pullulanase, were attributed to an interference in detection by phytoglycogen. Increased ADP-glucose pyrophosphorylase activity is attributed to a response by the maize endosperm cells to increased sucrose concentrations. The sugary-l genotype ofmaize (Zea mays), commonly grown maize kernel.