SI Table 1. Assessment of Genome Completeness
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METACYC ID Description A0AR23 GO:0004842 (Ubiquitin-Protein Ligase
Electronic Supplementary Material (ESI) for Integrative Biology This journal is © The Royal Society of Chemistry 2012 Heat Stress Responsive Zostera marina Genes, Southern Population (α=0. -
Screening and Identification of Key Biomarkers in Clear Cell Renal Cell Carcinoma Based on Bioinformatics Analysis
bioRxiv preprint doi: https://doi.org/10.1101/2020.12.21.423889; this version posted December 23, 2020. The copyright holder for this preprint (which was not certified by peer review) is the author/funder. All rights reserved. No reuse allowed without permission. Screening and identification of key biomarkers in clear cell renal cell carcinoma based on bioinformatics analysis Basavaraj Vastrad1, Chanabasayya Vastrad*2 , Iranna Kotturshetti 1. Department of Biochemistry, Basaveshwar College of Pharmacy, Gadag, Karnataka 582103, India. 2. Biostatistics and Bioinformatics, Chanabasava Nilaya, Bharthinagar, Dharwad 580001, Karanataka, India. 3. Department of Ayurveda, Rajiv Gandhi Education Society`s Ayurvedic Medical College, Ron, Karnataka 562209, India. * Chanabasayya Vastrad [email protected] Ph: +919480073398 Chanabasava Nilaya, Bharthinagar, Dharwad 580001 , Karanataka, India bioRxiv preprint doi: https://doi.org/10.1101/2020.12.21.423889; this version posted December 23, 2020. The copyright holder for this preprint (which was not certified by peer review) is the author/funder. All rights reserved. No reuse allowed without permission. Abstract Clear cell renal cell carcinoma (ccRCC) is one of the most common types of malignancy of the urinary system. The pathogenesis and effective diagnosis of ccRCC have become popular topics for research in the previous decade. In the current study, an integrated bioinformatics analysis was performed to identify core genes associated in ccRCC. An expression dataset (GSE105261) was downloaded from the Gene Expression Omnibus database, and included 26 ccRCC and 9 normal kideny samples. Assessment of the microarray dataset led to the recognition of differentially expressed genes (DEGs), which was subsequently used for pathway and gene ontology (GO) enrichment analysis. -
A Review on Agmatinase Inhibitors
www.ijcrt.org © 2020 IJCRT | Volume 8, Issue 12 December 2020 | ISSN: 2320-2882 A review on Agmatinase inhibitors 1Sunnica Biswas, 2Mr. R. T. Lohiya, 3Dr. Milind Umekar *1&2 Department Of Pharmaceutical Chemistry Smt. Kishoriti Bhoyar College of Pharmacy, Kamptee, Dst. Nagpur, 441002 Abstract : Agmatine is the product of arginine decarboxylation and can be hydrolyzed by agmatinase to putrescine, the precursor for biosynthesis of higher polyamines, spermidine, and spermine. Besides being an intermediate in polyamine metabolism, recent findings indicate that agmatine may play important regulatory roles in mammals. Agmatine, 4-aminobutyl guanidine, has recently been found in various mammalian organs and is thought to act as a neurotransmitter or neuromodulatory agent. The present study is to do a review on agmatine and its synthesized analogues till now for agmatinase inhibitory action. Agmatinase is a binuclear manganese metalloenzyme and belongs to the ureohydrolase superfamily that includes arginase, formiminoglutamase, and proclavaminate amidinohydrolase. Compared with a wealth of structural information available for arginases, no three dimensional structure of agmatinase has been reported. Agmatinase is an enzyme which blocks the mammalian agmatine which is ultimately responsible for the agmatine degradation in the body. Agmatinase is an enzyme which regulates the half life of agmatine in the brain. Hence a selective inhibitor of brain agmatinase is required. Several derivatives of agmatine are synthesized previously for agmatinase inhibitory activity but none of them showed selective inhibition. PZC (Piperazinecarboxamidine) is a derivative of agmatine or guanidine is expected to show selective inhibition of human agmatinase. A detailed review is carried out in order to understand the agmatinase inhibitor. -
Part One Amino Acids As Building Blocks
Part One Amino Acids as Building Blocks Amino Acids, Peptides and Proteins in Organic Chemistry. Vol.3 – Building Blocks, Catalysis and Coupling Chemistry. Edited by Andrew B. Hughes Copyright Ó 2011 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim ISBN: 978-3-527-32102-5 j3 1 Amino Acid Biosynthesis Emily J. Parker and Andrew J. Pratt 1.1 Introduction The ribosomal synthesis of proteins utilizes a family of 20 a-amino acids that are universally coded by the translation machinery; in addition, two further a-amino acids, selenocysteine and pyrrolysine, are now believed to be incorporated into proteins via ribosomal synthesis in some organisms. More than 300 other amino acid residues have been identified in proteins, but most are of restricted distribution and produced via post-translational modification of the ubiquitous protein amino acids [1]. The ribosomally encoded a-amino acids described here ultimately derive from a-keto acids by a process corresponding to reductive amination. The most important biosynthetic distinction relates to whether appropriate carbon skeletons are pre-existing in basic metabolism or whether they have to be synthesized de novo and this division underpins the structure of this chapter. There are a small number of a-keto acids ubiquitously found in core metabolism, notably pyruvate (and a related 3-phosphoglycerate derivative from glycolysis), together with two components of the tricarboxylic acid cycle (TCA), oxaloacetate and a-ketoglutarate (a-KG). These building blocks ultimately provide the carbon skeletons for unbranched a-amino acids of three, four, and five carbons, respectively. a-Amino acids with shorter (glycine) or longer (lysine and pyrrolysine) straight chains are made by alternative pathways depending on the available raw materials. -
Agmatinase Sirna (H): Sc-60060
SANTA CRUZ BIOTECHNOLOGY, INC. Agmatinase siRNA (h): sc-60060 BACKGROUND STORAGE AND RESUSPENSION Agmatinase (also known as agmatine ureohydrolase) results from the decar- Store lyophilized siRNA duplex at -20° C with desiccant. Stable for at least boxylation of L-arginine by arginine decarboxylase to form a metabolic inter- one year from the date of shipment. Once resuspended, store at -20° C, mediate in the biosynthesis of putresine and higher polyamines (spermidine avoid contact with RNAses and repeated freeze thaw cycles. and spermine). Agmatinase has been shown to play a role in several important Resuspend lyophilized siRNA duplex in 330 µl of the RNAse-free water biochemical processes in humans, ranging from effects on the central nervous provided. Resuspension of the siRNA duplex in 330 µl of RNAse-free water system to cell proliferation in cancer and viral replication. Agmatinase cat- makes a 10 µM solution in a 10 µM Tris-HCl, pH 8.0, 20 mM NaCl, 1 mM alyzes the hydrolysis of agmatine to putresine and urea and is a major target EDTA buffered solution. for drug therapy. Human Agmatinase retains about 30% identity to bacterial agmatinases and less than 20% identity to mammalian arginases. Residues APPLICATIONS required for binding of Mn2+ at the active site in bacterial Agmatinase and other members of the arginase superfamily are fully conserved in human Agmatinase siRNA (h) is recommended for the inhibition of Agmatinase Agmatinase. Agmatinase mRNA is most abundant in human liver and kidney, expression in human cells. but is also expressed in several other tissues, including skeletal muscle and brain. -
Mapping Active Site Residues in Glutamate-5-Kinase. the Substrate Glutamate and the Feed-Back Inhibitor Proline Bind at Overlapping Sites
View metadata, citation and similar papers at core.ac.uk brought to you by CORE provided by Elsevier - Publisher Connector FEBS Letters 580 (2006) 6247–6253 Mapping active site residues in glutamate-5-kinase. The substrate glutamate and the feed-back inhibitor proline bind at overlapping sites Isabel Pe´rez-Arellanoa, Vicente Rubiob, Javier Cerveraa,* a Centro de Investigacio´n Prı´ncipe Felipe, Avda. Autopista del Saler, 16, Valencia 46013, Spain b Instituto de Biomedicina de Valencia (IBV-CSIC), Jaime Roig 11, Valencia 46010, Spain Received 22 August 2006; revised 10 October 2006; accepted 12 October 2006 Available online 20 October 2006 Edited by Stuart Ferguson (a domain named after pseudo uridine synthases and archaeo- Abstract Glutamate-5-kinase (G5K) catalyzes the controlling first step of proline biosynthesis. Substrate binding, catalysis sine-specific transglycosylases) domain [10]. AAK domains and feed-back inhibition by proline are functions of the N-termi- bind ATP and a phosphorylatable acidic substrate, and make nal 260-residue domain of G5K. We study here the impact on a phosphoric anhydride [11]. The function of the PUA domain these functions of 14 site-directed mutations affecting 9 residues (a domain characteristically found in some RNA-modifying of Escherichia coli G5K, chosen on the basis of the structure of enzymes) [12] is not known. By deleting the PUA domain of the bisubstrate complex of the homologous enzyme acetylgluta- E. coli G5K we showed [10] that the isolated AAK domain, mate kinase (NAGK). The results support the predicted roles as the complete enzyme, forms tetramers, catalyzes the reac- of K10, K217 and T169 in catalysis and ATP binding and of tion and is feed-back inhibited by proline. -
Advances in Chitin/Chitosan Characterization and Applications
Advances in Chitin/Chitosan Characterization and Applications Edited by Marguerite Rinaudo and Francisco M. Goycoolea Printed Edition of the Special Issue Published in Polymers www.mdpi.com/journal/polymers Advances in Chitin/Chitosan Characterization and Applications Advances in Chitin/Chitosan Characterization and Applications Special Issue Editors Marguerite Rinaudo Francisco M. Goycoolea MDPI • Basel • Beijing • Wuhan • Barcelona • Belgrade Special Issue Editors Marguerite Rinaudo Francisco M. Goycoolea University of Grenoble Alpes University of Leeds France UK Editorial Office MDPI St. Alban-Anlage 66 4052 Basel, Switzerland This is a reprint of articles from the Special Issue published online in the open access journal Polymers (ISSN 2073-4360) from 2017 to 2018 (available at: https://www.mdpi.com/journal/polymers/ special issues/chitin chitosan) For citation purposes, cite each article independently as indicated on the article page online and as indicated below: LastName, A.A.; LastName, B.B.; LastName, C.C. Article Title. Journal Name Year, Article Number, Page Range. ISBN 978-3-03897-802-2 (Pbk) ISBN 978-3-03897-803-9 (PDF) c 2019 by the authors. Articles in this book are Open Access and distributed under the Creative Commons Attribution (CC BY) license, which allows users to download, copy and build upon published articles, as long as the author and publisher are properly credited, which ensures maximum dissemination and a wider impact of our publications. The book as a whole is distributed by MDPI under the terms and conditions of the Creative Commons license CC BY-NC-ND. Contents About the Special Issue Editors ..................................... ix Preface to ”Advances in Chitin/Chitosan Characterization and Applications” ......... -
Supplementary Table S1. Table 1. List of Bacterial Strains Used in This Study Suppl
Supplementary Material Supplementary Tables: Supplementary Table S1. Table 1. List of bacterial strains used in this study Supplementary Table S2. List of plasmids used in this study Supplementary Table 3. List of primers used for mutagenesis of P. intermedia Supplementary Table 4. List of primers used for qRT-PCR analysis in P. intermedia Supplementary Table 5. List of the most highly upregulated genes in P. intermedia OxyR mutant Supplementary Table 6. List of the most highly downregulated genes in P. intermedia OxyR mutant Supplementary Table 7. List of the most highly upregulated genes in P. intermedia grown in iron-deplete conditions Supplementary Table 8. List of the most highly downregulated genes in P. intermedia grown in iron-deplete conditions Supplementary Figures: Supplementary Figure 1. Comparison of the genomic loci encoding OxyR in Prevotella species. Supplementary Figure 2. Distribution of SOD and glutathione peroxidase genes within the genus Prevotella. Supplementary Table S1. Bacterial strains Strain Description Source or reference P. intermedia V3147 Wild type OMA14 isolated from the (1) periodontal pocket of a Japanese patient with periodontitis V3203 OMA14 PIOMA14_I_0073(oxyR)::ermF This study E. coli XL-1 Blue Host strain for cloning Stratagene S17-1 RP-4-2-Tc::Mu aph::Tn7 recA, Smr (2) 1 Supplementary Table S2. Plasmids Plasmid Relevant property Source or reference pUC118 Takara pBSSK pNDR-Dual Clonetech pTCB Apr Tcr, E. coli-Bacteroides shuttle vector (3) plasmid pKD954 Contains the Porpyromonas gulae catalase (4) -
Yeast Genome Gazetteer P35-65
gazetteer Metabolism 35 tRNA modification mitochondrial transport amino-acid metabolism other tRNA-transcription activities vesicular transport (Golgi network, etc.) nitrogen and sulphur metabolism mRNA synthesis peroxisomal transport nucleotide metabolism mRNA processing (splicing) vacuolar transport phosphate metabolism mRNA processing (5’-end, 3’-end processing extracellular transport carbohydrate metabolism and mRNA degradation) cellular import lipid, fatty-acid and sterol metabolism other mRNA-transcription activities other intracellular-transport activities biosynthesis of vitamins, cofactors and RNA transport prosthetic groups other transcription activities Cellular organization and biogenesis 54 ionic homeostasis organization and biogenesis of cell wall and Protein synthesis 48 plasma membrane Energy 40 ribosomal proteins organization and biogenesis of glycolysis translation (initiation,elongation and cytoskeleton gluconeogenesis termination) organization and biogenesis of endoplasmic pentose-phosphate pathway translational control reticulum and Golgi tricarboxylic-acid pathway tRNA synthetases organization and biogenesis of chromosome respiration other protein-synthesis activities structure fermentation mitochondrial organization and biogenesis metabolism of energy reserves (glycogen Protein destination 49 peroxisomal organization and biogenesis and trehalose) protein folding and stabilization endosomal organization and biogenesis other energy-generation activities protein targeting, sorting and translocation vacuolar and lysosomal -
770.Full-Text.Pdf
Published OnlineFirst January 14, 2019; DOI: 10.1158/1055-9965.EPI-18-0936 Research Article Cancer Epidemiology, Biomarkers Serum Metabolic Profiling Identified a Distinct & Prevention Metabolic Signature in Bladder Cancer Smokers: A Key Metabolic Enzyme Associated with Patient Survival Chandra Sekhar Amara1, Chandrashekar R. Ambati2, Venkatrao Vantaku1, Danthasinghe Waduge Badrajee Piyarathna1, Sri Ramya Donepudi2, Shiva Shankar Ravi1, James M. Arnold3, Vasanta Putluri2, Gurkamal Chatta4, Khurshid A. Guru5, Hoda Badr6, Martha K. Terris7, Roni J. Bollag7, Arun Sreekumar1,3, Andrea B. Apolo8, and Nagireddy Putluri1 Abstract Background: The current system to predict the outcome of nylalanine, proline, serine, valine, isoleucine, glycine, and smokers with bladder cancer is insufficient due to complex asparagine) and taurine were observed in bladder cancer genomic and transcriptomic heterogeneities. This study aims smokers. Integration of differential metabolomic gene signa- to identify serum metabolite-associated genes related to sur- ture and transcriptomics data from TCGA cohort revealed an vival in this population. intersection of 17 genes that showed significant correlation Methods: We performed LC/MS-based targeted metabo- with patient survival in bladder cancer smokers. Importantly, lomic analysis for >300 metabolites in serum obtained catechol-O-methyltransferase, iodotyrosine deiodinase, and from two independent cohorts of bladder cancer never tubulin tyrosine ligase showed a significant association with smokers, smokers, healthy smokers, and healthy never patient survival in publicly available bladder cancer smoker smokers. A subset of differential metabolites was validated datasets and did not have any clinical association in never using Biocrates absoluteIDQ p180 Kit. Genes associated smokers. with differential metabolites were integrated with a publicly Conclusions: Serum metabolic profiling of bladder cancer available cohort of The Cancer Genome Atlas (TCGA) to smokers revealed dysregulated amino acid metabolism. -
Serine Proteases with Altered Sensitivity to Activity-Modulating
(19) & (11) EP 2 045 321 A2 (12) EUROPEAN PATENT APPLICATION (43) Date of publication: (51) Int Cl.: 08.04.2009 Bulletin 2009/15 C12N 9/00 (2006.01) C12N 15/00 (2006.01) C12Q 1/37 (2006.01) (21) Application number: 09150549.5 (22) Date of filing: 26.05.2006 (84) Designated Contracting States: • Haupts, Ulrich AT BE BG CH CY CZ DE DK EE ES FI FR GB GR 51519 Odenthal (DE) HU IE IS IT LI LT LU LV MC NL PL PT RO SE SI • Coco, Wayne SK TR 50737 Köln (DE) •Tebbe, Jan (30) Priority: 27.05.2005 EP 05104543 50733 Köln (DE) • Votsmeier, Christian (62) Document number(s) of the earlier application(s) in 50259 Pulheim (DE) accordance with Art. 76 EPC: • Scheidig, Andreas 06763303.2 / 1 883 696 50823 Köln (DE) (71) Applicant: Direvo Biotech AG (74) Representative: von Kreisler Selting Werner 50829 Köln (DE) Patentanwälte P.O. Box 10 22 41 (72) Inventors: 50462 Köln (DE) • Koltermann, André 82057 Icking (DE) Remarks: • Kettling, Ulrich This application was filed on 14-01-2009 as a 81477 München (DE) divisional application to the application mentioned under INID code 62. (54) Serine proteases with altered sensitivity to activity-modulating substances (57) The present invention provides variants of ser- screening of the library in the presence of one or several ine proteases of the S1 class with altered sensitivity to activity-modulating substances, selection of variants with one or more activity-modulating substances. A method altered sensitivity to one or several activity-modulating for the generation of such proteases is disclosed, com- substances and isolation of those polynucleotide se- prising the provision of a protease library encoding poly- quences that encode for the selected variants. -
Fulltext01.Pdf
http://www.diva-portal.org This is the published version of a paper published in Cellular and Molecular Life Sciences (CMLS). Citation for the original published paper (version of record): Cava, F., Lam, H., de Pedro, M., Waldor, M. (2011) Emerging knowledge of regulatory roles of D-amino acids in bacteria. Cellular and Molecular Life Sciences (CMLS), 68(5): 817-831 http://dx.doi.org/10.1007/s00018-010-0571-8 Access to the published version may require subscription. N.B. When citing this work, cite the original published paper. Permanent link to this version: http://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-81861 Cell. Mol. Life Sci. (2011) 68:817–831 DOI 10.1007/s00018-010-0571-8 Cellular and Molecular Life Sciences REVIEW Emerging knowledge of regulatory roles of D-amino acids in bacteria Felipe Cava • Hubert Lam • Miguel A. de Pedro • Matthew K. Waldor Received: 13 July 2010 / Revised: 24 September 2010 / Accepted: 14 October 2010 / Published online: 14 December 2010 Ó The Author(s) 2010. This article is published with open access at Springerlink.com Abstract The D-enantiomers of amino acids have been Keywords D-amino acid Á Racemase Á Stationary phase Á thought to have relatively minor functions in biological Peptidoglycan Á Biofilm Á Regulation processes. While L-amino acids clearly predominate in nat- ure, D-amino acids are sometimes found in proteins that are Abbreviations not synthesized by ribosomes, and D-Ala and D-Glu are NRP Nonribosomal peptide routinely found in the peptidoglycan cell wall of bacteria. PG Peptidoglycan Here, we review recent findings showing that D-amino acids GlcNAc N-acetyl glucosamine have previously unappreciated regulatory roles in the bac- MurNAc N-acetylmuramic acid terial kingdom.