italictitle Taxobox name Pyrococcusfuriosus domain Archaea regnum Euryarchaeota phylum Euryarchaeota classis Thermococci ordo Thermococcales familia Thermococcaceae genus Pyrococcus species P. furiosus binomial Pyrococcusfuriosus binomial authority Erauso et al. 1993 Pyrococcusfuriosus is an extremophile ... marine sediments and studied by growing it in culture in a lab. Pyrococcusfuriosus is noted for its ... of Pyrococcusfuriosus are carbon dioxide CO sub 2 sub and hydrogen H sub 2 sub . The presence of hydrogen ..., P. furiosus does not. Pyrococcusfuriosus is also notable for an unusual and intriguingly simple ... in archaea citation needed . Uses The enzymes of Pyrococcusfuriosus are extremely thermostable. As a consequence, the DNA Polymerase from Pyrococcusfuriosus also known as Pfu DNA polymerase can .... It may be possible to use the enzymes of Pyrococcusfuriosus for applications in such industries ... P. furiosus with a related species of archaea, Pyrococcus abyssi , scientists have tried to determine ... temperature. Involvement in Space Research As Pyrococcusfuriosus can withstand large variations ... in greenhouses on Mars. The research involves taking a gene from Pyrococcusfuriosus and introducing into the plant Arabidopsis thaliana arabidopsis . Discovery Pyrococcusfuriosus was originally ..., and a colleague, Dr. Gerhard Fiala. Pyrococcusfuriosus actually originated a new genus of archaea ... Pyrococcusfuriosus sp. nov. represents a novel genus of marine heterotrophic archaebacteria growing .... Weiss, R. B. Dunn, D. M. year 2001 title Genomic sequence of hyperthermophile, Pyrococcusfuriosus ..., H.G. Daussmann, T. & van der Oost, J. year 2008 title Laboratory evolution of Pyrococcusfuriosus alcohol ... 2005 title A comparison of proteins from Pyrococcusfuriosus and Pyrococcus abyssi barophily in the physicochemical ... archaea stub de Pyrococcusfuriosus et Pyrococcusfuriosus es Pyrococcusfuriosus it Pyrococcusfuriosus ja pt Pyrococcusfuriosus ... more details
structure Three of the Pyrococcus species have been sequenced. P. furiosus is the largest containing 1.9Mb followed by Pyrococcus abyssi P. abyssi with 1.8Mb and Pyrococcus horikoshii P. horikoshii with 1.7Mb ...italic title Taxobox name Pyrococcus domain Archaea regnum Euryarchaeota phylum Euryarchaeota classis Thermococci ordo Thermococcales familia Thermococcaceae genus Pyrococcus genus authority Fiala and Stetter, 1986 subdivision ranks Species biology Species subdivision Pyrococcus abyssi P. abyssi Pyrococcus endeavori P. endeavori Pyrococcusfuriosus P. furiosusPyrococcus glycovorans P. glycovorans Pyrococcus horikoshii P. horikoshii Pyrococcus woesei P. woesei Pyrococcus is a genus biology genus ... www.ncbi.nlm.nih.gov Taxonomy Browser wwwtax.cgi?mode Info&id 2260 webpage on Pyrococcus . Data extracted ... Pyrococcus has similar characteristics of other thermoautotrophican archaea such as Archaeoglobus , and Methanococcus in the respect that they are all thermophile thermophilic and anaerobic. Pyrococcus ... sea depth than the other archaea. Studying Pyrococcus helps give insight to possible mechanisms ... The cells of Pyrococcus are about 0.8 2 m and are slightly irregular cocci in shape. They show a polar ... membrane. Pyrococcus species are anaerobic but vary slightly concerning their metabolism. Peptide fermentation is the principle metabolic pathway however, growth has been observed for P. furiosus ... . Ecology Pyrococcus species inhabit environments with extremely high temperatures such as undersea ... E, Haas B date 1987 title Pyrococcus woesei, sp. nov., an ultra thermophilic marine Archaebacterium ... 70 doi 10.1016 S0723 2020 87 80057 7 cite journal author Fiala G, Stetter KO date 1986 title Pyrococcusfuriosus sp. nov. represents a novel genus of marine heterotrophic archaebacteria growing optimally ... books Scientific databases Taxonomic references taxon Pyrococcus External links Taxonomic links microbe yes NCBI taxID 2260 taxoname Pyrococcus LSPN letter p LSPN taxoname pyrococcus archaea ... more details
Infobox rfam Name Pyrococcus C D box small nucleolar RNA image RF00095.jpg width caption Predicted secondary structure and sequence conservation of snoPyro CD Symbol snoPyro CD AltSymbols CD sno Pyro Rfam RF00095 miRBase miRBase family RNA type Gene Small nuclear RNA snRNA Small nucleolar RNA snoRNA CD box Tax domain Archaea GO GO 0006396 GO 0005730 SO SO 0000593 CAS number EntrezGene HGNCid OMIM PDB RefSeq Chromosome Arm Band LocusSupplementaryData DISPLAYTITLE Pyrococcus C D box small nucleolar RNA Pyrococcus C D box small nucleolar RNA are non coding RNA ncRNA molecules identified in the archaea l genus Pyrococcus which function in the modification of ribosomal RNA rRNA and transfer RNA tRNA . This type of modifiying RNA is usually located in the nucleolus of the eukaryotic cell, which is a major site of ribosomal RNA and snRNA biogenesis, but there is no corresponding visible structure in archaeal cells. This group of ncRNAs are known as snoRNA small nucleolar RNA s snoRNA and also often referred to as a guide RNAs because they direct associated protein enzymes to add a modification to specific nucleotides in target RNAs. C D box RNAs guide the addition of a methyl group CH3 to the 2 O position in the RNA backbone. Computational screens of archaeal genomes have identified SnoRNA C.2FD box C D box snoRNAs in a number of genomes ref name pmid10775111 cite journal author Omer AD, Lowe TM, Russell AG, Ebhardt H, Eddy SR, Dennis PP title Homologs of small nucleolar RNAs in Archaea journal Science volume 288 issue 5465 pages 517 22 year 2000 pmid 10775111 doi 10.1126 science.288.5465.517 ref . In particular 46 small RNAs were identified to be conserved in the genome s of three hyperthermophile Pyrococcus species ref name pmid10736225 cite journal author Gaspin C, Cavaill ... RNAs lessons from the Pyrococcus genomes journal J. Mol. Biol. volume 297 issue 4 pages 895 906 year ... name Pyrococcus C D box small nucleolar RNA http lowelab.ucsc.edu snoRNAdb snoRNAdb Small nucleolar ... more details
enzyme Name glyceraldehyde 3 phosphate dehydrogenase ferredoxin EC number 1.2.7.6 CAS number IUBMB EC number 1 2 7 6 GO code 0043797 image width caption In enzymology , a glyceraldehyde 3 phosphate dehydrogenase ferredoxin EC number 1.2.7.6 is an enzyme that catalysis catalyzes the chemical reaction D glyceraldehyde 3 phosphate H sub 2 sub O 2 oxidized ferredoxin math rightleftharpoons math 3 phospho D glycerate 2 H sup sup 2 reduced ferredoxin The 3 substrate biochemistry substrates of this enzyme are D glyceraldehyde 3 phosphate , water H sub 2 sub O , and oxidized ferredoxin , whereas its 3 product chemistry products are 3 phospho D glycerate , hydrogen ion H sup sup , and reduced ferredoxin . This enzyme belongs to the family of oxidoreductase s, specifically those acting on the aldehyde or oxo group of donor with an iron sulfur protein as acceptor. The systematic name of this enzyme class is D glyceraldehyde 3 phosphate ferredoxin oxidoreductase . Other names in common use include GAPOR , glyceraldehyde 3 phosphate Fd oxidoreductase , and glyceraldehyde 3 phosphate ferredoxin reductase . References reflist 1 cite journal author Mukund S, Adams MW year 1995 title Glyceraldehyde 3 phosphate ferredoxin oxidoreductase, a novel tungsten containing enzyme with a potential glycolytic role in the hyperthermophilic archaeon Pyrococcus furiosus journal J. Biol. Chem. volume 270 pages 8389&ndash 92 pmid 7721730 doi 10.1074 jbc.270.15.8389 issue 15 cite journal author Roy R, Menon AL, Adams MW year 2001 title Aldehyde oxidoreductases from Pyrococcus furiosus journal Methods Enzymol. volume 331 pages 132&ndash 44 pmid 11265456 doi 10.1016 S0076 6879 01 31052 2 chapter 11 Aldehyde Oxidoreductases from Pyrococcus furiosus series Methods in Enzymology isbn 9780121822323 Category EC 1.2.7 Category Enzymes of unknown structure 1.2 enzyme stub it Gliceraldeide 3 fosfato deidrogenasi ferredossina ja 3 ... more details
enzyme with a potential glycolytic role in the hyperthermophilic archaeon Pyrococcusfuriosus ... MW title Pyruvate ferredoxin oxidoreductase from the hyperthermophilic archaeon, Pyrococcusfuriosus ... Roy R, Menon AL, Adams MW year 2001 title Aldehyde oxidoreductases from Pyrococcusfuriosus journal ... 1991 title The novel tungsten iron sulfur protein of the hyperthermophilic archaebacterium, Pyrococcusfuriosus, is an aldehyde ferredoxin oxidoreductase. Evidence for its participation in a unique ... more details
their work as Lundberg et al., A High Fidelity Thermostable DNA Polymerase Isolated from PyrococcusFuriosus, Strategies 4 34 35 1991 and Gene in December of that year Gene. 1991 Dec 12 108 1 1 6 . U.S. ... 2F 22Pyrococcus furiosus 22 AND ABST 2Fpolymerase 29&Refine Refine Search&Query abst 2F 22Pyrococcus furiosus 22 and abst 2Fpolymerase and an 2Fstratagene Stratagene s Pfu U.S. Patents http www.patentlens.net ... more details
with a broad substrate specificity from the archaebacterium Pyrococcusfuriosus . ref name pmid8226989 ... archaebacterium Pyrococcusfuriosus. journal J Biol Chem year 1993 volume 268 issue ... more details
Pyrococcus glycovorans P. glycovorans small Barbier et al. 1999 small 5 clade 1 Pyrococcusfuriosus P. furiosus small Fiala and Stetter 1986 small 2 Pyrococcus horikoshii P. horikoshii small Gonz lez ... clade label1 Pyrococcus 1 clade 1 ? Pyrococcus abyssi P. abyssi small Erauso et al. 1993 small 2 ? Pyrococcus woesei P. woesei small Zillig 1988 small 3 ? Pyrococcus yayanosii P. yayanosii small ... E, Haas B date 1987 title Pyrococcus woesei, sp. nov., an ultra thermophilic marine Archaebacterium ... more details
This article was auto generated by User Polbot . Taxobox name Carolina madtom image status DD status system IUCN2.3 regnum Animalia phylum Chordata classis Actinopterygii ordo Siluriformes familia Ictaluridae genus Noturus species N. furiosus binomial Noturus furiosus binomial authority David Starr Jordan D. S. Jordan & Seth Eugene Meek Meek , 1889 synonyms The Carolina madtom Noturus furiosus is a species of fish in the Ictaluridae family. It is Endemism endemic to North Carolina . Source Gimenez Dixon, M. 1996. http www.iucnredlist.org search details.php 14901 all Noturus furiosus . http www.iucnredlist.org 2006 IUCN Red List of Threatened Species. Downloaded on 4 August 2007. Category Noturus Category Endemic fauna of North Carolina Category Fish of the United States catfish stub ca Noturus furiosus es Noturus furiosus pt Noturus furiosus sr Noturus furiosus vi Carolina madtom ... more details
enzyme Name ADP specific phosphofructokinase EC number 2.7.1.146 CAS number 237739 62 7 IUBMB EC number 2 7 1 146 GO code 0043844 image width caption In enzymology , an ADP specific phosphofructokinase EC number 2.7.1.146 is an enzyme that catalysis catalyzes the chemical reaction ADP D fructose 6 phosphate math rightleftharpoons math AMP D fructose 1,6 bisphosphate Thus, the two substrate biochemistry substrates of this enzyme are adenosine diphosphate ADP and D fructose 6 phosphate , whereas its two product chemistry products are adenosine monophosphate AMP and D fructose 1,6 bisphosphate . This enzyme belongs to the family of transferase s, specifically those transferring phosphorus containing groups phosphotransferase s with an alcohol group as acceptor. The systematic name of this enzyme class is ADP D fructose 6 phosphate 1 phosphotransferase . This enzyme is also called ADP 6 phosphofructokinase, ADP dependent phosphofructokinase . Structural studies As of late 2007, only one tertiary structure structure has been solved for this class of enzymes, with the Protein Data Bank PDB accession code PDB link 1U2X . References reflist 1 cite journal author WM date 1999 title Molecular and biochemical characterization of the ADP dependent phosphofructokinase from the hyperthermophilic archaeon Pyrococcus furiosus journal J. Biol. Chem. volume 274 pages 21023&ndash 8 pmid 10409652 doi 10.1074 jbc.274.30.21023 last2 Verhees first2 CH last3 Van Der Oost first3 J last4 Kengen first4 SW last5 Stams first5 AJ last6 De Vos first6 WM issue 30 enzyme stub Category EC 2.7.1 Category Enzymes of known structure ... more details
enzyme Name UMP kinase EC number 2.7.4.22 CAS number 9036 23 1 IUBMB EC number 2 7 4 22 GO code 0033862 image width caption In enzymology , an UMP kinase EC number 2.7.4.22 is an enzyme that catalysis catalyzes the chemical reaction ATP UMP math rightleftharpoons math ADP UDP Thus, the two substrate biochemistry substrates of this enzyme are adenosine triphosphate ATP and uridine monophosphate UMP , whereas its two product chemistry products are adenosine diphosphate ADP and uridine diphosphate UDP . This enzyme belongs to the family of transferase s, specifically those transferring phosphorus containing groups phosphotransferase s with a phosphate group as acceptor. The systematic name of this enzyme class is ATP UMP phosphotransferase . Other names in common use include uridylate kinase , UMPK , uridine monophosphate kinase , PyrH , UMP kinase , and SmbA . This enzyme participates in pyrimidine metabolism . Structural studies As of March 2010, 19 tertiary structure structures have been solved for this class of enzymes, and are deposited in the Protein Data Bank PDB . All have a 3 layer aba sandwich architecture CATH code 3.40.1160.10 . These include accession codes PDB link 2J4J , PDB link 2J4K , PDB link 2J4L , and PDB link 2VA1 . Search for all UMP Kinases in the PDB using the http www.ebi.ac.uk pdbe srv PDBeXplore enzyme enzyme Browser at http www.pdbe.org PDBe . input the EC number References reflist 1 cite journal author Gilles AM, Barzu O date 1995 title Escherichia coli UMP kinase, a member of the aspartokinase family, is a hexamer regulated by guanine nucleotides and UTP journal Biochemistry. volume 34 pages 5066 5074 pmid 7711027 doi 10.1021 bi00015a018 issue 15 cite journal author Marco Marin C, Gil Ortiz F, Rubio V date 2005 title The crystal structure of Pyrococcus furiosus UMP kinase provides insight into catalysis and regulation in microbial pyrimidine nucleotide biosynthesis journal J. Mol. Biol. volume 352 pages 438 454 pmid 16095620 doi 10.1016 j. ... more details
File Karl Stetter.jpg thumb Karl Stetter. Karl Otto Stetter born July 16, 1941 is a German microbiologist and authority on astrobiology . He is an expert on microbial life at high temperatures. Career Stetter was born in Munich and studied biology at the Technische Universit t Munich. He wrote his doctoral dissertation on Lactobacillus lactobacilli . From 1980 to 2002 he was professor at, and head of, the department of microbiology and of the Archaea center of the University of Regensburg . The majority of Professor Stetter s research has focused on sampling, isolating and characterizing archaeal organisms which comprise the third domain biology domain of life, particularly undiscovered extremely heat loving hyperthermophilic bacterium bacteria and Archaea , also called extremophile s, growing optimally between 80 and 113 C. Major discovery Nanoarchaeum equitans , an archaeal microorganism containing the world s smallest known genome , was discovered by Stetter in 2002 in a hydrothermal vent off the coast of Iceland . This archaebacterium was described in the scientific journal Nature in May 2002. Discoveries Among the other extremophiles discovered by Dr Stetter has been Pyrococcus furiosus , which was found on the Italian island of Vulcano Island Vulcano in 1981. This extremophile was the source of Pfu DNA polymerase. Stetter also discovered Aquifex aeolicus and Aquifex pyrophilus . Awards and memberships In 2003, Stetter was honored with the Leeuwenhoek Medal by the Royal Netherlands Academy of Arts and Sciences , an award given every 10 years to the scientist who has made the most outstanding contributions to the advancement of microbiology. Professor Stetter is member of the German Academy of Natural Scientists Leopoldina Deutsche Akademie der Naturforscher Leopoldina American Society of Microbiology ASM Bayerische Akademie der Wissenschaften Department of Microbiology and Molecular Genetics and Institute of Geophysics and Planetary Science IGPP , UCLA Deutsche ... more details
enzyme Name 3 methyl 2 oxobutanoate dehydrogenase ferredoxin EC number 1.2.7.7 CAS number IUBMB EC number 1 2 7 7 GO code 0043807 image width caption In enzymology , a 3 methyl 2 oxobutanoate dehydrogenase ferredoxin EC number 1.2.7.7 is an enzyme that catalysis catalyzes the chemical reaction 3 methyl 2 oxobutanoate CoA oxidized ferredoxin math rightleftharpoons math S 2 methylpropanoyl CoA CO sub 2 sub reduced ferredoxin The 3 substrate biochemistry substrates of this enzyme are 3 methyl 2 oxobutanoate , coenzyme A CoA , and oxidized ferredoxin , whereas its 3 product chemistry products are S 2 methylpropanoyl CoA , carbon dioxide CO sub 2 sub , and reduced ferredoxin . This enzyme belongs to the family of oxidoreductase s, specifically those acting on the aldehyde or oxo group of donor with an iron sulfur protein as acceptor. The systematic name of this enzyme class is . Other names in common use include 2 ketoisovalerate ferredoxin reductase , 3 methyl 2 oxobutanoate synthase ferredoxin , VOR , branched chain ketoacid ferredoxin reductase , branched chain oxo acid ferredoxin reductase , keto valine ferredoxin oxidoreductase , ketoisovalerate ferredoxin reductase , and 2 oxoisovalerate ferredoxin reductase . References reflist 1 cite journal author Heider J, Mai X, Adams MW date 1996 title Characterization of 2 ketoisovalerate ferredoxin oxidoreductase, a new and reversible coenzyme A dependent enzyme involved in peptide fermentation by hyperthermophilic archaea journal J. Bacteriol. volume 178 pages 780&ndash 7 pmid 8550513 issue 3 pmc 177725 cite journal author Tersteegen A, Linder D, Thauer RK, Hedderich R date 1997 title Structures and functions of four anabolic 2 oxoacid oxidoreductases in Methanobacterium thermoautotrophicum journal Eur. J. Biochem. volume 244 pages 862&ndash 8 pmid 9108258 doi 10.1111 j.1432 1033.1997.00862.x issue 3 cite journal author Schut GJ, Menon AL, Adams MW date 2001 title 2 keto acid oxidoreductases from Pyrococcus furiosus and Th ... more details
enzyme Name rubredoxin NAD P reductase EC number 1.18.1.4 CAS number 114514 31 7 IUBMB EC number 1 18 1 4 GO code 0015045 image width caption In enzymology , a rubredoxin NAD P reductase EC number 1.18.1.4 is an enzyme that catalysis catalyzes the chemical reaction reduced rubredoxin NAD P math rightleftharpoons math oxidized rubredoxin NAD P H H sup sup The 3 substrate biochemistry substrates of this enzyme are reduced rubredoxin , nicotinamide adenine dinucleotide NAD sup sup , and nicotinamide adenine dinucleotide phosphate NADP sup sup , whereas its 4 product chemistry products are oxidized rubredoxin , nicotinamide adenine dinucleotide NADH , nicotinamide adenine dinucleotide phosphate NADPH , and hydrogen ion H sup sup . This enzyme belongs to the family of oxidoreductase s, specifically those acting on iron sulfur proteins as donor with NAD or NADP as acceptor. The systematic name of this enzyme class is rubredoxin NAD P oxidoreductase . Other names in common use include rubredoxin nicotinamide adenine dinucleotide phosphate reductase , rubredoxin nicotinamide adenine , dinucleotide phosphate reductase , NAD P rubredoxin oxidoreductase , and NAD P H rubredoxin oxidoreductase . This enzyme participates in fatty acid metabolism . References reflist 1 cite journal author Petitdemange H, Blusson H, Gay R date 1981 title Detection of NAD P H rubredoxin oxidoreductases in Clostridia journal Anal. Biochem. volume 116 pages 564&ndash 70 pmid 6274224 doi 10.1016 0003 2697 81 90403 6 issue 2 cite journal author Ma K, Adams MW date 1999 title A hyperactive NAD P H Rubredoxin oxidoreductase from the hyperthermophilic archaeon Pyrococcus furiosus journal J. Bacteriol. volume 181 pages 5530&ndash 3 pmid 10464233 issue 17 pmc 94068 1.18 enzyme stub Category EC 1.18.1 Category NADPH dependent enzymes Category NADH dependent enzymes Category Enzymes of unknown structure it Rubredossina NAD P reduttasi ja NAD P ... more details
Infobox protein family Symbol GHMP kinases N Name GHMP kinases N terminal domain image PDB 1k47 EBI.jpg width caption crystal structure of the streptococcus pneumoniae phosphomevalonate kinase pmk Pfam PF00288 Pfam clan CL0329 InterPro IPR006204 SMART PROSITE PDOC00545 MEROPS SCOP 1fwl TCDB OPM family OPM protein CAZy CDD Infobox protein family Symbol GHMP kinases C Name GHMP kinases C terminal image PDB 1s4e EBI.jpg width caption pyrococcus furiosus galactokinase in complex with galactose, adp and magnesium Pfam PF08544 Pfam clan InterPro IPR013750 SMART PROSITE PDOC00545 MEROPS SCOP 1fwl TCDB OPM family OPM protein CAZy CDD In molecular biology, the GHMP kinase family is a protein family family of kinase enzymes . Members of this family include homoserine kinase homoserine kinases EC number 2.7.1.39 , galactokinase galactokinases EC number 2.7.1.6 , and mevalonate kinase mevalonate kinases EC number 2.7.1.36 . These kinases make up the GHMP kinase Superfamily molecular biology superfamily of Adenosine triphosphate ATP dependent enzyme s. ref name pmid8382990 cite journal author Bork P, Sander C, Valencia A title Convergent evolution of similar enzymatic function on different protein folds the hexokinase, ribokinase, and galactokinase families of sugar kinases journal Protein Sci. volume 2 issue 1 pages 31 40 year 1993 month January pmid 8382990 pmc 2142297 doi 10.1002 pro.5560020104 url ref These enzymes are involved in the biosynthesis of isoprene isoprenes and amino acid s as well as in carbohydrate metabolism . These enzymes contain, in their N terminal section, a conserved sequence conserved Glycine Gly Serine Ser rich region which is probably involved in the binding of ATP. ref name pmid1846667 cite journal author Tsay YH, Robinson GW title Cloning and characterization of ERG8, an essential gene of Saccharomyces cerevisiae that encodes phosphomevalonate kinase journal Mol. Cell. Biol. volume 11 issue 2 pages 620 31 year 1991 month February pmid 1846667 pmc 35 ... more details
for the French ships French ship Argonaute Infobox protein family Symbol Piwi Name Argonaute Piwi domain image 1u04 argonaute.png width caption An argonaute protein from Pyrococcus furiosus . Protein Data Bank PDB PDBe 1U04 . PIWI domain is on the right, PAZ domain to the left. Pfam PF02171 Pfam clan InterPro IPR003165 SMART PROSITE PS50822 MEROPS SCOP TCDB OPM family OPM protein CDD cd02826 PDB Infobox protein family Symbol Paz Name Argonaute Paz domain image width caption Pfam PF12212 Pfam clan InterPro IPR021103 SMART PROSITE MEROPS SCOP b.34.14.1 TCDB OPM family OPM protein CDD PDB Image Argonaute 1u04 1ytu composite.png thumb Left A full length argonaute protein from the archaea species Pyrococcus furiosus . Protein Data Bank PDB http www.pdbe.org 1u04 1U04 . Right The PIWI domain of an argonaute protein in complex with double stranded RNA Protein Data Bank PDB http www.pdbe.org 1ytu 1YTU . The base stacking interaction between the 5 base on the guide strand and a conserved tyrosine residue light blue is highlighted the stabilizing divalent cation magnesium is shown as a gray sphere. Argonaute proteins are the catalytic components of the RNA induced silencing complex RISC , the protein complex responsible for the gene silencing phenomenon known as RNA interference RNAi . ref name Cenik cite journal author Cenik ES, Zamore PD. title Argonaute proteins. journal Current Biology year 2011 volume 21 issue 12 pages R446 9 pmid 21683893 doi 10.1016 j.cub.2011.05.020 ref Argonaute proteins bind different classes of small non coding RNAs, including microRNA s miRNAs , small interfering RNA s siRNAs and Piwi interacting RNA s piRNAs . ref name Zamore cite journal author Ghildiyal M, Zamore PD year 2009 title Small silencing RNAs an expanding universe url journal Nat. Rev. Genet volume 10 issue 2 pages 94 108 doi 10.1038 nrg2504 pmid 19148191 pmc 2724769 ref Small RNAs guide Argonaute proteins to their specific targets through sequence complementarity, which typically lea ... more details
from Pyrococcusfuriosus year 1992 journal Journal of Biomolecular NMR volume 2 issue 5 pages 527 ... 113 substituted rubredoxin from Pyrococcusfuriosus year 1992 journal J. Am. Chem. Soc. volume 114 issue ... more details
enzyme Name superoxide reductase EC number 1.15.1.2 CAS number 250679 67 5 IUBMB EC number 1 15 1 2 GO code 0050605 image width caption Superoxide reductase is an enzyme that catalysis catalyzes the conversion of highly reactive and toxic superoxide O sub 2 sub sup sup into less toxic hydrogen peroxide H sub 2 sub O sub 2 sub and molecular oxygen O sub 2 sub reduced rubredoxin O sub 2 sub sup sup 2 H sup sup math rightleftharpoons math rubredoxin H sub 2 sub O sub 2 sub Fe sup 2 sup O sub 2 sub sup sup 2 H sup sup math rightleftharpoons math Fe sup 3 sup H sub 2 sub O sub 2 sub Hydrogen peroxide in turn is converted to molecular oxygen by the enzyme catalase . The 3 substrate biochemistry substrates of this enzyme are reduced rubredoxin , superoxide , and hydrogen ion H sup sup , whereas its two product chemistry products are rubredoxin and hydrogen peroxide H sub 2 sub O sub 2 sub . This enzyme belongs to the family of oxidoreductase s, specifically those acting on superoxide as acceptor only sub subclass identified to date . The systematic name of this enzyme class is rubredoxin superoxide oxidoreductase . Other names in common use include neelaredoxin , and desulfoferrodoxin . Structural studies As of 2007 alt As of late 2007 , 9 tertiary structure structures have been solved for this class of enzymes, with Protein Data Bank PDB accession codes PDB link 1VZG , PDB link 1VZH , PDB link 1VZI , PDB link 1Y07 , PDB link 2AMU , PDB link 2HVB , PDB link 2JI1 , PDB link 2JI2 , and PDB link 2JI3 . References reflist Further reading refbegin cite journal author Jenney FE Jr, Verhagen MF, Cui X, Adams MW date 1999 title Anaerobic microbes oxygen detoxification without superoxide dismutase journal Science. volume 286 pages 306&ndash 9 pmid 10514376 doi 10.1126 science.286.5438.306 issue 5438 cite journal author Yeh AP, Hu Y, Jenney FE Jr, Adams MW, Rees DC date 2000 title Structures of the superoxide reductase from Pyrococcus furiosus in the oxidized and reduced states jour ... more details
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