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 extremophilic species of Archaea . It is notable for having an optimum growth temperature of 100 C a temperature that would destroy most living organisms , and for being one of the few organisms .... Properties Pyrococcusfuriosus is noted for its rapid doubling time of 37 minutes under optimal ... hydrolyzed to glucose . Pyrococcusfuriosus is also notable for an unusual and intriguingly ... pnas.1331436100 ref Uses The enzymes of Pyrococcusfuriosus are extremely thermostable. As a consequence, the DNA Polymerase from Pyrococcusfuriosus also known as Pfu DNA polymerase can be used in the polymerase chain reaction PCR DNA amplification process. Involvement in Space Research As Pyrococcusfuriosus can withstand large variations in temperature 100 C , it is being used to do research ... taking a gene from Pyrococcusfuriosus and introducing into the plant Arabidopsis thaliana arabidopsis . Discovery Pyrococcusfuriosus was originally isolated Anaerobic organism anaerobically from geothermally ... of the complete genome of Pyrococcusfuriosus was completed in 2001 by scientists at the University ..., G. Stetter, K. O. year 1986 title Pyrococcusfuriosus sp. nov. represents a novel genus of marine ..., Pyrococcusfuriosus implications for physiology and enzymology journal Methods in Enzymology ... Archaea species archaea stub de Pyrococcusfuriosus es Pyrococcusfuriosus it Pyrococcusfuriosus ja pt Pyrococcusfuriosus ..., coding for some 2,065 proteins. The extremophile s scientific name The name lang grc Latn Pyrococcus ... to grow in temperatures of around 100 degrees Celsius. The species name lang la furiosus means rushing ... more details
. Genome Structure Three of the Pyrococcus species have been sequenced. P. furiosus is the largest ... Fiala G, Stetter KO date 1986 title Pyrococcusfuriosus sp. nov. represents a novel genus of marine ...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 In alpha taxonomy taxonomy , Pyrococcus is a genus biology genus of the Thermococcaceae . ref See the National Center for Biotechnology Information NCBI http www.ncbi.nlm.nih.gov Taxonomy Browser wwwtax.cgi?mode Info&id 2260 webpage on Pyrococcus ... and Significance Pyrococcus has similar characteristics of other archaea such as Archaeoglobus .... Pyrococcus differs, however, because it s optimal growth temperature is nearly 100 sup o sup C and dwells at a greater sea depth than the other archaea. Studying Pyrococcus helps give insight to possible ... was detected between species as well. Cell Structure and Metabolism The cells of Pyrococcus are about ... by an S layer enclosing a periplasmic space around the cytoplasmic membrane. Pyrococcus ... metabolic pathway however, growth has been observed for P. furiosus and P. abyssi on starch ... for growth, growth is enhanced with the addition of S sup o sup . Ecology Pyrococcus species inhabit ... Pyrococcus woesei, sp. nov., an ultra thermophilic marine Archaebacterium, representing a novel ...&ndash 61 doi 10.1007 BF00413027 Scientific 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 stub Category Archaea genera es Pyrococcus fr Pyrococcus ja ... more details
orphan date February 2009 Rfam box acc RF00095 description Pyrococcus C D box small nucleolar RNA abbreviation snoPyro CD avg length 56.70 avg identity 60.00 type Gene snRNA snoRNA CD box se Griffiths Jones SR ss Predicted PFOLD release 10.0 Pyrococcus C D box small nucleolar RNA are non coding RNA ncRNA molecules identified in the archaeal 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 genomes of three hyperthermophile Pyrococcus species ref name pmid10736225 cite journal author Gaspin C, Cavaill J, Erauso G, Bachellerie JP title Archaeal homologs of eukaryotic methylation guide small nucleolar RNAs lessons from the Pyrococcus genomes journal J. Mol. Biol. volume 297 issue 4 pages 895 906 year 2000 pmid 10736225 doi 10.1006 jmbi.2000.3593 ref . References references External links Rfam id RF00095 name Pyrococcus C D box small nucleolar RNA http lowelab.ucsc.edu snoRNAdb snoRNAdb molecular cell biology stub Category Small nuclear RNA ... 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 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 Name Aldehyde ferredoxin oxidoreductase EC number 1.2.7.5 CAS number 138066 90 7 IUBMB EC number 1 2 7 5 GO code image width caption In enzymology , an aldehyde ferredoxin oxidoreductase EC number 1.2.7.5 is an enzyme that catalysis catalyzes the chemical reaction an aldehyde H sub 2 sub O 2 oxidized ferredoxin math rightleftharpoons math an acid 2 H sup sup 2 reduced ferredoxin The 3 substrate biochemistry substrates of this enzyme are aldehyde , water H sub 2 sub O , and oxidized ferredoxin , whereas its 3 product chemistry products are acid , 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 aldehyde ferredoxin oxidoreductase . This enzyme is also called AOR . References reflist 1 cite journal author Mukund S, Adams MW date 1991 title The novel tungsten iron sulfur protein of the hyperthermophilic archaebacterium, Pyrococcus furiosus, is an aldehyde ferredoxin oxidoreductase. Evidence for its participation in a unique glycolytic pathway journal J. Biol. Chem. volume 266 pages 14208&ndash 16 pmid 1907273 issue 22 cite journal author Johnson JL, Rajagopalan KV, Mukund S, Adams MW date 1993 title Identification of molybdopterin as the organic component of the tungsten cofactor in four enzymes from hyperthermophilic Archaea journal J. Biol. Chem. volume 268 pages 4848&ndash 52 pmid 8444863 issue 7 cite journal author Chan MK, Mukund S, Kletzin A, Adams MW, Rees DC date 1995 title Structure of a hyperthermophilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase journal Science. volume 267 pages 1463&ndash 9 pmid 7878465 doi 10.1126 science.7878465 issue 5203 cite journal author Roy R, Menon AL, Adams MW date 2001 title Aldehyde oxidoreductases from Pyrococcus furiosus journal Methods Enzymol. volume 331 pages 132&ndash 44 pmid 11265456 doi 10.1016 S0076 ... more details
Polymerase Isolated from PyrococcusFuriosus, Strategies 4 34 35 1991 and Gene in December of that year ... adv.htm&r 0&f S&l 50&d PTXT&RS 28ABST 2F 22Pyrococcus furiosus 22 AND ABST 2Fpolymerase 29&Refine Refine Search&Query abst 2F 22Pyrococcus furiosus 22 and abst 2Fpolymerase and an 2Fstratagene Stratagene ... more details
for the French ships French ship Argonaute Image 1u04 argonaute.png thumb An argonaute protein from Pyrococcusfuriosus . Protein Data Bank PDB http www.pdbe.org 1u04 1U04 Image Argonaute 1u04 1ytu composite.png thumb Left A full length argonaute protein from the archaea species Pyrococcusfuriosus . 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 . Argonaute proteins bind small interfering RNA siRNA fragments and have endonuclease activity directed against messenger RNA mRNA strands that are base pair complementary to their bound siRNA fragment. The proteins are also partially responsible for selection of the guide strand and destruction of the passenger strand of the siRNA substrate. ref name Rand Rand TA, Petersen S, Du F, Wang X. 2005 . Argonaute2 cleaves the anti guide strand of siRNA during RISC activation. Cell 123 4 621 9. ref The structural basis for binding of RNA to the argonaute protein has been examined by X ray crystallography of the binding structural domain domain of an RNA bound argonaute protein. The phosphorylation phosphorylated 5 end of the RNA strand enters a conservation genetics conserved basicity basic surface binding site pocket and makes contacts through a divalent cation such as magnesium and by aromaticity aromatic stacking chemistry stacking between the 5 nucleotide in the siRNA and a conserved tyrosine residue. This site is thought to form a nucleation site for the binding of the siRNA to its mRNA target. ref name Ma cite ... 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 Jordan & 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 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
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 Gesellschaft f r Hygiene und Mikrobiologi ... 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
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 Orphan date February 2009 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&ndash 74 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&nd ... 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
from Pyrococcusfuriosus year 1992 journal Journal of Biomolecular NMR volume 2 issue 5 pages ... 113 substituted rubredoxin from Pyrococcusfuriosus year 1992 journal J. Am. Chem. Soc. volume ... more details
gallery Image Jmol screenshot 2hvy.jpg Crystal structure of an H ACA box RNP from Pyrococcusfuriosus Image Jmol screenshot hemoglobin.png Highlighting two salt bridges in hemoglobin tetramer ... more details
enzyme Name ADP specific glucokinase EC number 2.7.1.147 CAS number 173585 07 4 IUBMB EC number 2 7 1 147 GO code 0043843 image width caption PBB geneid 83440 In enzymology , an ADP specific glucokinase EC number 2.7.1.147 also known as ADP dependent glucokinase is an enzyme that catalysis catalyzes the chemical reaction ADP D glucose math rightleftharpoons math AMP D glucose 6 phosphate Thus, the two substrate biochemistry substrates of this enzyme are adenosine diphosphate ADP and D glucose , whereas its two product chemistry products are adenosine monophosphate AMP and D glucose 6 phosphate . This enzyme belongs to the family of transferase s, specifically those transferring phosphorus containing groups phosphotransferase s with an alcohol group as acceptor. In humans, the ADP dependent glucokinase is encoded by the ADPGK gene . ref name pmid14975750 cite journal author Ronimus RS, Morgan HW title Cloning and biochemical characterization of a novel mouse ADP dependent glucokinase journal Biochem. Biophys. Res. Commun. volume 315 issue 3 pages 652 8 year 2004 month March pmid 14975750 doi 10.1016 j.bbrc.2004.01.103 url issn ref 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 1GC5 . References reflist Further reading refbegin 2 cite journal author Kengen SW, Tuininga JE, de Bok FA, Stams AJ, de Vos WM year 1995 title Purification and characterization of a novel ADP dependent glucokinase from the hyperthermophilic archaeon Pyrococcus furiosus journal J. Biol. Chem. volume 270 pages 30453&ndash 7 pmid 8530474 doi 10.1074 jbc.270.51.30453 issue 51 cite journal author Gerhard DS, Wagner L, Feingold EA, et al. title The status, quality, and expansion of the NIH full length cDNA project the Mammalian Gene Collection MGC . journal Genome Res. volume 14 issue 10B pages 2121 7 year 2004 pmid 15489334 doi 10.1101 gr.2596504 pmc 528928 cite journal autho ... more details
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