A genus of anaerobic, chemolithotropic coccoid ARCHAEA, in the family DESULFUROCOCCACEAE. They live in marine environments.
A family of archaea, in the order DESULFUROCOCCALES, consisting of anaerobic cocci which utilize peptides, proteins or carbohydrates facultatively by sulfur respiration or fermentation. There are eight genera: AEROPYRUM, Desulfurococcus, Ignicoccus, Staphylothermus, Stetteria, Sulfophoboccus, Thermodiscus, and Thermosphaera. (From Bergey's Manual of Systematic Bacteriology, 2d ed)
A kingdom in the domain ARCHAEA comprised of thermoacidophilic, sulfur-dependent organisms. The two orders are SULFOLOBALES and THERMOPROTEALES.
Proteins found in any species of archaeon.
A transfer RNA which is specific for carrying threonine to sites on the ribosomes in preparation for protein synthesis.
A family of THERMOPROTEALES consisting of variable length rigid rods without septa. They grow either chemolithoautotrophically or by sulfur respiration. The four genera are: PYROBACULUM; THERMOPROTEUS; Caldivirga; and Thermocladium. (From Bergey's Manual of Systematic Bacteriology, 2d ed)
Deoxyribonucleic acid that makes up the genetic material of archaea.
The genetic complement of an archaeal organism (ARCHAEA) as represented in its DNA.
Hot springs on the ocean floor. They are commonly found near volcanically active places such as mid-oceanic ridges.
One of the three domains of life (the others being BACTERIA and Eukarya), formerly called Archaebacteria under the taxon Bacteria, but now considered separate and distinct. They are characterized by: (1) the presence of characteristic tRNAs and ribosomal RNAs; (2) the absence of peptidoglycan cell walls; (3) the presence of ether-linked lipids built from branched-chain subunits; and (4) their occurrence in unusual habitats. While archaea resemble bacteria in morphology and genomic organization, they resemble eukarya in their method of genomic replication. The domain contains at least four kingdoms: CRENARCHAEOTA; EURYARCHAEOTA; NANOARCHAEOTA; and KORARCHAEOTA.
A subcategory of chaperonins found in ARCHAEA and the CYTOSOL of eukaryotic cells. Group II chaperonins form a barrel-shaped macromolecular structure that is distinct from GROUP I CHAPERONINS in that it does not utilize a separate lid like structure to enclose proteins.
Ribonucleic acid in archaea having regulatory and catalytic roles as well as involvement in protein synthesis.
An enzyme that activates threonine with its specific transfer RNA. EC 6.1.1.3.
The extent to which an enzyme retains its structural conformation or its activity when subjected to storage, isolation, and purification or various other physical or chemical manipulations, including proteolytic enzymes and heat.
Viruses whose hosts are in the domain ARCHAEA.
The first enzyme of the proline degradative pathway. It catalyzes the oxidation of proline to pyrroline-5-carboxylic acid in the presence of oxygen and water. The action is not reversible. The specific activity of proline oxidase increases with age. EC 1.5.3.-.
The protein complement of an organism coded for by its genome.
A general term collectively applied to tumors associated with the APUD CELLS series, irrespective of their specific identification.
Messages between computer users via COMPUTER COMMUNICATION NETWORKS. This feature duplicates most of the features of paper mail, such as forwarding, multiple copies, and attachments of images and other file types, but with a speed advantage. The term also refers to an individual message sent in this way.
The systematic study of the complete complement of proteins (PROTEOME) of organisms.
Uncontrolled release of biological material from its containment. This either threatens to, or does, cause exposure to a biological hazard. Such an incident may occur accidentally or deliberately.
An mRNA metabolic process that distinguishes a normal STOP CODON from a premature stop codon (NONSENSE CODON) and facilitates rapid degradation of aberrant mRNAs containing premature stop codons.
An amino acid-specifying codon that has been converted to a stop codon (CODON, TERMINATOR) by mutation. Its occurance is abnormal causing premature termination of protein translation and results in production of truncated and non-functional proteins. A nonsense mutation is one that converts an amino acid-specific codon to a stop codon.
The extent to which an RNA molecule retains its structural integrity and resists degradation by RNASE, and base-catalyzed HYDROLYSIS, under changing in vivo or in vitro conditions.
A publication issued at stated, more or less regular, intervals.
Antisera from immunized animals that is purified and used as a passive immunizing agent against specific BACTERIAL TOXINS.
A bibliographic database that includes MEDLINE as its primary subset. It is produced by the National Center for Biotechnology Information (NCBI), part of the NATIONAL LIBRARY OF MEDICINE. PubMed, which is searchable through NLM's Web site, also includes access to additional citations to selected life sciences journals not in MEDLINE, and links to other resources such as the full-text of articles at participating publishers' Web sites, NCBI's molecular biology databases, and PubMed Central.
Ribulose substituted by one or more phosphoric acid moieties.
An order of CRENARCHAEOTA comprised of irregular coccoid to disc-shaped, hyperthermophiles, and found in submarine hydrothermal systems and solfataric hot springs.
Nucleosides in which the base moiety is substituted with one or more sulfur atoms.

Cloning, expression, and characterization of the first archaeal ATP-dependent glucokinase from aerobic hyperthermophilic archaeon Aeropyrum pernix. (1/73)

The gene encoding the ATP-dependent glucokinase of hyperthermophilic archaeon Aeropyrum pernix was identified, cloned, and functionally expressed in Escherichia coli. The deduced amino acid sequence showed 40% identity to that of the putative glucokinase from hyperthermophilic archaeon Pyrobacurum aerophilum. The purified recombinant enzyme was a monomer with a molecular mass of 35 kDa. The enzyme retained its full activity on heating at 70 degrees C for 10 min and retained 65% of the activity after 10-min incubation at 100 degrees C. The enzyme exclusively catalyzed the phosphorylation of D-glucose using ATP as a phosphoryl donor. ITP was accepted in addition to ATP. The rate dependence with both glucose and ATP followed Michaelis-Menten kinetics, with apparent K(m) values of 0.054 and 0.50 mM, respectively. The enzyme activity required divalent cations; Mg(2+), which was most effective, could partially be replaced by Mn(2+) or Ca(2+). Phylogenetic analysis revealed that the glucokinase from A. pernix does not belong to the clusters of enzymes found in bacteria and eukarya. This is the first description of the characteristics of an ATP-dependent glucokinase from an archaeon.  (+info)

Comparison of sequence masking algorithms and the detection of biased protein sequence regions. (2/73)

MOTIVATION: Separation of protein sequence regions according to their local information complexity and subsequent masking of low complexity regions has greatly enhanced the reliability of function prediction by sequence similarity. Comparisons with alternative methods that focus on compositional sequence bias rather than information complexity measures have shown that removal of compositional bias yields at least as sensitive and much more specific results. Besides the application of sequence masking algorithms to sequence similarity searches, the study of the masked regions themselves is of great interest. Traditionally, however, these have been neglected despite evidence of their functional relevance. RESULTS: Here we demonstrate that compositional bias seems to be a more effective measure for the detection of biologically meaningful signals. Typical results on proteins are compared to results for sequences that have been randomized in various ways, conserving composition and local correlations for individual proteins or the entire set. It is remarkable that low-complexity regions have the same form of distribution in proteins as in randomized sequences, and that the signal from randomized sequences with conserved local correlations and amino acid composition almost matches the signal from proteins. This is not the case for sequence bias, which hence seems to be a genuinely biological phenomenon in contrast to patches of low complexity.  (+info)

Bifunctional phosphoglucose/phosphomannose isomerases from the Archaea Aeropyrum pernix and Thermoplasma acidophilum constitute a novel enzyme family within the phosphoglucose isomerase superfamily. (3/73)

The hyperthermophilic crenarchaeon Aeropyrum pernix contains phosphoglucose isomerase (PGI) activity. However, obvious homologs with significant identity to known PGIs could not be identified in the sequenced genome of this organism. The PGI activity from A. pernix was purified and characterized. Kinetic analysis revealed that, unlike all known PGIs, the enzyme catalyzed reversible isomerization not only of glucose 6-phosphate but also of epimeric mannose 6-phosphate at similar catalytic efficiency, thus defining the protein as bifunctional phosphoglucose/phosphomannose isomerase (PGI/PMI). The gene pgi/pmi encoding PGI/PMI (open reading frame APE0768) was identified by matrix-assisted laser desorption ionization time-of-flight analyses; the gene was overexpressed in Escherichia coli as functional PGI/PMI. Putative PGI/PMI homologs were identified in several (hyper)thermophilic archaea and two bacteria. The homolog from Thermoplasma acidophilum (Ta1419) was overexpressed in E. coli, and the recombinant enzyme was characterized as bifunctional PGI/PMI. PGI/PMIs showed low sequence identity to the PGI superfamily and formed a distinct phylogenetic cluster. However, secondary structure predictions and the presence of several conserved amino acids potentially involved in catalysis indicate some structural and functional similarity to the PGI superfamily. Thus, we propose that bifunctional PGI/PMI constitutes a novel protein family within the PGI superfamily.  (+info)

Aeropyrum camini sp. nov., a strictly aerobic, hyperthermophilic archaeon from a deep-sea hydrothermal vent chimney. (4/73)

A novel hyperthermophilic archaeon, designated strain SY1(T), was isolated from a deep-sea hydrothermal vent chimney sample collected from the Suiyo Seamount in the Izu-Bonin Arc, Japan, at a depth of 1385 m. The cells were irregular cocci (1.2 to 2.1 micro m in diameter), occurring singly or in pairs, and stained Gram-negative. Growth was observed between 70 and 97 degrees C (optimum, 85 degrees C; 220 min doubling time), pH 6.5 and 8.8 (optimum, pH 8.0), and salinity of 2.2 and 5.3 % (optimum, 3.5 %). It was a strictly aerobic heterotroph capable of growing on complex proteinaceous substrates such as yeast extract and tryptone. The G+C content of the genomic DNA was 54.4 mol%. Phylogenetic analysis based on the 16S rDNA sequence of the isolate indicated that the isolate was closely related to Aeropyrum pernix strain K1(T). However, no significant genetic relatedness was observed between them by DNA-DNA hybridization. On the basis of the molecular and physiological traits of the new isolate, the name Aeropyrum camini sp. nov. is proposed, with the type strain SY1(T) (=JCM 12091(T)=ATCC BAA-758(T)).  (+info)

Crystal structure of an acylpeptide hydrolase/esterase from Aeropyrum pernix K1. (5/73)

Acylpeptide hydrolases (APH; also known as acylamino acid releasing enzyme) catalyze the removal of an N-acylated amino acid from blocked peptides. The crystal structure of an APH from the thermophilic archaeon Aeropyrum pernix K1 to 2.1 A resolution confirms it to be a member of the prolyl oligopeptidase family of serine proteases. The structure of apAPH is a symmetric homodimer with each subunit comprised of two domains. The N-terminal domain is a regular seven-bladed beta-propeller, while the C-terminal domain has a canonical alpha/beta hydrolase fold and includes the active site and a conserved Ser445-Asp524-His556 catalytic triad. The complex structure of apAPH with an organophosphorus substrate, p-nitrophenyl phosphate, has also been determined. The complex structure unambiguously maps out the substrate binding pocket and provides a basis for substrate recognition by apAPH. A conserved mechanism for protein degradation from archaea to mammals is suggested by the structural features of apAPH.  (+info)

Alteration of product specificity of Aeropyrum pernix farnesylgeranyl diphosphate synthase (Fgs) by directed evolution. (6/73)

Directed evolution of the C25 farnesylgeranyl diphosphate synthase of Aeropyrum pernix (Fgs) was carried out by error-prone PCR with an in vivo color complementation screen utilizing carotenoid biosynthetic pathway enzymes. Screening yielded 12 evolved clones with C20 geranylgeranyl diphosphate synthase activity which were isolated and characterized in order to understand better the chain elongation mechanism of this enzyme. Analysis of these mutants revealed three different mechanisms of product chain length specificity. Two mutants (A64T and A64V) have a single mutation at the 8th amino acid upstream of a conserved first aspartate-rich motif (FARM), which is involved in the mechanism for chain elongation reaction of all prenyl diphosphate synthases. One mutant (A135T) carries a single mutation at the 7th amino acid upstream of another conserved region (141GQ142), which was recently found to be another important region controlling chain elongation of a type III C20 geranylgeranyl diphosphate synthase and Escherichia coli C15 farnesyl diphosphate synthase. Finally, one mutant carrying four mutations (V84I, H88R, I177 M and M191V) is of interest. Molecular modeling, site-directed mutagenesis and in vitro assays of this mutant suggest that product chain-length distribution can be also controlled by a structural change provoked by a cooperative interaction of amino acids.  (+info)

Structure of an XPF endonuclease with and without DNA suggests a model for substrate recognition. (7/73)

The XPF/Mus81 structure-specific endonucleases cleave double-stranded DNA (dsDNA) within asymmetric branched DNA substrates and play an essential role in nucleotide excision repair, recombination and genome integrity. We report the structure of an archaeal XPF homodimer alone and bound to dsDNA. Superposition of these structures reveals a large domain movement upon binding DNA, indicating how the (HhH)(2) domain and the nuclease domain are coupled to allow the recognition of double-stranded/single-stranded DNA junctions. We identify two nonequivalent DNA-binding sites and propose a model in which XPF distorts the 3' flap substrate in order to engage both binding sites and promote strand cleavage. The model rationalises published biochemical data and implies a novel role for the ERCC1 subunit of eukaryotic XPF complexes.  (+info)

Log P effect of organic solvents on a thermophilic alcohol dehydrogenase. (8/73)

An alcohol dehydrogenase from the hyperthermophilic archaeon Aeropyrum pernix was activated by water-miscible organic solvents. This activation was influenced by the kind and the concentration of the added organic solvents. The k(cat) was increased by a factor of over ten when the mole fraction of acetonitrile was 0.1. This effect was large when organic solvents with large log P values were added. In fact, the k(cat) showed a strong positive correlation with the log P value of the mixed solvent at a constant mole fraction of water, while it was not affected by the kind of organic solvents added. Both the activation enthalpy and the entropy decreased with an increase in log P. The contribution of the activation enthalpy to the free energy of activation was larger than that of the activation entropy, and the free energy of activation decreased with an increase in log P.  (+info)

Thank you for your interest in spreading the word on Molecular & Cellular Proteomics.. NOTE: We only request your email address so that the person you are recommending the page to knows that you wanted them to see it, and that it is not junk mail. We do not capture any email address.. ...
Enzymatic Degradation of PrPSc by a Protease Secreted from Aeropyrum pernix K1. . Biblioteca virtual para leer y descargar libros, documentos, trabajos y tesis universitarias en PDF. Material universiario, documentación y tareas realizadas por universitarios en nuestra biblioteca. Para descargar gratis y para leer online.
Sako, Y., Nomura, N., Uchida, A., Ishida, Y., Morii, H., Koga, Y., Hoaki, T., and Maruyama, T. 1996. Aeropyrum pernix gen. nov., sp. nov., a novel aerobic hyperthermophilic archaeon growing at temperatures up to 100 degrees C. Int. J. Syst. Bacteriol. 46:1070-1077 ...
ID AEPER1_1_PE483 STANDARD; PRT; 370 AA. AC AEPER1_1_PE483; Q9YE84; DT 00-JAN-0000 (Rel. 1, Created) DT 00-JAN-0000 (Rel. 2, Last sequence update) DT 00-JAN-0000 (Rel. 3, Last annotation update) DE RecName: Full=Putative methylthioribose-1-phosphate isomerase; DE Short=M1Pi; Short=MTR-1-P isomerase; EC=5.3.1 23;AltName: Full=MTNA-like DE protein; Short=aMTNA;AltName: Full=S-methyl-5-thioribose-1-phosphate DE isomerase; (AEPER1_1.PE483). GN OrderedLocusNames=APE_0686; OS AEROPYRUM PERNIX K1. OC Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales; OC Desulfurococcaceae; Aeropyrum. OX NCBI_TaxID=272557; RN [0] RP -.; RG -.; RL -.; CC -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS AEPER1_1.PE483. CC Aeropyrum pernix K1, complete genome. CC annotated by Ensembl Genomes CC -!- ANNOTATIONS ORIGIN:MTNA_AERPE CC -!- FUNCTION: Catalyzes the interconversion of methylthioribose-1- CC phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P) CC (By similarity). CC -!- CATALYTIC ACTIVITY: ...
Proteome IDi ,p>The proteome identifier (UPID) is the unique identifier assigned to the set of proteins that constitute the ,a href=http://www.uniprot.org/manual/proteomes_manual>proteome,/a>. It consists of the characters UP followed by 9 digits, is stable across releases and can therefore be used to cite a UniProt proteome.,p>,a href=/help/proteome_id target=_top>More...,/a>,/p> ...
Multifunctional RNA-binding protein that recognizes the K-turn motif in ribosomal RNA, the RNA component of RNase P, box H/ACA, box C/D and box C/D sRNAs.
In publishing the research results obtained by use of the BIOLOGICAL RESOURCE, the USER is expected to cite the literature specified by the DEPOSITOR ...
Affiliation:国立研究開発法人産業技術総合研究所,その他部局等,研究員, Research Field:Applied molecular and cellular biology,Applied materials science/Crystal engineering,Digestive surgery,Functional biochemistry,Laboratory medicine, Keywords:糖鎖,NMR,糖認識ドメイン,レクチン,蛋白質,Aeropyrum pernix K1,進化,Aminoacyl-tRNA synthetase,肝線維化,バイオマーカー, # of Research Projects:7, # of Research Products:27, Ongoing Project:動脈硬化性大動脈瘤の網羅的糖鎖解析による新たな疾患関連指標の探索
Biological membranes, defining the boundary of cells and eukaryotic organelles, are mainly composed of lipids and membrane proteins. Interactions between these lipids and proteins are needed to preserve the tight seal of the membrane, but also to induce structure for proper function in many membrane proteins. In this thesis, interactions between three different kinds of peptides, i.e. small proteins, and model membranes are studied by spectroscopic methods.. First, the membrane interaction of two paddle domains, KvAPp, from the voltage-gated potassium channel KvAP from Aeropyrum pernix, and HsapBKp, from the human, large conductance, calcium-activated potassium channel HsapBK, was studied (paper I and II). In paper I, a high-resolution solution NMR structure of HsapBKp in detergent micelles is presented revealing a helix-turn-helix motif. Small structural differences between HsapBKp and KvAPp, positioning the arginines differently, are presented. These structural differences may explain why BK ...
Opko Health (NASDAQ: OPK) and Pernix Therapeutics (NASDAQ:PTX) are both healthcare companies, but which is the better stock? We will compare the two businesses based on the strength of their valuation, profitability, dividends, analyst recommendations, risk, earnings and institutional ownership. Institutional & Insider Ownership 22.9% of Opko Health shares are owned by institutional investors. Comparatively, […]
Both biopharmaceutical companies Relypsa Inc (NASDAQ:RLYP) and Pernix Therapeutics Holdings Inc (NASDAQ:PTX) run into obstacles amidst preparing for the la
The virions of members of the Guttaviridae have an ovoid shape, measuring 55 x 75 nm (for Aeropyrum pernix ovoid virus 1 (APOV1), Betaguttavirus) to 80 x 130 nm (for Sulfolobus newzealandicus droplet-shaped virus (SNDV), Alphaguttavirus), when analysed by cryo-electron microscopy [{Arnold et al., 2000:10873785RJOHTXArnold et al., 2000, SNDV, a novel virus of the extremely thermophilic and acidophilic archaeon Sulfolobus, Virology, 272, 2, 409-16RJOMREFMochizuki et al., 2011:21784945RJOHTXMochizuki et al., 2011, Provirus induction in hyperthermophilic archaea: characterization of Aeropyrum pernix spindle-shaped virus 1 and Aeropyrum pernix ovoid virus 1, J Bacteriol, 193, 19, 5412-9}]. The virion surface is covered by globular subunits, which are ~3.5 nm in width. In negative-contrast electron micrographs, the virions are slightly pleomorphic, most displaying a droplet-like shape. Virions of SNDV are decorated with dense filaments attached to the pointed end of the virion; such appendages were ...
Archaeal viruses have evolved to infect hosts often thriving in extreme conditions such as high temperatures. However, there is a paucity of information on archaeal virion structures, genome packaging, and determinants of temperature resistance. The rod-shaped virus APBV1 (Aeropyrum pernix bacilliform virus 1) is among the most thermostable viruses known; it infects a hyperthermophile Aeropyrum pernix, which grows optimally at 90 °C. Here we report the structure of APBV1, determined by cryo-electron microscopy at near-atomic resolution. Tight packing of the major virion glycoprotein (VP1) is ensured by extended hydrophobic interfaces, and likely contributes to the extreme thermostability of the helical capsid. The double-stranded DNA is tightly packed in the capsid as a left-handed superhelix and held in place by the interactions with positively charged residues of VP1. The assembly is closed by specific capping structures at either end, which we propose to play a role in DNA packing and delivery.
Archaeal viruses have evolved to infect hosts often thriving in extreme conditions such as high temperatures. However, there is a paucity of information on archaeal virion structures, genome packaging, and determinants of temperature resistance. The rod-shaped virus APBV1 (Aeropyrum pernix bacilliform virus 1) is among the most thermostable viruses known; it infects a hyperthermophile Aeropyrum pernix, which grows optimally at 90 °C. Here we report the structure of APBV1, determined by cryo-electron microscopy at near-atomic resolution. Tight packing of the major virion glycoprotein (VP1) is ensured by extended hydrophobic interfaces, and likely contributes to the extreme thermostability of the helical capsid. The double-stranded DNA is tightly packed in the capsid as a left-handed superhelix and held in place by the interactions with positively charged residues of VP1. The assembly is closed by specific capping structures at either end, which we propose to play a role in DNA packing and delivery.
fig 3 conservation of glutamate switch in AAA+ proteins. (a) Sequence alignments of selected members of each clade for which the crystal structures are known. The color scheme follows that used in Figure 4. RFCs, replication factor C small subunit from Archaeoglobus fulgidus; Orc1, Orc1 protein from Aeropyrum pernix; p97D1, p97 D1 AAA+ domain from Mus musculus; SV40, SV40 large T antigen; PspF, PspF from Escherichia coli; HslU, HslU from E. coli; RuvBL1, RuvB-like 1 (TIP49a, Pontin) from Homo sapiens. (b) Plot of side chain torsion angles for 50 active site glutamate (DExx box) residues from AAA+ protein structures in the Protein Data Bank (http://www.rcsb.org/) with a resolution better than 3.5 Å. Only one copy from the asymmetric unit was used if angles were similar, to reduce redundancy. The appropriate glutamate residue was selected from individual PDB files and the side chain torsion angles were calculated using the CCP4 program ANGLES40, then normalized to 0-360° for display. The values ...
MORRISTOWN, N.J., May 09, 2016-- Pernix Therapeutics Holdings, Inc., a specialty pharmaceutical company, today announced that on May 6, 2016, the Patent Trial and Appeal Board of the United States Patent and Trademark Office denied a petition for inter partes review filed by Graybar Pharmaceuticals, LLC against Pozen, Inc. This petition, which was filed on November...
Pernix Therapeutics Holdings Inc (NASDAQ:PTX) announced the distribution of TREXIMET® (sumatriptan and naproxen sodium) 10/60 mg to wholesalers has
... BOCA RATON Fla. Aug. 9 2013 /PRNewswire/ ...About Breckenridge: Breckenridge Pharmaceutical Inc. is a private... ... ...,Breckenridge,Enters,Into,Agreement,to,Acquire,Certain,Cypress,Assets,from,Pernix,Therapeutics,medicine,advanced medical technology,medical laboratory technology,medical device technology,latest medical technology,Health
The KvAP crystal MW binary option indicator every association and collection Spain , vaio z boot options, joe ross trading spreads and seasonals, binary option trading system striker9 review 360 pearson
Staphylothermus marinus is a marine organism that was isolated from hydrothermal sediment off the the coast of Vulcano Island in Italy. It can also be found from black smokers on the ocean floor. In a rich medium, Staphylothermus marinus grows in an optimum temperature of 92 degrees Celsius, but when nutrients are sparce, the optimum temperature drops to 85 degrees Celsius. For growth in a lab, a complex nutrient source is needed for optimum growth. The morphology of the Staphylothermus marinus can differ depending on the nutrients available. When nutrients are plentiful, Staphylothermus marinus grow as giant cells in a slightly irregular coccus shape with diameters up to 15 mm. Low nutrient concentrations produce little cells with diameters ranging from 0.5 to 1.0 mm. Up to 100 of these cells can cluster together to form grape-like groups. S. marinus is related to Aeropyrum pernix, Hyperthermus butylicus, and Ignicoccus hospitalis. (5) Describe the appearance, habitat, etc. of the organism, ...
BrunchClust produces 7 clusters: two complete for ATP-A and ATP-B and one incomplete for ATP-F. ATP-A and ATP-B clusters contain paralogs that are also reported as a result of clustering. There are two paralogs on the ATP-A branch one is of Rhodopirellula baltica and the second is of Methanosarcina acetivorans, and there are three paralogs on the ATP-B branch: two are from the same species as those on the ATP-A branch, i.e. Rhodopirellula baltica and Methanosarcina acetivoran, and the third is from Chlorobium tepidum. List of 30 taxa: 16 Bacteria: Aquifex aeolicus, Bacillus subtilis, Chlorobium tepidum, Corynebacterium glutamicum, Deinococcus radiodurans, Geobacillus kaustophilus, Geobacter sulfurreducens, Gloeobacter violaceus, Nostoc sp., Pseudomonas aeruginosa, Rhodopirellula baltica, Rhodopseudomonas palustris, Streptococcus thermophilus, Streptomyces coelicolor, Thermotoga maritime, Thermus thermophilus, and 14 Archaea: Aeropyrum pernix,Archaeoglobus fulgidus,Haloarcula marismortui, ...
Equities.com is an advanced financial information center and next-generation communication platform that connects self-directed investors with startup and small cap companies, market experts, and professional service providers and vendors.
1BTZ: Episelection: novel Ki approximately nanomolar inhibitors of serine proteases selected by binding or chemistry on an enzyme surface.
Acylpeptide hydrolase catalyzes the removal of the terminal blocking group together with the first amino acid residue of a peptide substrate: Acyl - AA1 - AA2 - AA3… AAn → Acyl - AA1 + AA2 - AA3… AAn...
Vice President PRA Healthsciences Salt Lake City, UT Disclosures: Consultant/Independent Contractor: Alcobra, Bonti, Charleston Labs, Daiichi Sankyo, Depomed, Egalet, Indivior, Insys, Kempharm, Mallinckrodt, Merck, Pain Therapeutics, Pernix, Pfizer, Shionogi, Teva, Trevena, Trevi, Vallon Pharmaceuticals Advisory Board: BDSI, Charleston Labs, Depomed, Egalet, Ensysce Biosciences, Inspirion Therapeutics, Insys Therapeutics, Mallinkcrodt Pharmaceuticals, Pfizer, Teva, Trevena
L-Proline, L-seryl-L-lysyl-L-prolyl-L-threonyl-L-threonyl-L-lysyl-L-glutaminyl-L-arginyl-L- glutaminyl-L-asparaginyl-L-lysyl-L-prolyl-L-prolyl-L-asparaginyl-L-lysyl ...
Before you buy Alba Botanica Good & Clean™ Dual Textured Exfoliating Towelettes, check out 40 Influenster reviews. Mattie O. said Seriously anything ALBA...
Aeropyrum pernix archaea serve as natural hosts. There is currently only one species in this genus: the type species Aeropyrum ... Aeropyrum pernix archaea serve as the natural host. Transmission routes are passive diffusion. Prangishvili, D; Mochizuki, T; ... pernix ovoid virus 1. Group: dsDNA Order: Unassigned Family: Guttaviridae Genus: Betaguttavirus Aeropyrum pernix ovoid virus 1 ...
Kato-Murayama M, Bessho Y, Shirouzu M, Yokoyama S (2005). "Crystal structure of the RNA 2'-phosphotransferase from Aeropyrum ...
Mino K, Ishikawa K (2003). "Characterization of a novel thermostable O-acetylserine sulfhydrylase from Aeropyrum pernix K1". J ... "A novel O-phospho-L-serine sulfhydrylation reaction catalyzed by O-acetylserine sulfhydrylase from Aeropyrum pernix K1". FEBS ... "Crystallization and preliminary X-ray diffraction analysis of O-acetylserine sulfhydrylase from Aeropyrum pernix K1". Acta ...
April 1999). "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon, Aeropyrum pernix K1". DNA Research. 6 (2 ...
Aeropyrum pernix K1". DNA Res. 6 (2): 83-101, 145-52. doi:10.1093/dnares/6.2.83. PMID 10382966. Polisson C, Robinson D (June ...
"Biochemical analysis of a DNA replication origin in the archaeon Aeropyrum pernix". Journal of Molecular Biology. 363 (2): 355- ... "Conformational changes induced by nucleotide binding in Cdc6/ORC from Aeropyrum pernix". Journal of Molecular Biology. 343 (3 ...
Lee PC, Mijts BN, Petri R, Watts KT, Schmidt-Dannert C (November 2004). "Alteration of product specificity of Aeropyrum pernix ... Aeropyrum pernix. Molecularevolution with alteration in product specificity". European Journal of Biochemistry. 267 (2): 321-8 ...
... is a family of viruses that replicate in hyperthermophilic archaea of the genus Aeropyrum, specifically Aeropyrum ... The virions of Aeropyrum coil-shaped virus (ACV) are non-enveloped and in the shape of hollow cylinders that are formed by a ... ACV could not be replicaed in other strains of A. pernix or in Aeropyrum camini, so the original A. pernix culture was used for ... ACV was first isolated from a sample of Aeropyrum pernix (A. pernix) taken from the coastal Yamagawa Hot Spring, where the ...
Comparison to other sequenced genomes suggests that A. saccharovorans is most closely related to Aeropyrum pernix. The genome ... which also contains Aeropyrum pernix. Acidilobales species are widely distributed in hot springs with acidic environments, ...
"Diversity of viruses of the hyperthermophilic archaeal genus Aeropyrum, and isolation of the Aeropyrum pernix bacilliform virus ... There is one genus in this family (Clavavirus). Within this genus, a single species has been described to date: Aeropyrum ...
In 2004, two primitive versions of hemoglobin were discovered in M. acetivorans and another archaeon, Aeropyrum pernix. Known ...
... but in Aeropyrum pernix and some other archaea O-phosphoserine is used. CysK and CysM are homologues, but belong to the PLP ... "A novel O-phospho-L-serine sulfhydrylation reaction catalyzed by O-acetylserine sulfhydrylase from Aeropyrum pernix K1". FEBS ...
The crystal structures of the YARSs from Archeoglobus fulgidus, Pyrococcus horikoshii and Aeropyrum pernix have also been ...
Archaeoglobus fulgidus Methanococcus jannaschii Aeropyrum pernix Sulfolobus Methanopyrus kandleri strain 116, an archaeon in 80 ...
The structure of DERAs across many organisms: DERAs from Escherichia coli and Aeropyrum pernix shares 37.7% sequence identity ...
Characterization of Aeropyrum pernix spindle-shaped virus 1 and Aeropyrum pernix ovoid virus 1. J Bacteriol 193(19):5412-5419 ... Betaguttavirus Aeropyrum pernix ovoid virus 1 Viruses in the family Guttaviridae are enveloped. The diameter is around 70-95 nm ...
Characterization of Aeropyrum pernix spindle-shaped virus 1 and Aeropyrum pernix ovoid virus 1". J Bacteriol 193:5412-5419. 6. ... "Diversity of viruses of the hyperthermophilic archaeal genus Aeropyrum, and isolation of the Aeropyrum pernix bacilliform virus ...
MeSH B07.075.200.500 - desulfurococcaceae MeSH B07.075.200.500.050 - aeropyrum MeSH B07.075.200.650 - pyrodictiaceae MeSH ...
... and the other one by the Aeropyrum coil-shaped virus (Spiraviridae) infecting a hyperthermophilic (optimal growth at 90-95 °C) ...
Genus Acidilobus Genus Acidococcus Genus Aeropyrum Genus Desulfurococcus Genus Ignicoccus Genus Staphylothermus Genus Stetteria ...
... phiO18P Aeromonas virus pIS4A Aeromonas virus ZPAH7 Aeropyrum coil-shaped virus Aeropyrum pernix bacilliform virus 1 Aeropyrum ...
PubMed references for Aeropyrum PubMed Central references for Aeropyrum Google Scholar references for Aeropyrum NCBI taxonomy ... Life taxonomy pages for Aeropyrum Search Species2000 page for Aeropyrum MicrobeWiki page for Aeropyrum LPSN page for Aeropyrum ... In taxonomy, Aeropyrum is a genus of the Desulfurococcaceae. The name Aeropyrum derives from: Greek noun aer, aeros (ἀήρ, ἀέρος ... Sako Y; Nomura N; Uchida A; Ishida Y; Morii H; Koga Y; Hoaki T; Maruyama T (1996). "Aeropyrum pernix gen. nov., sp. nov., a ...
Type strain of Aeropyrum pernix at BacDive - the Bacterial Diversity Metadatabase KEGG Genome : Aeropyrum pernix. ... The cells of Aeropyrum pernix are spherical in shape and approximately 1 μm in diameter. The envelope surrounding the cells of ... Aeropyrum pernix is a species of extremophile archaean in the archaean phylum Crenarchaeota. It is an obligatorily thermophilic ... Aeropyrum pernix was the first strictly aerobic hyperthermophilic Archaea to be discovered. It was originally isolated from ...
... dan yang lainnya oleh Aeropyrum coil berbentuk virus ("Spiraviridae") menginfeksi inang hipertermofilik (pertumbuhan optimal ...
... and the other one by the Aeropyrum coil-shaped virus ("Spiraviridae") infecting a hyperthermophilic (optimal growth at 90-95 °C ...
PubMed references for Aeropyrum PubMed Central references for Aeropyrum Google Scholar references for Aeropyrum NCBI taxonomy ... Life taxonomy pages for Aeropyrum Search Species2000 page for Aeropyrum MicrobeWiki page for Aeropyrum LPSN page for Aeropyrum ... In taxonomy, Aeropyrum is a genus of the Desulfurococcaceae. The name Aeropyrum derives from: Greek noun aer, aeros (ἀήρ, ἀέρος ... Sako Y; Nomura N; Uchida A; Ishida Y; Morii H; Koga Y; Hoaki T; Maruyama T (1996). "Aeropyrum pernix gen. nov., sp. nov., a ...
Type strain of Aeropyrum pernix at BacDive - the Bacterial Diversity Metadatabase KEGG Genome : Aeropyrum pernix. ... The cells of Aeropyrum pernix are spherical in shape and approximately 1 μm in diameter. The envelope surrounding the cells of ... Aeropyrum pernix is a species of extremophile archaean in the archaean phylum Crenarchaeota. It is an obligatorily thermophilic ... Aeropyrum pernix was the first strictly aerobic hyperthermophilic Archaea to be discovered. It was originally isolated from ...
"Provirus Induction in Hyperthermophilic Archaea: Characterization of Aeropyrum pernix Spindle-Shaped Virus 1 and Aeropyrum ...
Aeropyrum species Aeropyrum pernix Name. Homonyms. Aeropyrum pernix Sako et al., 1996. Bibliographic References. * (2012) ... Aeropyrum pernix Sako et al., 1996 Dataset GBIF Backbone Taxonomy Rank SPECIES Published in Int. J. Syst. Bacteriol. 46::1076 ... Aeropyrum pernix gen. nov., sp. nov., a novel aerobic hyperthermophilic archaeon growing at temperatures up to 100 degrees C. ...
Retrieved from "https://species.wikimedia.org/w/index.php?title=Aeropyrum_pernix_ovoid_virus_1&oldid=6010329" ...
Aeropyrum pernix. Mutation(s): 0 Find proteins for Q9YEV6 (Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC ... STRUCTURE OF THE AEROPYRUM PERNIX ORC1 PROTEIN IN COMPLEX WITH DNA. *DOI: 10.2210/pdb2V1U/pdb ...
... Jin-Suk Han1 and Kazuhiko ... Jin-Suk Han and Kazuhiko Ishikawa, "Active site of Zn2+-dependent sn-glycerol-1-phosphate dehydrogenase from Aeropyrum pernix ...
This proteome is part of the Aeropyrum pernix pan proteome (fasta) A strictly aerobic hyperthermophilic archaeon isolated from ... Proteomes - Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1). Basket 0 ... "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon, Aeropyrum pernix K1.". Kawarabayasi Y., Hino Y., ... 272557 - Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1). ...
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1). Mutation(s): 0 Gene Names: trpS. EC: 6.1.1.2. ... Find proteins for Q9Y924 (Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)) ... Organism(s): Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1) ... Crystal structure of tryptophanyl-tRNA synthetase from hyperthermophilic archaeon, Aeropyrum pernix K1. *DOI: 10.2210/pdb3A04/ ...
Outside the unusual cell wall of hyperthermophilic archaeon Aeropyrum pernix. Gianna Palmieri, Raffaele Cannio, Immacolata ... Outside the unusual cell wall of hyperthermophilic archaeon Aeropyrum pernix. Gianna Palmieri, Raffaele Cannio, Immacolata ... Outside the unusual cell wall of hyperthermophilic archaeon Aeropyrum pernix Message Subject (Your Name) has sent you a message ... Outside the unusual cell wall of hyperthermophilic archaeon Aeropyrum pernix. Gianna Palmieri, Raffaele Cannio, Immacolata ...
Aeropyrum pernix to bind DNA. (doi: 10.5562/cca1772). Ključne riječi. Aeropyrum pernix; hyperthermophile; archaea; Alba; DNA ... "Heterologous Expression of the Alba Protein from the Hyperthermophilic Archaeon Aeropyrum Pernix." Croatica Chemica Acta, vol. ... "Heterologous Expression of the Alba Protein from the Hyperthermophilic Archaeon Aeropyrum Pernix." Croatica Chemica Acta 84, br ... histone counterparts, the Alba proteins, were identified in the Aeropyrum pernix genome (APE1832.1. and APE1823). By using a ...
Insights into the maturation of pernisine, a subtilisin-like protease from the hyperthermophilic archaeon Aeropyrum pernix. ... Pernisine is a subtilisin-like protease that was originally identified in the hyperthermophilic archaeon Aeropyrum pernix, ... Pernisine from the hyperthermophilic archaeon Aeropyrum pernix is a proteolytic enzyme that can degrade infective prion ... Insights into the maturation of pernisine, a subtilisin-like protease from the hyperthermophilic archaeon Aeropyrum pernix ...
In publishing the research results obtained by use of the BIOLOGICAL RESOURCE, the USER is expected to cite the literature specified by the DEPOSITOR ...
We show that the two VKORs of Aeropyrum pernix assume opposite orientations in the cytoplasmic membrane, when expressed in E. ... Aeropyrum pernix membrane topology of protein VKOR promotes protein disulfide bond formation in two subcellular compartments ... Aeropyrum pernix membrane topology of protein VKOR promotes protein disulfide bond formation in two subcellular compartments, ... We show that the two VKORs of Aeropyrum pernix assume opposite orientations in the cytoplasmic membrane, when expressed in E. ...
lipidi, arheje, Aeropyrum pernix, arheosomi, citoksičnost, Aeropyrum pernix, archaeosomes, cytoxicity, endocytosis. Work type: ... Cytotoxicity and uptake of archaeosomes prepared from Aeropyrum pernix lipids. Batista Napotnik, Tina (Author), Valant, Janez ( ...
... from Aeropyrum pernix K1. Plus protein sequence and external database links. ... Domain assignment for gi,118431509,ref,YP_874902.1, from Aeropyrum pernix K1. Domain architecture ...
Enzymatic Degradation of PrPSc by a Protease Secreted from Aeropyrum pernix K1. . Biblioteca virtual para leer y descargar ... An R30 fraction from the growth medium of Aeropyrum pernix was analyzed for the protease that can digest the pathological prion ... Enzymatic Degradation of PrPSc by a Protease Secreted from Aeropyrum pernix K1 - Descarga este documento en PDF. Documentación ... Enzymatic Degradation of PrPSc by a Protease Secreted from Aeropyrum pernix K1. ...
The species abbreviations are: Af, Archaeoglobus fulgidus; Ape, Aeropyrum pernix; Hsp, Halobacterium sp.; Mace, Methanosarcina ...
Aeropyrum pernix. APE1495 APE1659 APE1961 7516538. 7447932. 7431108 Agrobacterium tumefaciens mocA AAB07785 ...
The ligands PEP and E4P were obtained from the DAHPS structures of Aeropyrum pernix (PDB: 1VS1) and Thermotoga maritima (PDB: ... d-arabino-heptulosonate 7-phosphate synthase from Aeropyrum pernix. Bioorg Chem 40:79-86. https://doi.org/10.1016/j.bioorg. ...
AEROPYRUM PERNIX K1. OC Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales; OC Desulfurococcaceae; Aeropyrum. OX NCBI_ ... CC Aeropyrum pernix K1, complete genome. CC annotated by Ensembl Genomes CC -!- ANNOTATIONS ORIGIN:MTNA_AERPE CC -!- FUNCTION: ...
Aeropyrum pernix (Aper), Sulfolobus solfataricus (Sulso); bacteria: Thermotoga maritima (Thema), Deinococcus radiodurans (Deira ...
Aeropyrum pernix, grown aerobically. The redox spectrum of the isolated c-type cytochrome showed a characteristic α-band peak ... Sako Y, Nomura N, Uchida A, Ishida Y, Morii H, Koga Y, Hoakai T, Maruyama T: Aeropyrum pernix gen. nov., sp. nov., a novel ... Aeropyrum pernix is a hyperthermophilic crenarchaeon isolated from the seas of Japan, and its complete genome sequence has been ... Schematic representation of the respiratory chain of Aeropyrum pernix K1. Genes encoding cytochrome c oxidase and other ...
The thermostable serine protease pernisine originates from the hyperthermophilic Archaeaon Aeropyrum pernix and has valuable ... Extracellular production of the engineered thermostable protease pernisine from Aeropyrum pernix K1 in Streptomyces rimosus. * ... Pernisine is an alkaline protease from Aeropyrum pernix that belongs to the class of proteases designated as the subtilases, or ... Enzymatic degradation of PrPSc by a protease secreted from Aeropyrum pernix K1. PLoS ONE. 2012;7:e39548. ...
... and Aeropyrum pernix (72), but one or two FKBPs. Hyperthermophilic bacteria, Thermotoga maritima and Aquifex aeolicus which are ... Aeropyrum pernix K1. DNA Res 6, 83-101, 145-152 (1999) 73. Szabo, A., T. Langer, H. Schroder, J. Flanagan, B. Bukau & F. U. ... and Aeropyrum pernix (72). We isolated genes encoding a short-type FKBP from Methanococcus thermolithotrophicus (77) and ...
Abbreviations: AF, Archaeoglobus fulgidus; APE, Aeropyrum pernix; Bsu, B. subtilis; DVU, Desulfovibrio vulgaris; lmo, L. ...
Aeropyrum pernix; ARCFU, Archaeoglobus fulgidus; METJA, Methanococcus jannaschii; METTH, Methanobacterium thermoautotrophicum; ...
Steen, Ida Helene; Madsen, Marit; Lien, Torleiv; Birkeland, Nils-Kåre. 2000. Isocitrate dehydrogenase from Aeropyrum pernix. ... Steen, Ida Helene; Madsen, Marit Steine; Lien, Torleiv; Birkeland, Nils-Kåre. 2000. Isocitrate dehydrogenase from Aeropyrum ... Aeropyrum pernix and Thermotoga maritima. Acta Crystallographica Section D: Biological Crystallography. 2162-2164. ... Thermodynamic and kinetic stability of a large multi-domain enzyme from the hyperthermophile Aeropyrum pernix. Extremophiles. ...
Aeropyrum pernix K1 (Q9Y9L0.1; 61% sequence identity); P.hor., Pyrococcus horikoshii OT3 (NP_143112.1; 57% sequence identity); ... and its orthologs from Aeropyrum pernix (ApPrx), Pyrococcus horikoshii (PhPrx) and Thermococcus kodakarensis (TkPrx), ... The structure was solved by molecular replacement using the homologous Aeropyrum pernix peroxiredoxin (ApPrx) structure as a ...
Crystallization and preliminary crystallographic studies of putative threonyl-tRNA synthetases from Aeropyrum pernix and ...
  • Aeropyrum pernix was the first strictly aerobic hyperthermophilic Archaea to be discovered. (wikipedia.org)
  • Jin-Suk Han and Kazuhiko Ishikawa, "Active site of Zn 2+ -dependent sn -glycerol-1-phosphate dehydrogenase from Aeropyrum pernix K1," Archaea , vol. 1, no. 5, pp. 311-317, 2005. (hindawi.com)
  • The Alba proteins are small (approximately 10 kDa), DNA-binding, basic proteins that appear to partly compensate for the lack of histones in the archaea Aeropyrum pernix and other hyperthermophiles. (srce.hr)
  • 1999). "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon, Aeropyrum pernix K1" (PDF). (wikipedia.org)
  • Two sequences of these potential histone counterparts, the Alba proteins, were identified in the Aeropyrum pernix genome (APE1832.1 and APE1823). (srce.hr)
  • CC Aeropyrum pernix K1, complete genome. (univ-lyon1.fr)
  • There are two potential histone counterpart peptide sequences (Alba1 and Alba2) in the Aeropyrum pernix genome (APE1832.1 and APE1823). (nih.gov)
  • From the Aeropyrum pernix K1 genome through Vibrio cholerae El Tor N16961, all genomes or subsets of each may be queried. (wisc.edu)
  • Aeropyrum pernix is a species of extremophile archaean in the archaean phylum Crenarchaeota. (wikipedia.org)
  • An R30 fraction from the growth medium of Aeropyrum pernix was analyzed for the protease that can digest the pathological prion protein isoform PrPSc from different species human, bovine, deer and mouse. (duhnnae.com)
  • In taxonomy, Aeropyrum is a genus of the Desulfurococcaceae. (wikipedia.org)
  • Novel prenyltransferase gene encoding farnesylgeranyl diphosphate synthase from a hyperthermophilic archaeon, Aeropyrum pernix. (genome.jp)
  • The electrophoretic mobility shift assay demonstrated the ability of the Alba1 and Alba2 proteins from Aeropyrum pernix to bind DNA. (srce.hr)
  • Pernisine from the hyperthermophilic archaeon Aeropyrum pernix is a proteolytic enzyme that can degrade infective prion proteins and thus has a potential use for disinfection of prion-contaminated surfaces. (asm.org)
  • It appears that the Aeropyrum homologues both contain the equivalent of this residue, and are thus both Alba1-type proteins. (nih.gov)
  • DIP is widespread among extreme archaeal hyperthermophiles, such as Methanotorris igneus , Aeropyrum pernix , Stetteria hydrogenophila , Pyrodictium occultum , Pyrolobus fumarii , Archaeoglobus spp. (asm.org)
  • Bacterial taxonomy Microbiology See the NCBI webpage on Aeropyrum. (wikipedia.org)
  • it infects a hyperthermophile Aeropyrum pernix, which grows optimally at 90 °C. Here we report the structure of APBV1, determined by cryo-electron microscopy at near-atomic resolution. (archives-ouvertes.fr)
  • Pernisine is a subtilisin-like protease that was originally identified in the hyperthermophilic archaeon Aeropyrum pernix , which lives in extreme marine environments. (asm.org)
  • The thermostable serine protease pernisine originates from the hyperthermophilic Archaeaon Aeropyrum pernix and has valuable industrial applications. (biomedcentral.com)
  • Pernisine is an alkaline protease from Aeropyrum pernix that belongs to the class of proteases designated as the subtilases, or more specifically, peptidase S8. (biomedcentral.com)
  • New Latin neuter gender noun Aeropyrum, air fire, referring to the hyperthermophilic respirative character of the organism. (wikipedia.org)
  • Bacterial expression plasmid clone of Aeropyrum pernix APE0993. (riken.jp)
  • One, Aeropyrum pernix, is limited to oxygen-based respiration, survives optimally in near-boiling saltwater, and was first discovered among thermal sea vents off Japan. (innovations-report.com)
  • The structure was solved by molecular replacement using the homologous Aeropyrum pernix peroxiredoxin (ApPrx) structure as a search model. (iucr.org)
  • A gene encoding a D-2-deoxyribose-5-phosphate aldolase (DERA) homologue was identified in the hyperthermophilic archaeon Aeropyrum pernix. (nii.ac.jp)
  • Here, we isolated a c -type cytochrome-containing enzyme complex from the membranes of the hyperthermophilic archaeon, Aeropyrum pernix , grown aerobically. (beds.ac.uk)
  • The enzyme from Aeropyrum pernix prefers farnesyl diphosphate as allylic substrate. (genome.jp)
  • Variation of the Virus-Related Elements within Syntenic Genomes of the Hyperthermophilic Archaeon Aeropyrum" (PDF). (wikipedia.org)
  • 2011). 'Heterologous Expression of the Alba Protein from the Hyperthermophilic Archaeon Aeropyrum Pernix', Croatica Chemica Acta , 84(4), str. (srce.hr)
  • Črnigoj M, Hanzlowsky A, Vilfan T, Poklar Ulrih N. Heterologous Expression of the Alba Protein from the Hyperthermophilic Archaeon Aeropyrum Pernix. (srce.hr)
  • The envelope surrounding the cells of Aeropyrum is about 25 nm wide. (wikipedia.org)
  • Bacterial expression plasmid clone of Aeropyrum pernix APE1596. (riken.jp)