Aeropyrum: A genus of anaerobic, chemolithotropic coccoid ARCHAEA, in the family DESULFUROCOCCACEAE. They live in marine environments.Desulfurococcaceae: 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)Crenarchaeota: A kingdom in the domain ARCHAEA comprised of thermoacidophilic, sulfur-dependent organisms. The two orders are SULFOLOBALES and THERMOPROTEALES.Archaeal Proteins: Proteins found in any species of archaeon.RNA, Transfer, Thr: A transfer RNA which is specific for carrying threonine to sites on the ribosomes in preparation for protein synthesis.Thermoproteaceae: 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)DNA, Archaeal: Deoxyribonucleic acid that makes up the genetic material of archaea.Genome, Archaeal: The genetic complement of an archaeal organism (ARCHAEA) as represented in its DNA.Hydrothermal Vents: Hot springs on the ocean floor. They are commonly found near volcanically active places such as mid-oceanic ridges.Archaea: 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.Group II Chaperonins: 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.RNA, Archaeal: Ribonucleic acid in archaea having regulatory and catalytic roles as well as involvement in protein synthesis.Threonine-tRNA Ligase: An enzyme that activates threonine with its specific transfer RNA. EC 6.1.1.3.Enzyme Stability: 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.Archaeal Viruses: Viruses whose hosts are in the domain ARCHAEA.Proline Oxidase: 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.-.Proteome: The protein complement of an organism coded for by its genome.Apudoma: A general term collectively applied to tumors associated with the APUD CELLS series, irrespective of their specific identification.Electronic Mail: 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.Proteomics: The systematic study of the complete complement of proteins (PROTEOME) of organisms.Nonsense Mediated mRNA Decay: 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.Codon, Nonsense: 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.RNA Stability: 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.Periodicals as Topic: A publication issued at stated, more or less regular, intervals.Antitoxins: Antisera from immunized animals that is purified and used as a passive immunizing agent against specific BACTERIAL TOXINS.PubMed: 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.BooksSulfolobus solfataricus: A species of thermoacidophilic ARCHAEA in the family Sulfolobaceae, found in volcanic areas where the temperature is about 80 degrees C and SULFUR is present.Sulfolobus: A genus of aerobic, chemolithotrophic, coccoid ARCHAEA whose organisms are thermoacidophilic. Its cells are highly irregular in shape, often lobed, but occasionally spherical. It has worldwide distribution with organisms isolated from hot acidic soils and water. Sulfur is used as an energy source.Pentose Phosphate Pathway: An oxidative decarboxylation process that converts GLUCOSE-6-PHOSPHATE to D-ribose-5-phosphate via 6-phosphogluconate. The pentose product is used in the biosynthesis of NUCLEIC ACIDS. The generated energy is stored in the form of NADPH. This pathway is prominent in tissues which are active in the synthesis of FATTY ACIDS and STEROIDS.Ribosome Subunits, Small, Archaeal: The small subunit of archaeal RIBOSOMES. It is composed of the 16S RIBOSOMAL RNA and about 28 different RIBOSOMAL PROTEINS.Thermoplasma: A genus of facultatively anaerobic heterotrophic archaea, in the order THERMOPLASMALES, isolated from self-heating coal refuse piles and acid hot springs. They are thermophilic and can grow both with and without sulfur.Transketolase: An enzyme of the transferase class that catalyzes the conversion of sedoheptulose 7-phosphate and D-glyceraldehyde 3-phosphate to D-ribose 5-phosphate and D-xylulose 5-phosphate in the PENTOSE PHOSPHATE PATHWAY. (Dorland, 27th ed) EC 2.2.1.1.Authorship: The profession of writing. Also the identity of the writer as the creator of a literary production.Sinorhizobium: A genus of gram-negative, aerobic, nonsporeforming rods which usually contain granules of poly-beta-hydroxybutyrate. (From Bergey's Manual of Determinative Bacteriology, 9th ed)Terminology as Topic: The terms, expressions, designations, or symbols used in a particular science, discipline, or specialized subject area.Click Chemistry: Organic chemistry methodology that mimics the modular nature of various biosynthetic processes. It uses highly reliable and selective reactions designed to "click" i.e., rapidly join small modular units together in high yield, without offensive byproducts. In combination with COMBINATORIAL CHEMISTRY TECHNIQUES, it is used for the synthesis of new compounds and combinatorial libraries.Students: Individuals enrolled in a school or formal educational program.Species Specificity: The restriction of a characteristic behavior, anatomical structure or physical system, such as immune response; metabolic response, or gene or gene variant to the members of one species. It refers to that property which differentiates one species from another but it is also used for phylogenetic levels higher or lower than the species.Students, Medical: Individuals enrolled in a school of medicine or a formal educational program in medicine.Fatigue: The state of weariness following a period of exertion, mental or physical, characterized by a decreased capacity for work and reduced efficiency to respond to stimuli.Databases, Protein: Databases containing information about PROTEINS such as AMINO ACID SEQUENCE; PROTEIN CONFORMATION; and other properties.Sequence Analysis, Protein: A process that includes the determination of AMINO ACID SEQUENCE of a protein (or peptide, oligopeptide or peptide fragment) and the information analysis of the sequence.Systems Integration: The procedures involved in combining separately developed modules, components, or subsystems so that they work together as a complete system. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)Internet: A loose confederation of computer communication networks around the world. The networks that make up the Internet are connected through several backbone networks. The Internet grew out of the US Government ARPAnet project and was designed to facilitate information exchange.Proteins: Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein.Mevalonic AcidMeiosis: A type of CELL NUCLEUS division, occurring during maturation of the GERM CELLS. Two successive cell nucleus divisions following a single chromosome duplication (S PHASE) result in daughter cells with half the number of CHROMOSOMES as the parent cells.Crossing Over, Genetic: The reciprocal exchange of segments at corresponding positions along pairs of homologous CHROMOSOMES by symmetrical breakage and crosswise rejoining forming cross-over sites (HOLLIDAY JUNCTIONS) that are resolved during CHROMOSOME SEGREGATION. Crossing-over typically occurs during MEIOSIS but it may also occur in the absence of meiosis, for example, with bacterial chromosomes, organelle chromosomes, or somatic cell nuclear chromosomes.Recombination, Genetic: Production of new arrangements of DNA by various mechanisms such as assortment and segregation, CROSSING OVER; GENE CONVERSION; GENETIC TRANSFORMATION; GENETIC CONJUGATION; GENETIC TRANSDUCTION; or mixed infection of viruses.Chromosome Pairing: The alignment of CHROMOSOMES at homologous sequences.Metaphase: The phase of cell nucleus division following PROMETAPHASE, in which the CHROMOSOMES line up across the equatorial plane of the SPINDLE APPARATUS prior to separation.DNA Breaks, Double-Stranded: Interruptions in the sugar-phosphate backbone of DNA, across both strands adjacently.Synaptonemal Complex: The three-part structure of ribbon-like proteinaceous material that serves to align and join the paired homologous CHROMOSOMES. It is formed during the ZYGOTENE STAGE of the first meiotic division. It is a prerequisite for CROSSING OVER.

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)

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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 ...
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.
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 ...
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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 ...
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 ...
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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, ...
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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...
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 ...
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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. "Viral Zone". ExPASy. Retrieved ... 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 ...
Aeropyrum pernix K1". DNA Res. 6 (2): 83-101, 145-52. doi:10.1093/dnares/6.2.83. PMID 10382966. Ravin NV, Mardanov AV, Beletsky ...
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 ...
Lee, P.C.; Mijts, B.N.; Petri, R.; Watts, K.T.; Schmidt-Dannert, C. (2004). "Alteration of product specificity of Aeropyrum ... Aeropyrum pernix. Molecular evolution with alteration in product specificity". Eur. J. Biochem. 267: 321-328. doi:10.1046/j. ...
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 ... Aeropyrum pernix bacilliform virus 1. The name is derived from the Latin word clava meaning stick. The virons are bacilliform ...
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 ...
Characterization of Aeropyrum pernix spindle-shaped virus 1 and Aeropyrum pernix ovoid virus 1. J Bacteriol 193(19):5412-5419 ... Aeropyrum pernix ovoid virus 1 Viruses in Guttaviridae are enveloped. The diameter is around 70-95 nm, with a length of 110-185 ...
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 ...
Aeropyrum coil-shaped virus Family: Unassigned Genus: Bacilladnavirus Chaetoceros salsugineum DNA virus 01 Order: Unassigned ... Aeropyrum pernix ovoid virus 1 Family: Hytrosaviridae Genus: Glossinavirus Glossina hytrovirus Genus: Muscavirus Musca ... Aeropyrum pernix bacilliform virus 1 Family: Corticoviridae Genus: Corticovirus Pseudoalteromonas phage PM2 Family: ...
... infecting halophilic archaea and the other one by the Aeropyrum coil-shaped virus ("Spiraviridae") infecting a ...
Genus Acidilobus Genus Acidococcus Genus Aeropyrum Genus Desulfurococcus Genus Ignicoccus Genus Staphylothermus Genus Stetteria ...
Aes508 Aeromonas virus AS4 Aeromonas virus phiO18P 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 ... Aeropyrum Search Tree of Life taxonomy pages for Aeropyrum Search Species2000 page for Aeropyrum MicrobeWiki page for Aeropyrum ... In taxonomy, Aeropyrum is a genus of the Desulfurococcaceae. The name Aeropyrum derives from: Greek noun aer, aeros (ἀήρ, ἀέρος ... Aeropyrum entry in LPSN [Euzéby, J.P. (1997). "List of Bacterial Names with Standing in Nomenclature: a folder available on the ...
The cells of Aeropyrum pernix are spherical in shape and approximately 1 µm in diameter. The envelope surrounding the cells of ... Type strain of Aeropyrum pernix at BacDive - the Bacterial Diversity Metadatabase Napotnik, T.B.; Valant, J.; Gmajner, D.; ... 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 ...
... and the other one by the Aeropyrum coil-shaped virus ("Spiraviridae") infecting a hyperthermophilic (optimal growth at 90-95 °C ...
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. ...
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 ...
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. ...
PubMed references for Aeropyrum PubMed Central references for Aeropyrum Google Scholar references for Aeropyrum NCBI taxonomy ... Aeropyrum Search Tree of Life taxonomy pages for Aeropyrum Search Species2000 page for Aeropyrum MicrobeWiki page for Aeropyrum ... In taxonomy, Aeropyrum is a genus of the Desulfurococcaceae. The name Aeropyrum derives from: Greek noun aer, aeros (ἀήρ, ἀέρος ... Aeropyrum entry in LPSN [Euzéby, J.P. (1997). "List of Bacterial Names with Standing in Nomenclature: a folder available on the ...
The cells of Aeropyrum pernix are spherical in shape and approximately 1 µm in diameter. The envelope surrounding the cells of ... Type strain of Aeropyrum pernix at BacDive - the Bacterial Diversity Metadatabase Napotnik, T.B.; Valant, J.; Gmajner, D.; ... 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 ...
Retrieved from "https://species.wikimedia.org/w/index.php?title=Aeropyrum_pernix_ovoid_virus_1&oldid=6010329" ...
... 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/ ...
Aeropyrum pernix. Mutation(s): 0 EC: 3.4.19.1. Find proteins for Q9YBQ2 (Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM ... Crystal structure of an acylpeptide hydrolase/esterase from Aeropyrum pernix K1. Bartlam, M., Wang, G., Yang, H., Gao, R., Zhao ... The crystal structure of an APH from the thermophilic archaeon Aeropyrum pernix K1 to 2.1 A resolution confirms it to be a ... Crystal structure of an acylpeptide hydrolase/esterase from Aeropyrum pernix K1 in complex with p-nitrophenyl phosphate. *DOI: ...
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 ...
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. ...
... 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 ...
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:RFCL_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. ...
  • It appears that the Aeropyrum homologues both contain the equivalent of this residue, and are thus both Alba1-type proteins. (nih.gov)
  • Here, interactions between two paddle domains, KvAPp from the K v channel from Aeropyrum pernix and HsapBKp from the BK channel from Homo sapiens , and membrane models have been studied by spectroscopy. (diva-portal.org)
  • First, the membrane interaction of two paddle domains, K v APp, from the voltage-gated potassium channel K v AP from Aeropyrum pernix , and HsapBKp, from the human, large conductance, calcium-activated potassium channel HsapBK, was studied ( paper I and II ). (diva-portal.org)