Aeropyrum
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
RNA, Transfer, Thr
Thermoproteaceae
Hydrothermal Vents
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
RNA, Archaeal
Enzyme Stability
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)
Outside the unusual cell wall of hyperthermophilic archaeon Aeropyrum pernix | Molecular & Cellular Proteomics
Enzymatic Degradation of PrPSc by a Protease Secreted from Aeropyrum pernix K1 - pdf descargar
Aeropyrum pernix Sako et al., 1996
HOGENOM: AEPER1 1 PE483
Aeropyrum pernix ovoid virus 1 (APOV1)
rpl7ae - 50S ribosomal protein L7Ae - Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1) - rpl7ae...
ApeEx03F01 - Aeropyrum pernix
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List of Archaea genera
2009 Aeropyrum Sako et al. 1996 Acidilobus Prokofeva et al. 2000 Caldisphaera Itoh et al. 2003 ?Stetteria Jochimsen, Peinemann- ...
Betaguttavirus
Aeropyrum pernix archaea serve as natural hosts. There is only one species in this genus: Aeropyrum pernix ovoid virus 1. ... Aeropyrum pernix archaea serve as the natural host. Transmission routes are passive diffusion. Prangishvili, D; Mochizuki, T; ...
2'-phosphotransferase
Kato-Murayama M, Bessho Y, Shirouzu M, Yokoyama S (2005). "Crystal structure of the RNA 2'-phosphotransferase from Aeropyrum ...
O-phosphoserine sulfhydrylase
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 ...
List of sequenced archaeal genomes
April 1999). "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon, Aeropyrum pernix K1". DNA Research. 6 (2 ...
List of restriction enzyme cutting sites: A
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 ...
Origin of replication
"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 ...
Geranylfarnesyl diphosphate synthase
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 ...
Spiraviridae
... 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 replicated in other strains of A. pernix or in Aeropyrum camini, so the original A. pernix culture was used ... ACV was first isolated from a sample of Aeropyrum pernix (A. pernix) taken from the coastal Yamagawa Hot Spring, where the ...
Terpene
"Modified mevalonate pathway of the archaeon Aeropyrum pernix proceeds via trans -anhydromevalonate 5-phosphate". Proceedings of ...
Acidilobus saccharovorans
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, ...
TRNA-intron endonuclease
The heterotetramer (αβ)2 structure is found in Nanoarchaeum equitans, Pyrobaculum aerophilum, Aeropyrum pernix, and ...
Clavaviridae
"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 ...
Methanosarcina
In 2004, two primitive versions of hemoglobin were discovered in M. acetivorans and another archaeon, Aeropyrum pernix. Known ...
Methionine
... 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 ...
Archaeal virus
Spiravirus Aeropyrum coil-shaped virus has the largest known genome of an ssDNA virus at about 35 kb. Some archaeal viruses, ... Aeropyrum coil-shaped virus was identified in 2012 as the first spiravirus and the first known ssDNA archaeal virus. Sulfolobus ... The genomes of archaeal viruses vary in size significantly, ranging from 5.3 kilobases (kb) in clavavirus Aeropyrum pernix ...
Tyrosine-tRNA ligase
The crystal structures of the YARSs from Archeoglobus fulgidus, Pyrococcus horikoshii and Aeropyrum pernix have also been ...
Hyperthermophile
Archaeoglobus fulgidus Methanococcus jannaschii Aeropyrum pernix Sulfolobus Methanopyrus kandleri strain 116, an archaeon in 80 ...
Deoxyribose-phosphate aldolase
The structure of DERAs across many organisms: DERAs from Escherichia coli and Aeropyrum pernix shares 37.7% sequence identity ...
Guttaviridae
Characterization of Aeropyrum pernix spindle-shaped virus 1 and Aeropyrum pernix ovoid virus 1. J Bacteriol 193(19):5412-5419 ... Alphaguttavirus Sulfolobus newzealandicus droplet-shaped virus Betaguttavirus Aeropyrum pernix ovoid virus 1 Viruses in the ...
David Prangishvili
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 ...
List of MeSH codes (B07)
MeSH B07.075.200.500 - desulfurococcaceae MeSH B07.075.200.500.050 - aeropyrum MeSH B07.075.200.650 - pyrodictiaceae MeSH ...
Archaea
... and the other one by the Aeropyrum coil-shaped virus (Spiraviridae) infecting a hyperthermophilic (optimal growth at 90-95 °C) ...
List of virus species
... phiO18P Aeromonas virus pIS4A Aeromonas virus ZPAH7 Aeropyrum coil-shaped virus Aeropyrum pernix bacilliform virus 1 Aeropyrum ...
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 ... Aeropyrum entry in LPSN; Euzéby, J.P. (1997). "List of Bacterial Names with Standing in Nomenclature: a folder available on the ...
Aeropyrum pernix
Type strain of Aeropyrum pernix at BacDive - the Bacterial Diversity Metadatabase KEGG Genome : Aeropyrum pernix (Articles with ... 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 archaea in the archaeal phylum Thermoproteota. It is an obligatorily thermophilic ... Aeropyrum pernix was the first strictly aerobic hyperthermophilic Archaea to be discovered. It was originally isolated from ...
Pernix16
- Aeropyrum pernix gen. nov., sp. (wikipedia.org)
- A Unique Catalytic Triad Revealed By the Crystal Structure of APE0912, A Short-Chain Dehydrogenase/Reductase Family Protein From Aeropyrum Pernix K1 Proteins V. 70 1640 2008 . (atomistry.com)
- In the present study, we identify two prenyltransferases and a prenyl reductase responsible for the biosynthesis of C25,C25-diether lipids in the hyperthermophilic archaeon Aeropyrum pernix. (nii.ac.jp)
- Mapping the network of correlated residues onto the 3D structure of the Kv channel from Aeropyrum pernix disclosed correlations between residues in the voltage-sensor paddle and the pore region, including regions that are involved in the gating transition. (bgu.ac.il)
- Using saturation mutagenesis, we investigated the role of a conserved residue (Arg(526)) at the active site of acylaminoacyl peptidase from hyperthermophilic Aeropyrum pernix K1 in substrate discrimination and catalytic mechanism. (inrae.fr)
- Crystal Structure of an Acylpeptide Hydrolase/Esterase from Aeropyrum pernix K1. (inrae.fr)
- 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. (inrae.fr)
- Nomura, N., Sako, Y. and Uchida, A. Molecular characterization and postsplicing fate of three introns within the single rRNA operon of the hyperthermophilic archaeon Aeropyrum pernix K1. (riken.jp)
- UP000010469) Desulfurococcales Desulfurococcaceae Aeropyrum Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100. (expasy.org)
- Some examples include:Aeropyrum pernix.Thermosphaera aggregans.Ignisphaera aggregans.Sulfolobus tokodaii.Metallosphaera sedula.Staphylothermus marinus.Thermoproteus tenax. (psichologyanswers.com)
- Examples include:Acidilobus saccharovorans.Aeropyrum pernix.Desulfurococcus kamchatkensis.Hyperthermus butylicus.Igniococcus hospitalis.Ignisphaera aggregans.Pyrolobus fumarii.Staphylothermus hellenicus.Meer items. (psichologyanswers.com)
- My principle objective was to isolate the DNA encoding Lipoic Acid Synthase (lipA) in Aeropyrum pernix (a thermophilic bacterium), and to over express the protein (LipA). (woodstock-online.com)
- It is synthesised by LipA in the following reaction:DNA from Aeropyrum pernix was kindly provided by Dr. M. Kreik (Southampton University), which contained the required gene. (woodstock-online.com)
- Finally, the bacteria containing the correct plasmid were allowed to grow in bacterial culture medium and the protein was isolated using Nickel affinity chromatography.The purified DNA of the thermophilic bacteria Aeropyrum pernix was provided. (woodstock-online.com)
- Despite their abundance in mesophilic bacteria, the only available prokaryotic Kv channel structure comes from a hyperthermophilic archaea Aeropyrum pernix (KvAP), which may not be representative of mesophilic bacterial Kv channels. (ccemmp.org)
- Herstellung rekombinanter aa 3 - und ba 3 -Cytochrom-c-Oxidasen von Aeropyrum pernix K1 in Paracoccus denitrificans und Reinigung der Wildtyp-aa 3 - und ba 3 -Cytochrom-c-Oxidasen aus Aeropyrum pernix K1. (mpg.de)
Archaeon1
- Variation of the Virus-Related Elements within Syntenic Genomes of the Hyperthermophilic Archaeon Aeropyrum" (PDF). (wikipedia.org)
Desulfurococcaceae1
- In taxonomy, Aeropyrum is a genus of the Desulfurococcaceae. (wikipedia.org)
Desulfurococcus1
- The most frequently occurring genera were Aeropyrum (18.1%), Desulfurococcus (11.1%), Ignicoccus (9.8%), Vulcanisaeta (7.8%) and Staphylothermus (7.0%) (68 hits in total). (microrna21.com)