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

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)

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

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)

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

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)

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

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)

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

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)

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

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)

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

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)

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

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)

*  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 ...
*  Aeropyrum pernix
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 ...
*  Betaguttavirus
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 ...
*  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
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 ...
*  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 ...
*  Geranylfarnesyl diphosphate synthase
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. ...
*  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, ...
*  Clavaviridae
"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 ...
*  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 ...
*  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 ...
*  Guttaviridae
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 ...
*  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 ...
*  Taxonomic list of viruses
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: ...
*  Archaea
... infecting halophilic archaea and the other one by the Aeropyrum coil-shaped virus ("Spiraviridae") infecting a ...
*  List of Archaea genera
Genus Acidilobus Genus Acidococcus Genus Aeropyrum Genus Desulfurococcus Genus Ignicoccus Genus Staphylothermus Genus Stetteria ...
*  List of virus species
Aes508 Aeromonas virus AS4 Aeromonas virus phiO18P Aeropyrum coil-shaped virus Aeropyrum pernix bacilliform virus 1 Aeropyrum ...
Aeropyrum pernix ovoid virus 1 (APOV1)  Aeropyrum pernix ovoid virus 1 (APOV1)
"Provirus Induction in Hyperthermophilic Archaea: Characterization of Aeropyrum pernix Spindle-Shaped Virus 1 and Aeropyrum ...
more infohttp://www.uniprot.org/proteomes/UP000008911
Aeropyrum pernix Sako et al., 1996  Aeropyrum pernix Sako et al., 1996
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. ...
more infohttps://www.gbif.org/species/1000037
Enzymatic Degradation of PrPSc by a Protease Secreted from Aeropyrum pernix K1 - pdf descargar  Enzymatic Degradation of PrPSc by a Protease Secreted from Aeropyrum pernix K1 - pdf descargar
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. ...
more infohttp://libros.duhnnae.com/2017/jun7/149814542840-Enzymatic-Degradation-of-PrPSc-by-a-Protease-Secreted-from-Aeropyrum-pernix-K1.php
باستانیان - ویکی‌پدیا، دانشنامهٔ آزاد  باستانیان - ویکی‌پدیا، دانشنامهٔ آزاد
... and the other one by the Aeropyrum coil-shaped virus ("Spiraviridae") infecting a hyperthermophilic (optimal growth at 90-95 °C ...
more infohttps://fa.wikipedia.org/wiki/%D8%A8%D8%A7%D8%B3%D8%AA%D8%A7%D9%86%DB%8C%D8%A7%D9%86?match=en
Archaea - Wikipedia  Archaea - Wikipedia
... and the other one by the Aeropyrum coil-shaped virus ("Spiraviridae") infecting a hyperthermophilic (optimal growth at 90-95 °C ...
more infohttps://en.m.wikipedia.org/wiki/Archaea
KAKEN - Researchers | KUNO Atsushi (50302287)  KAKEN - Researchers | KUNO Atsushi (50302287)
Aeropyrum pernix K1,進化,Aminoacyl-tRNA synthetase,肝線維化,バイオマ ... 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 … More / protein / 古細菌 ... Aeropyrum pernix / Archaea identity / 臨床 / WFA-M2BP / マクロファージ / 分離培養
more infohttps://nrid.nii.ac.jp/nrid/1000050302287/
Aeropyrum - Wikipedia  Aeropyrum - Wikipedia
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 ...
more infohttps://en.wikipedia.org/wiki/Aeropyrum
Aeropyrum pernix - Wikipedia  Aeropyrum pernix - Wikipedia
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 ...
more infohttps://en.wikipedia.org/wiki/Aeropyrum_pernix
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)  Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
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). ...
more infohttp://www.uniprot.org/proteomes/UP000002518
Active site of Zn2+-dependent sn-glycerol-1-phosphate dehydrogenase from Aeropyrum pernix K1  Active site of Zn2+-dependent sn-glycerol-1-phosphate dehydrogenase from Aeropyrum pernix K1
... Jin-Suk Han1 and Kazuhiko ... Jin-Suk Han and Kazuhiko Ishikawa, "Active site of Zn2+-dependent sn-glycerol-1-phosphate dehydrogenase from Aeropyrum pernix ...
more infohttps://www.hindawi.com/journals/archaea/2005/257264/cta/
Microbiology Society Journals | Aeropyrum pernix membrane topology of protein VKOR promotes protein disulfide bond formation in...  Microbiology Society Journals | Aeropyrum pernix membrane topology of protein VKOR promotes protein disulfide bond formation in...
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. ...
more infohttp://mic.microbiologyresearch.org/content/journal/micro/10.1099/mic.0.000569
Purification and biochemical properties of a cytochrome bc complex from the aerobic hyperthermophilic archaeon Aeropyrum pernix...  Purification and biochemical properties of a cytochrome bc complex from the aerobic hyperthermophilic archaeon Aeropyrum pernix...
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 ...
more infohttps://0-bmcmicrobiol-biomedcentral-com.brum.beds.ac.uk/articles/10.1186/1471-2180-11-52
Purification and biochemical properties of a cytochrome bc complex from the aerobic hyperthermophilic archaeon Aeropyrum pernix...  Purification and biochemical properties of a cytochrome bc complex from the aerobic hyperthermophilic archaeon Aeropyrum pernix...
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 ...
more infohttps://bmcmicrobiol.biomedcentral.com/articles/10.1186/1471-2180-11-52
AKR Superfamily || Potential AKR Members  AKR Superfamily || Potential AKR Members
Aeropyrum pernix. APE1495 APE1659 APE1961 7516538. 7447932. 7431108 Agrobacterium tumefaciens mocA AAB07785 ...
more infohttps://www.med.upenn.edu/akr/potential.html
Isolation an d biochemical characterization of a metagenome- derive d 3- deoxy- d-arabino-heptulosonate-7-phosphate synthase...  Isolation an d biochemical characterization of a metagenome- derive d 3- deoxy- d-arabino-heptulosonate-7-phosphate synthase...
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. ...
more infohttps://link.springer.com/article/10.1186%2Fs13568-019-0742-4
KEGG T00023: APE 2106.1  KEGG T00023: APE 2106.1
Aeropyrum pernix: APE_2106.1. Entry. APE_2106.1 CDS T00023 Definition. (GenBank) ATP-dependent 6-phosphofructokinase. ...
more infohttp://www.genome.jp/dbget-bin/www_bget?ape:APE_2106.1
Evaluation method for the potential functionome harbored in the genome and metagenome | BMC Genomics | Full Text  Evaluation method for the potential functionome harbored in the genome and metagenome | BMC Genomics | Full Text
Aeropyrum pernix, neq:Nanoarchaeum equitans. Blue bar: old KAAS, Red bar: new KAAS. Figure S9. Effect of database dependency on ...
more infohttps://bmcgenomics.biomedcentral.com/articles/10.1186/1471-2164-13-699