The cytoplasmic hydrogenase (SHI) of the hyperthermophilic archaeon Pyrococcus furiosus is an NADP(H)-dependent heterotetrameric enzyme that contains a nickel-iron catalytic site, flavin, and six iron-sulfur clusters. It has potential utility in a range of bioenergy systems in vitro, but a major obstacle in its use is generating sufficient amounts. We have engineered P. furiosus to overproduce SHI utilizing a recently developed genetic system. In the overexpression (OE-SHI) strain, transcription of the four-gene SHI operon was under the control of a strong constitutive promoter, and a Strep-tag II was added to the N terminus of one subunit. OE-SHI and wild-type P. furiosus strains had similar rates of growth and H 2 production on maltose. Strain OE-SHI had a 20-fold higher transcription of the polycistronic hydrogenase mRNA encoding SHI, and the specific activity of the cytoplasmic hydrogenase was ∼10-fold higher when compared with the wild-type strain, although the expression levels of genes

The coordinated activities of AlaAT and GDH have been proposed to play an important role in the maintenance of the redox balance during fermentative growth of P. furiosus(19). These activities result in a change in the relative flux of pyruvate to acetate formation toward alanine formation. Pyruvate is therefore used as a catabolic electron sink. Due to the important role AlaAT plays in this pathway, this enzyme was purified from P. furiosus and represents the first AlaAT purified from either an archaeon or a hyperthermophile.. Similar to the AlaAT from mesophilic sources, the active form of the enzyme was found to be a homodimer with a subunit molecular mass of 43.5 kDa (22, 34, 36). It has been reported that the AlaATs have a high substrate specificity and are only able to transaminate alanine or glutamate (22, 34, 36). The P. furiosus enzyme, however, was capable of utilizing aspartate and, to a much lesser extent, the branched-chain amino acids with α-ketoglutarate as the amino acceptor, ...

The single cubane cluster ferredoxin (Fd) from the hyperthermophilic archaeon Pyrococcus furiosus (Pf) possesses several unique properties when compared even to Fds from other hyperthermophilic archaea or bacteria. These include an equilibrium molecular heterogeneity, a six- to seven-residue increase in size, an Asp rather than the Cys as one cluster ligand, and a readily reducible disulfide bond. NMR assignments and determination of both secondary structure and tertiary contacts remote from the paramagnetic oxidized cluster of Pf 3Fe Fd with an intact disulfide bond reported previously (Teng Q., Zhou, Z. H., Smith, E. T., Busse, S.C., Howard, J. B. Adams, M. W. W., and La Mar, G. (1994) Biochemistry 33, 6316-6328) are extended here to the 4Fe oxidized cluster WT (1H and 15N) and D14C (1H only) Fds with an intact disulfide bond and to the 4Fe oxidized WT Fd (1H and 15N) with a cleaved disulfide bond. All forms are shown to possess a long (13-member) α-helix, two β-sheets (one double-, one triple

TY - JOUR. T1 - Characterization of RNase HII substrate recognition using RNase HII-argonaute chimaeric enzymes from Pyrococcus furiosus. AU - Kitamura, Sayaka. AU - Fujishima, Kosuke. AU - Sato, Asako. AU - Tsuchiya, Daisuke. AU - Tomita, Masaru. AU - Kanai, Akio. PY - 2010/3/15. Y1 - 2010/3/15. N2 - RNase H (ribonuclease H) is an endonuclease that cleaves the RNA strand of RNA-DNA duplexes. It has been reported that the three-dimensional structure of RNase H is similar to that of the PIWI domain of the Pyrococcus furiosus Ago (argonaute) protein, although the two enzymes share almost no similarity in their amino acid sequences. Eukaryotic Ago proteins are key components of the RNA-induced silencing complex and are involved in microRNA or siRNA (small interfering RNA) recognition. In contrast, prokaryotic Ago proteins show greater affinity for RNA-DNA hybrids than for RNA-RNA hybrids. Interestingly, we found that wild-type Pf-RNase HII (P. furiosus, RNase HII) digests RNA-RNA duplexes in the ...

TY - JOUR. T1 - Influence of temperature on the production of archaeal thermoactive alcohol dehydrogenases from Pyrococcus furiosus with recombinant E. coli. AU - Kube, J.. AU - Brokamp, C.. AU - Machielsen, M.P.. AU - van der Oost, J.. AU - Markl, H.. PY - 2006. Y1 - 2006. N2 - The heterologous production of a thermoactive alcohol dehydrogenase (AdhC) from Pyrococcus furiosus in Escherichia coli was investigated. E. coli was grown in a fed-batch bioreactor in minimal medium to high cell densities (cell dry weight 76 g/l, OD600 of 150). Different cultivation strategies were applied to optimize the production of active AdhC, such as lowering the cultivation temperature from 37 to 28°C, heat shock of the culture from 37 to 42°C and from 37 to 45°C, and variation of time of induction (induction at an OD600 of 40, 80 and 120). In addition to the production of active intracellular protein, inclusion bodies were always observed. The maximal activity of 30 U/l (corresponding to 6 mg/l active ...

Pyrococcus furiosus PfuCP carboxypeptidase: metallocarboxypeptidase isolated from Pyrococcus furiosus; activated by cobalt; amino acid sequence in first source

Electron bifurcation has recently gained acceptance as the third mechanism of energy conservation in which energy is conserved through the coupling of exergonic and endergonic reactions. A structure-based mechanism of bifurcation has been elucidated recently for the flavin-based enzyme NADH-dependent ferredoxin NADP+ oxidoreductase I (NfnI) from the hyperthermophillic archaeon Pyrococcus furiosus. NfnI is thought to be involved in maintaining the cellular redox balance, producing NADPH for biosynthesis by recycling the two other primary redox carriers, NADH and ferredoxin. The P. furiosus genome encodes an NfnI paralog termed NfnII, and the two are differentially expressed depending on the growth conditions. In this study, we show that deletion of the genes encoding either NfnI or NfnII affects the cellular concentrations of NAD(P)H and particularly NADPH. This results in a moderate to severe growth phenotype in deletion mutants, demonstrating a key role for each enzyme in maintaining redox ...

The ribosome consists of small and large subunits each composed of dozens of proteins and RNA molecules. However, the functions of many of the individual protomers within the ribosome are still unknown. In this article, we describe the solution NMR structure of the ribosomal protein RP-L35Ae from the archaeon Pyrococcus furiosus. RP-L35Ae is buried within the large subunit of the ribosome and belongs to Pfam protein domain family PF01247, which is highly conserved in eukaryotes, present in a few archaeal genomes, but absent in bacteria. The protein adopts a six-stranded anti-parallel β-barrel analogous to the tRNA binding motif fold. The structure of the P. furiosus RP-L35Ae presented in this article constitutes the first structural representative from this protein domain family.

Pyrococcus furiosus (rushing fireball) was named for the ability of this archaeal coccus to rapidly swim at its optimal growth temperature, around 100 degrees C. Early electron microscopic studies identified up to 50 cell surface appendages originating from one pole of the coccus, which have been called flagella. We have analyzed these putative motility organelles and found them to be composed primarily (,95%) of a glycoprotein that is homologous to flagellins from other archaea. Using various electron microscopic techniques, we found that these flagella can aggregate into cable-like structures, forming cell-cell connections between ca. 5% of all cells during stationary growth phase. P. furiosus cells could adhere via their flagella to carbon-coated gold grids used for electron microscopic analyses, to sand grains collected from the original habitat (Porto di Levante, Vulcano, Italy), and to various other surfaces. P. furiosus grew on surfaces in biofilm-like structures, forming microcolonies ...

TY - CHAP. T1 - Protease activity in the hyperthermophilic archeon Pyrococcus furiosus.. AU - Voorhorst, W.G.B.. AU - Eggen, R.I.L.. AU - de Vos, W.M.. PY - 1993. Y1 - 1993. M3 - Abstract. BT - Abstract CEC meeting Biotechnology of extremophiles. Hamburg/D (1993). ER - ...

TY - CONF. T1 - Tungsten transport protein A (WtpA0 in Pyrococcus furiosus: first member of a new class of molybdate and tungstate transporters. AU - Bevers, LE. AU - Hagedoorn, PL. AU - Hagen, WR. PY - 2006. Y1 - 2006. KW - Geen BTA classificatie. M3 - Poster. Y2 - 11 December 2006 through 12 December 2006. ER - ...

Vol 13: Genetic engineering of Pyrococcus furiosus to use chitin as a carbon source.. . 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.

TY - CONF. T1 - Stabilization of recombinant β-glycosidase CelB from Pyrococcus furiosus by entrapment in the cell membrane of E. coli. AU - Kamrat, Thomas. AU - Nidetzky, Bernd. PY - 2004. Y1 - 2004. M3 - Poster. ER - ...

Pyrococcus furiosus ATCC ® 43587™ Designation: DSM 3638 TypeStrain=True Application: Produces intracellular protease PfpI Biotechnology

1E19: The 1.5-A Resolution Crystal Structure of the Carbamate Kinase-Like Carbamoyl Phosphate Synthetase from the Hyperthermophilic Archaeon Pyrococcus Furiosus, Bound to Adp, Confirms that This Thermoestable Enzyme is a Carbamate Kinase, and Provides Insights Into Substrate Binding and Stability in Carbamate Kinases

article{1ebb7d8e-f841-4330-8220-2d334e5f5cde, abstract = {A bacterial thermostable citrate synthase has been analyzed to investigate the structural basis of its thermostability, and to compare such features with those previously identified in archaeal citrate synthases. The gene encoding the citrate synthase from Thermus aquaticus was identified from a gene library by screening with a PCR fragment amplified from genomic DNA using a primer based on the determined N-terminal amino acid sequence and a citrate synthase consensus primer. Apart from high sequence similarities with citrate synthase sequences within the Thermus/Deinococcus group, the analyzed enzyme has highest similarities with the enzyme from the hyperthermophilic Archaeon Pyrococcus furiosus. The recombinant enzyme is a dimer with high specific activity. Compared to its thermoactivity (Topt at 80°C), the thermal stability of the enzyme is high, as judged from its Tm (101°C), and from irreversible thermal inactivation assays. ...

The extracellular α-amylase from the hyperthermophilic archaeum Pyrococcus furiosus (PFA) is extremely thermostable and of an industrial importance and interest. PFA aggregates and accumulates as insoluble inclusion bodies when expressed as a heterologous protein at a high level in Escherichia coli. In the present study, we investigated the roles of chaperones from P. furiosus in the soluble expression of recombinant PFA in E. coli. The results indicate that co-expression of PFA with the molecular chaperone prefoldin alone significantly increased the soluble expression of PFA. Although, co-expression of other main chaperone components from P. furiosus, such as the small heat shock protein (sHSP) or chaperonin (HSP60), was also able to improve the soluble expression of PFA to a certain extent. Co-expression of chaperonin or sHSP in addition to prefoldin did not further increase the soluble expression of PFA. This finding emphasizes the biotechnological potentials of the molecular chaperone prefoldin

Using both electron cryo-tomography and helical reconstruction, the first structure of the entire archaellum machinery with an assembled filament has been determined, providing the structural basis for our understanding of archaeal motility.

p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.,/p> ,p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.,/p> ,p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).,/p> ,p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x,sup>64,/sup> + x,sup>4,/sup> + x,sup>3,/sup> + x + 1. The algorithm is described in the ISO 3309 standard. ,/p> ,p class=publication>Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.,br /> ,strong>Cyclic redundancy and other checksums,/strong>,br /> ,a href=http://www.nrbook.com/b/bookcpdf.php>Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993),/a>),/p> Checksum:i ...

TET aminopeptidases are dodecameric particles shared in the three life domains involved in various biological processes, from carbon source provider in archaea to eye-pressure regulation in humans. Each subunit contains a dinuclear metal site (M1 and M2) responsible for the enzyme catalytic activity. However, the role of each metal ion is still uncharacterized. Noteworthy, while mesophilic TETs are activated by Mn(2+), hyperthermophilic TETs prefers Co(2+). Here, by means of anomalous x-ray crystallography and enzyme kinetics measurements of the TET3 aminopeptidase from the hyperthermophilic organism Pyrococcus furiosus (PfTET3), we show that M2 hosts the catalytic activity of the enzyme, while M1 stabilizes the TET3 quaternary structure and controls the active site flexibility in a temperature dependent manner. A new third metal site (M3) was found in the substrate binding pocket, modulating the PfTET3 substrate preferences. These data show that TET activity is tuned by the molecular interplay among

1J22: X-Ray and Biochemical Anatomy of an Archaeal XPF/Rad1/Mus81 Family Nuclease. Similarity between Its Endonuclease Domain and Restriction Enzymes

Benach J, Edstrom WC, Lee I, Das K, Cooper B, Xiao R, Liu J, Rost B, Acton TB, Montelione GT, et al. The 2.35 A structure of the TenA homolog from Pyrococcus furiosus supports an enzymatic function in thiamine metabolism. Acta Crystallogr D Biol Crystallogr. 2005 ;61(Pt 5):589-98. ...

Benach J, Edstrom WC, Lee I, Das K, Cooper B, Xiao R, Liu J, Rost B, Acton TB, Montelione GT, et al. The 2.35 A structure of the TenA homolog from Pyrococcus furiosus supports an enzymatic function in thiamine metabolism. Acta Crystallogr D Biol Crystallogr. 2005 ;61(Pt 5):589-98. ...

Intact protein analysis via top-down mass spectrometry (MS) provides the unique capability of fully characterizing protein isoforms and combinatorial post-translational modifications (PTMs) compared to the bottom-up MS approach. Front-end protein separation poses a challenge for analyzing complex mixtures of intact proteins on a proteomic scale. Here we applied capillary electrophoresis (CE) through a sheathless capillary electrophoresis-electrospray ionization (CESI) interface coupled to an Orbitrap Elite mass spectrometer to profile the proteome from Pyrococcus furiosus. CESI-top-down MS analysis of Pyrococcus furiosus cell lysate identified 134 proteins and 291 proteoforms with a total sample consumption of 270 ng in 120 min of total analysis time. Truncations and various PTMs were detected, including acetylation, disulfide bonds, oxidation, glycosylation, and hypusine. This is the largest scale analysis of intact proteins by CE-top-down MS to date ...

Pyrococcus is a genus of Thermococcaceaen archaean. Pyrococcus has similar characteristics of other thermoautotrophican archaea such as Archaeoglobus, and Methanococcus in the respect that they are all thermophilic and anaerobic. Pyrococcus differs, however, because its optimal growth temperature is nearly 100 °C and dwells at a greater sea depth than the other archaea. Studying Pyrococcus helps give insight to possible mechanisms used to endure extreme environmental conditions like high temperatures and high pressure. Three of the Pyrococcus species have been sequenced. P. furiosus is the largest containing 1.9Mb followed by P. abyssi with 1.8Mb and P. horikoshii with 1.7Mb.[citation needed] The genomes encode for many different metabolic enzymes which gives themselves a wider spectrum of living conditions because they can transport and metabolize a wide range of organic substances. Variation was detected between species as well. The cells of Pyrococcus are about 0.8-2 μm and are slightly ...

Domain: Archaea Phylum: Euryarchaeota Class: Thermococci Order: Thermococcales Family: Thermococcaceae Genus: Pyrococcus Species: Furiosus A weird litt...

1] Zeng, X., J. L. Birrien, Y. Fouquet, G. Cherkashov, M. Jebbar, J. Quérellou, P. Oger, M. A. Cambon-Bonavita, X. Xiao, and D. Prieur (2009) Pyrococcus CH1, an obligate piezophilic hyperthermophile: extending the upper pressure-temperature limits for life, ISME J. 3: 7, 873-876; doi: 10.1038/ismej.2009.21 [2] ,http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?id=529709, [3] Birrien, J. L., X. Zeng, M. Jebbar, M. A. Cambon-Bonavita, J. Quérellou, P. Oger, N. Bienvenu, X. Xiao, and D. Prieur (2011) Pyrococcus yayanosii sp. nov., an obligate piezophilic hyperthermophilic archaeon isolated from a deep-sea hydrothermal vent, Int J Syst Evol Microbiol 61: 12, 2827-2831; doi: 10.1099/ijs.0.024653-0 [4] Jun, X., L. Lupeng, X. Minjuan, P. Oger, W. Fengping, M. Jebbar, and X. Xiang (2011) Complete genome sequence of the obligate piezophilic hyperthermophilic archaeon Pyrococcus yayanosii CH1, J Bacteriol 193: 16, 4297-4298; doi: 10.1128/JB.05345-11 [5] ...

ID Q8U4B1_PYRFU Unreviewed; 663 AA. AC Q8U4B1; DT 01-JUN-2002, integrated into UniProtKB/TrEMBL. DT 01-JUN-2002, sequence version 1. DT 25-OCT-2017, entry version 68. DE RecName: Full=V-type ATP synthase subunit I {ECO:0000256,RuleBase:RU361189}; GN OrderedLocusNames=PF0177 {ECO:0000313,EMBL:AAL80301.1}; OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1). OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae; OC Pyrococcus. OX NCBI_TaxID=186497 {ECO:0000313,EMBL:AAL80301.1, ECO:0000313,Proteomes:UP000001013}; RN [1] {ECO:0000313,EMBL:AAL80301.1, ECO:0000313,Proteomes:UP000001013} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1 RC {ECO:0000313,Proteomes:UP000001013}; RX PubMed=10430560; RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M., RA DiRuggiero J., Robb F.T.; RT Divergence of the hyperthermophilic archaea Pyrococcus furiosus and RT P. horikoshii inferred from complete genomic ...

The proteasome is a protein-destroying apparatus involved in many essential cellular functions, such as regulation of cell cycle, cell differentiation, signal transduction pathways, antigen processing for appropriate immune responses, stress signaling, inflammatory responses, and apoptosis. It is capable of degrading a variety of cellular proteins in a rapid and timely fashion and most substrate proteins are modified by ubiquitin before their degradation by the proteasome. The proteasome is a large protein complex consisting of a proteolytic core called the 20S particle and ancillary factors that regulate its activity in various ways. The most common form is the 26S proteasome containing one 20S core particle and two 19S regulatory particles that enable the proteasome to degrade ubiquitinated proteins by an ATP-dependent mechanism. Another form is the immunoproteasome containing two 11S regulatory particles, PA28 alpha and PA28 beta, which are induced by interferon gamma under the conditions of ...

A novel maltose-forming α-amylase (PSMA) was recently found in the hyperthermophilic archaeon Pyrococcus sp. ST04. This enzyme shows ,13% amino-acid sequence identity to other known α-amylases and displays a unique enzymatic property in that it hydrolyzes both α-1,4-glucosidic and α-1,6-glucosidic linkages of substrates, recognizing only maltose units, in an exo-type manner. Here, the crystal structure of PSMA at a resolution of 1.8 Å is reported, showing a tight ring-shaped tetramer with monomers composed of two domains: an N-domain (amino acids 1-341) with a typical GH57 family (β/α)7-barrel fold and a C-domain (amino acids 342-597) composed of α-helical bundles. A small closed cavity observed in proximity to the catalytic residues Glu153 and Asp253 at the domain interface has the appropriate volume and geometry to bind a maltose unit, accounting for the selective exo-type maltose hydrolysis of the enzyme. A narrow gate at the putative subsite +1 formed by residue Phe218 and Phe452 is ...

Glutamate dehydrogenase (GDH) from the hyperthermophilic Archaeon ES4 (optimal growth temperature 98 degrees C and maximum growth temperature 110 degrees C) was purified to homogeneity. The purified native enzyme had an M(r) of 270,000 +/- 5,000 and was shown by gel filtration and SDS-polyacrylamide gel electrophoresis to be a hexamer with identical subunits of M(r) = 46,000 +/- 3,000. The hexameric subunit composition was also evident from electron micrographs, which show a triangular antiprism structure very similar to that of bovine GDH. The enzyme is exceptionally thermostable, with a half-time of inactivation of 3.5 h at 105 degrees C. Differential scanning calorimetry revealed a tm for denaturation of 113 degrees C, and a tm for activation at 60 degrees C. Antigenic cross-reaction with ES4 GDH was observed with the purified GDH from the thermophilic Archaea, Pyrococcus furiosus and Thermococcus litoralis as well as with bovine and yeast GDHs. The genome of ES4 was shown to contain a single ...

Angiotensin-converting enzyme (ACE) has a critical role in cardiovascular function by cleaving the carboxy terminal His-Leu dipeptide from angiotensin I to produce a potent vasopressor octapeptide, angiotensin II. Inhibitors of ACE are a first line of therapy for hypertension, heart failure, myocardial infarction and diabetic nephropathy. Notably, these inhibitors were developed without knowledge of the structure of human ACE, but were instead designed on the basis of an assumed mechanistic homology with carboxypeptidase A1. Here we present the X-ray structure of human testicular ACE and its complex with one of the most widely used inhibitors, lisinopril (N2-[(S)-1-carboxy-3-phenylpropyl]-l-lysyl-l-proline; also known as Prinivil or Zestril), at 2.0 Å resolution. Analysis of the three-dimensional structure of ACE shows that it bears little similarity to that of carboxypeptidase A, but instead resembles neurolysin2 and Pyrococcus furiosus carboxypeptidase3-zinc metallopeptidases with no detectable

Output. Pressure aided proteolysis of β-casein. M.E. Bruins, N. Creusot, H. Gruppen, A.E.M. Janssen, R.M. Boom. Submitted. Inactivation and conformational studies of β-glucosidase from Pyrococcus furiosus in the pressure-temperature-plane. M.E. Bruins, F. Meersman, A.E.M. Janssen, K. Heremans, R.M. Boom. (2008) Accepted in FEBS journal. Methylation in methanol-water mixtures: the effect of solvent quality and high-pressure. M.E. Bruins, K.M. Bekers, A.E.M. Janssen, R.M. Boom. (2008) Biophysical Chemistry. 134: 207-213. Full Text. The effect of pressure and temperature on the gelatinisation of starch at various starch concentrations. T. Baks, M.E. Bruins, A.E.M. Janssen, R.M. Boom. (2008) Biomacromolecules. 9(1): 296-304. Full Text. Effect of gelatinisation and hydrolysis conditions on the selectivity of starch hydrolysis with α-amylase from B. licheniformis. T. Baks, M.E. Bruins, A.M. Matser, A.E.M. Janssen, R.M. Boom. (2008) Journal of Agricultural and Food Chemistry. 56(2): 488-495. Full ...

Jung J-H, Seo D-H, Holden JF, Park C-S. 2014. Maltose-forming α-amylase from the hyperthermophilic archaeon Pyrococcus sp. ST04.. Appl Microbiol Biotechnol. 98(5):2121-31. ...

SWISS-MODEL Template Library (SMTL) entry for 1rwd.1. Backbone NMR Structure of a Mutant P. Furiosus Rubredoxin Using Residual Dipolar Couplings

Thermus and Pyrococcus Argonautes have been characterised as novel defence systems, revealing their unique property to use DNA guides for DNA interference.

The Adams Lab is part of the Department of Biochemistry and Molecular Biology at The University of Georgia. The laboratory is housed the Life Sciences Complex on South campus and has been in operation for nearly a decade. The group has a general interest in anaerobic microorganisms, particularly archaea and particularly those growing near and above 100 C, the so-called hyperthermophiles. The archaeon Pyrococcus furiosus and the bacterium Thermotoga maritima are being used as model systems. Projects involve the physiology, metabolism, enzymology, bioinorganic chemistry, and functional and structural genomics of these organisms. For example, the genome of P. furiosus contains approximately 2,200 ORFs, but the functions of much less than half of them are known.

In arginine biosynthesis two alternative pathways have evolved to split off the acetyl group ofN-acetylornithine.Enterobacteriaceae, Vibrionaceae,Myxococcus xanthus, and possibly also the archaeonSulfolobus acidocaldarius use a linear pathway in which the formation of ornithine is mediated by acetyl ornithinase (encoded by argE) (14, 12, 31, 36). Other bacteria, archaea, and eukaryotic microbes recycle the acetyl group by transacetylation of N-acetylornithine and glutamate (26). The transacetylation is catalyzed by ornithine acetyltransferase (encoded by argJ), an enzyme which in some organisms is also able to use acetyl coenzyme A to acetylate glutamate and in this way bypasses the first step of the linear pathway (11, 26). Ornithine carbamoyltransferase (encoded by argF) converts ornithine and carbamoyl phosphate (CP) into citrulline. CP is extremely thermolabile, and in Pyrococcus furiosus(17), Pyrococcus abyssi (25), andThermus thermophilus ZO5 (32), it appears to be protected from thermal ...

Pyrococcus horikoshii ATCC ® 700860D-5™ Designation: Genomic DNA from Pyrococcus horikoshii Strain JCM 9974 TypeStrain=True Application:

article{b41029bc-b035-41ca-a67d-c87d61d9f120, abstract = {Optimization of hexyl-beta-glycoside synthesis from lactose in hexanol at low water activity and high temperature was investigated using beta-glycosidases from hyperthermophilic organisms: Sulfolobus solfataricus (LacS) and Pyrococcus furiosus (CelB). The method for water activity adjustment by equilibration with saturated salt solutions was adapted for use at high temperature. The influence of enzyme immobilization (on XAD-4, XAD-16, or Celite), addition of surfactants (AOT or SDS), substrate concentration, water activity, and temperature (60-90degreesC) on enzymatic activity and hexyl-beta-glycoside yield were examined. Compared to other beta-glycosidases in lactose conversion into alkyl glycoside, these enzymes showed high activity in a hexanol one-phase system and synthesized high yields of both hexyl-beta-galactoside and hexyl-beta-glucoside. Using 32 g/l lactose (93 mM), LacS synthesized yields of 41% galactoside (38.1 mM) and 29% ...

IMAGE: Students pose next to the first generation of transgenic tomatoes expressing the gene encoding superoxide reductase (SOR) from the extremophilic microorganism Pyrococcus furiosus. SOR reduces toxic free radicals and results in plants with increased, heat, light and drought tolerance. The tomatoes were developed at NC State by Wendy Boss and Amy Grunden and funded by the NASA Institute for Advanced Concepts.. In Rothschilds lab, they treat extremophiles as a genetic hardware store, she explained, packed with capabilities that they can borrow in order to, for example, engineer desiccation resistance in other organisms. This kind of bio-engineering could be used to develop crops that will grow in more saline conditions as sea-levels rise or be able to tolerate the extreme weather patterns of our climate-changed future - and it will also be needed to design seeds that can withstand cosmic radiation on their way to Mars.. After all, according to Rothschild, its not a question of ...

1999 97. Schwerdtfeger, R. M., Chiaraluce, R., Consalvi, V., Scandurra, R., Antranikian, G. (1999) Stability, refolding and Ca2+ binding of pullulanase from the hyperthermophilic archaeon Pyrococcus woesei . Eur. J. Biochem. 264:479-487. 96. Linden, A., Niehaus, F., Antranikian, G. (20 00) Single-step purification of a recombinant thermostable α-amylase after solubilization of the enzyme from insoluble aggregates. Journal of Chromtography B. 737: 253-259. 95. Andrade, C.M., Pereira, N. Jr., Antranikian, G. (1999) Extremely thermophilic microorganisms and their polymerhydrolytic enzymes. Revista de Microbiologia 30: 287-298. 94. Stefanova, M. E., Schwerdtfeger, R., Antranikian, G., Scandurra, R. (1999) Heat-stable pullulanase from Bacillus acidopullulyticus : characterization and refolding after guanidinium chloride-induced unfolding. Extremophiles 3: 147-152. 93. Niehaus, F., Bertoldo, C., Kähler, M., Antranikian, G. (1999) Extremophiles as a source of novel enzymes for industrial application. ...

Mono- and Stereopictres of 5.0 Angstrom coordination sphere of Potassium atom in PDB 3l01: Crystal Structure of Monomeric Glycogen Synthase From Pyrococcus Abyssi

p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.,/p> ,p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.,/p> ,p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).,/p> ,p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x,sup>64,/sup> + x,sup>4,/sup> + x,sup>3,/sup> + x + 1. The algorithm is described in the ISO 3309 standard. ,/p> ,p class=publication>Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.,br /> ,strong>Cyclic redundancy and other checksums,/strong>,br /> ,a href=http://www.nrbook.com/b/bookcpdf.php>Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993),/a>),/p> Checksum:i ...

Pasomsup P. 2010. Isolation of pure culture and studies of physiological properties of a new hyperthermophullic archaeon Pyrococcus sp. strain Pikanate 5017 from Pong Dueat hot spring, Huai Nam Dang National Park. Thesis for Master of Science (Microbiology), Silpakorn University, 92 pp. (In Thai ...

RNase P, a ribozyme-based ribonucleoprotein (RNP) complex that catalyzes tRNA 5′-maturation, is ubiquitous in all domains of life, but the evolution of its protein components (RNase P proteins, RPPs) is not well understood. Archaeal RPPs may provide clues on how the complex evolved from an ancient ribozyme to an RNP with multiple archaeal and eukaryotic (homologous) RPPs, which are unrelated to the single bacterial RPP. Here, we analyzed the sequence and structure of archaeal RPPs from over 600 available genomes. All five RPPs are found in eight archaeal phyla, suggesting that these RPPs arose early in archaeal evolutionary history. The putative ancestral genomic loci of archaeal RPPs include genes encoding several members of ribosome, exosome, and proteasome complexes, which may indicate coevolution/coordinate regulation of RNase P with other core cellular machineries. Despite being ancient, RPPs generally lack sequence conservation compared to other universal proteins. By analyzing the relative

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The enzymes isolated from some extremophiles have proven to be of great use in the biotechnology industry, able to function under conditions that would denature enzymes taken from most normal organisms. The most commonly used DNA polymerase for the polymerase chain reaction technique is Taq DNA polymerase, originally isolated from Thermus aquaticus, a bacterial species found in surface aquatic locations such as Yellowstone National Park hot springs. For a few PCR applications, the lack of proofreading by Taq DNA polymerase is a problem. The DNA polymerase from Thermococcus litoralis was shown to have a proofreading exonuclease activity. (Mattila et al, 1991)Thermococcus litoralis was isolated from a deep sea hydrothermal vent. This DNA polymerase is marketed as Vent polymerase. Another heat stable polymerase comes from the organism Pyrococcus furiosus, (Pfu). This organism grows optimally at 100°C, making it a hyperthermophile. Taq DNA polymerase is adequate for most PCR, but one study ...

The gene (PH1074) encoding the NAD kinase of the hyperthermophilic archaeon Pyrococcus horikoshii was identified in the genome database, cloned, and functionally expressed in Escherichia coli. The recombinant enzyme was purified to homogeneity by heat treatment at 90 degrees C for 20 min and one successive HiTrap affinity chromatography step. The purified enzyme was easily precipitated by dialysis against phosphate buffer without NaCl and imidazole and was usually stored in buffer containing 0.5 M NaCl and 0.5 M imidazole to avoid precipitation. The molecular mass of the active enzyme was determined to be 145 kDa by a gel filtration method, and the enzyme was composed of a tetramer of 37-kDa subunits. The archaeal enzyme utilized several nucleoside triphosphates, such as GTP, CTP, UTP, and ITP, as well as ATP and inorganic polyphosphates [poly(P)] as phosphoryl donors for NAD phosphorylation. The enzyme utilized poly(P)27 (the average length of the phosphoryl chain was 27) as the most active ...

Empadinhas, N., Marugg, J.D., Borges, N., Santos, H. and da Costa, M.S. (2001). Pathway for the synthesis of mannosylglycerate in the hyperthermophilic archaeon Pyrococcus horikoshii. Biochemical and genetic characterization of key-enzymes. J. Biol. Chem. 276: 43580-43588. PMID 11562374. ...

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The protein encoded by this gene is a homodimeric integral membrane gelatinase belonging to the serine protease family. It is selectively expressed in reactive stromal fibroblasts of epithelial cancers, granulation tissue of healing wounds, and malignant cells of bone and soft tissue sarcomas. This protein is thought to be involved in the control of fibroblast growth or epithelial-mesenchymal interactions during development, tissue repair, and epithelial carcinogenesis. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Apr 2014] ...