Relevant bibliographies by topics / Psychrophilic enzyme

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  2. Dissertations / Theses
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Academic literature on the topic 'Psychrophilic enzyme'

Author: Grafiati
Published: 9 March 2023
Last updated: 10 March 2023

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Journal articles on the topic "Psychrophilic enzyme"

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Kazuoka, Takayuki, Shouhei Takigawa, Noriaki Arakawa, Yoshiyuki Hizukuri, Ikuo Muraoka, Tadao Oikawa, and Kenji Soda. "Novel Psychrophilic and Thermolabile l-Threonine Dehydrogenase from Psychrophilic Cytophaga sp. Strain KUC-1." Journal of Bacteriology 185, no. 15 (August 1, 2003): 4483–89. http://dx.doi.org/10.1128/jb.185.15.4483-4489.2003.

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ABSTRACT A psychrophilic bacterium, Cytophaga sp. strain KUC-1, that abundantly produces a NAD+-dependent l-threonine dehydrogenase was isolated from Antarctic seawater, and the enzyme was purified. The molecular weight of the enzyme was estimated to be 139,000, and that of the subunit was determined to be 35,000. The enzyme is a homotetramer. Atomic absorption analysis showed that the enzyme contains no metals. In these respects, the Cytophaga enzyme is distinct from other l-threonine dehydrogenases that have thus far been studied. l-Threonine and dl-threo-3-hydroxynorvaline were the substrates, and NAD+ and some of its analogs served as coenzymes. The enzyme showed maximum activity at pH 9.5 and at 45°C. The kinetic parameters of the enzyme are highly influenced by temperatures. The Km for l-threonine was lowest at 20°C. Dead-end inhibition studies with pyruvate and adenosine-5′-diphosphoribose showed that the enzyme reaction proceeds via the ordered Bi Bi mechanism in which NAD+ binds to an enzyme prior to l-threonine and 2-amino-3-oxobutyrate is released from the enzyme prior to NADH. The enzyme gene was cloned into Escherichia coli, and its nucleotides were sequenced. The enzyme gene contains an open reading frame of 939 bp encoding a protein of 312 amino acid residues. The amino acid sequence of the enzyme showed a significant similarity to that of UDP-glucose 4-epimerase from Staphylococcus aureus and belongs to the short-chain dehydrogenase-reductase superfamily. In contrast, l-threonine dehydrogenase from E. coli belongs to the medium-chain alcohol dehydrogenase family, and its amino acid sequence is not at all similar to that of the Cytophaga enzyme. l-Threonine dehydrogenase is significantly similar to an epimerase, which was shown for the first time. The amino acid residues playing an important role in the catalysis of the E. coli and human UDP-glucose 4-epimerases are highly conserved in the Cytophaga enzyme, except for the residues participating in the substrate binding.
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Jaafar, Nardiah Rizwana, Dene Littler, Travis Beddoe, Jamie Rossjohn, Rosli Md Illias, Nor Muhammad Mahadi, Mukram Mohamed Mackeen, Abdul Munir Abdul Murad, and Farah Diba Abu Bakar. "Crystal structure of fuculose aldolase from the Antarctic psychrophilic yeastGlaciozyma antarcticaPI12." Acta Crystallographica Section F Structural Biology Communications 72, no. 11 (October 27, 2016): 831–39. http://dx.doi.org/10.1107/s2053230x16015612.

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Fuculose-1-phosphate aldolase (FucA) catalyses the reversible cleavage of L-fuculose 1-phosphate to dihydroxyacetone phosphate (DHAP) and L-lactaldehyde. This enzyme from mesophiles and thermophiles has been extensively studied; however, there is no report on this enzyme from a psychrophile. In this study, the gene encoding FucA fromGlaciozyma antarcticaPI12 (GaFucA) was cloned and the enzyme was overexpressed inEscherichia coli, purified and crystallized. The tetrameric structure of GaFucA was determined to 1.34 Å resolution. The overall architecture of GaFucA and its catalytically essential histidine triad are highly conserved among other fuculose aldolases. Comparisons of structural features between GaFucA and its mesophilic and thermophilic homologues revealed that the enzyme has typical psychrophilic attributes, indicated by the presence of a high number of nonpolar residues at the surface and a lower number of arginine residues.
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Rathour, Rashmi, Juhi Gupta, Bhawna Tyagi, and Indu Shekhar Thakur. "Production and characterization of psychrophilic α-amylase from a psychrophilic bacterium, Shewanella sp. ISTPL2." Amylase 4, no. 1 (November 18, 2020): 1–10. http://dx.doi.org/10.1515/amylase-2020-0001.

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AbstractA psychrophilic and halophilic bacterial isolate, Shewanella sp. ISTPL2, procured from the pristine Pangong Lake, Ladakh, Jammu and Kashmir, India, was used for the production and characterization of the psychrophilic and alkalophilic α-amylase enzyme. The α-amylase is a critical enzyme that catalyses the hydrolysis of α-1,4-glycosidic bonds of starch molecules and is predominately utilized in biotechnological applications. The highest enzyme activity of partially purified extracellular α-amylase was 10,064.20 U/mL after 12 h of incubation in a shake flask at pH 6.9 and 10 °C. Moreover, the maximum intracellular α-amylase enzyme activity (259.62 U/mL) was also observed at 6 h of incubation. The extracellular α-amylase was refined to the homogeneity with the specific enzyme activity of 36,690.47 U/mg protein corresponding to 6.87-fold purification. The optimized pH and temperature for the α-amylase were found to be pH 8 and 4 °C, respectively, suggesting its stability at alkaline conditions and low or higher temperatures. The amylase activity was highly activated by Cu2+, Fe2+ and Ca2+, while inhibited by Cd2+, Co2+ and Na2+. As per our knowledge, the current study reports the highest activity of a psychrophilic α-amylase enzyme providing prominent biotechnological potential.
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Mat-Sharani, Shuhaila, Reyad Al Moheer, Farah-Diba Abu-Bakar, Abdul-Munir Abdul-Murad, and Nor-Muhammad Mahadi. "Structure Flexibility of Alpha-galactosidase from a Marine Psychrophilic Yeast, Glaciozyma antarctica PI12." Squalen Bulletin of Marine and Fisheries Postharvest and Biotechnology 17, no. 3 (December 30, 2022): 121–30. http://dx.doi.org/10.15578/squalen.680.

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Factors that contribute to maintaining the flexibility or stability of an enzyme structure may depend on the composition of each amino acid with different characteristics, providing a purpose and bonding features within the structure. Based on this assumption, a study using homology modeling and a comparative study to observe different structure behaviors of an enzyme at an extremely low temperature (psychrophile) against temperate (mesophile) and high temperature (thermophile) was performed. The subject, a-galactosidase from Glaciozyma antarctica as a marine psychrophilic candidate was chosen against a-galactosidase from Trichoderma reesei (mesophile) and Ramsonia emersonii (thermophile). This enzyme catalyzes the hydrolysis of a-1-6 linked terminal galactosyl residues which can be found in a wide range of the organism. The ability of G. antarctica to grow in extremely cold temperatures rendered the question that the enzyme must have special characteristics to adapt to the cold condition. Based on the homology modeling and molecular dynamics study, a comparison of the structure of G. antarctica a-galactosidase enzymes with its homolog from the mesophilic and thermophilic fungi showed that G. antarctica a-galactosidase enzyme confers its flexibility by the increased number of small amino acids with reduced charges, more loops, a fewer number of hydrogen and disulfide bonds in its structure. Furthermore, a-galactosidase has potential for commercialization in bleach paper and the baking industry also a treatment for bloating and Fabry disease.
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Yang, Guang, Matteo Mozzicafreddo, Patrizia Ballarini, Sandra Pucciarelli, and Cristina Miceli. "An In-Silico Comparative Study of Lipases from the Antarctic Psychrophilic Ciliate Euplotes focardii and the Mesophilic Congeneric Species Euplotes crassus: Insight into Molecular Cold-Adaptation." Marine Drugs 19, no. 2 (January 27, 2021): 67. http://dx.doi.org/10.3390/md19020067.

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Cold-adapted enzymes produced by psychrophilic organisms have elevated catalytic activities at low temperatures compared to their mesophilic counterparts. This is largely due to amino acids changes in the protein sequence that often confer increased molecular flexibility in the cold. Comparison of structural changes between psychrophilic and mesophilic enzymes often reveal molecular cold adaptation. In the present study, we performed an in-silico comparative analysis of 104 hydrolytic enzymes belonging to the family of lipases from two evolutionary close marine ciliate species: The Antarctic psychrophilic Euplotes focardii and the mesophilic Euplotes crassus. By applying bioinformatics approaches, we compared amino acid composition and predicted secondary and tertiary structures of these lipases to extract relevant information relative to cold adaptation. Our results not only confirm the importance of several previous recognized amino acid substitutions for cold adaptation, as the preference for small amino acid, but also identify some new factors correlated with the secondary structure possibly responsible for enhanced enzyme activity at low temperatures. This study emphasizes the subtle sequence and structural modifications that may help to transform mesophilic into psychrophilic enzymes for industrial applications by protein engineering.
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Sulthana, Shaheen, Purusharth I. Rajyaguru, Pragya Mittal, and Malay K. Ray. "rnrGene from the Antarctic Bacterium Pseudomonas syringae Lz4W, Encoding a Psychrophilic RNase R." Applied and Environmental Microbiology 77, no. 22 (September 16, 2011): 7896–904. http://dx.doi.org/10.1128/aem.05683-11.

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ABSTRACTRNase R is a highly processive, hydrolytic 3′-5′ exoribonuclease belonging to the RNB/RNR superfamily which plays significant roles in RNA metabolism in bacteria. The enzyme was observed to be essential for growth of the psychrophilic Antarctic bacteriumPseudomonas syringaeLz4W at a low temperature. We present results here pertaining to the biochemical properties of RNase R and the RNase R-encoding gene (rnr) locus from this bacterium. By cloning and expressing a His6-tagged form of theP. syringaeRNase R (RNase RPs), we show that the enzyme is active at 0 to 4°C but exhibits optimum activity at ∼25°C. The enzyme is heat labile in nature, losing activity upon incubation at 37°C and above, a hallmark of many psychrophilic enzymes. The enzyme requires divalent cations (Mg2+and Mn2+) for activity, and the activity is higher in 50 to 150 mM KCl when it largely remains as a monomer. On synthetic substrates, RNase RPsexhibited maximum activity on poly(A) and poly(U) in preference over poly(G) and poly(C). The enzyme also degraded structuredmalE-malFRNA substrates. Analysis of the cleavage products shows that the enzyme, apart from releasing 5′-nucleotide monophosphates by the processive exoribonuclease activity, produces four-nucleotide end products, as opposed to two-nucleotide products, of RNA chain byEscherichia coliRNase R. Interestingly, three ribonucleotides (ATP, GTP, and CTP) inhibited the activity of RNase RPsin vitro. The ability of the nonhydrolyzable ATP-γS to inhibit RNase RPsactivity suggests that nucleotide hydrolysis is not required for inhibition. This is the first report on the biochemical property of a psychrophilic RNase R from any bacterium.
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Drienovska, Ivana, Eva Chovancova, Tana Koudelakova, Jiri Damborsky, and Radka Chaloupkova. "Biochemical Characterization of a Novel Haloalkane Dehalogenase from a Cold-Adapted Bacterium." Applied and Environmental Microbiology 78, no. 14 (May 11, 2012): 4995–98. http://dx.doi.org/10.1128/aem.00485-12.

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ABSTRACTA haloalkane dehalogenase, DpcA, fromPsychrobacter cryohalolentisK5, representing a novel psychrophilic member of the haloalkane dehalogenase family, was identified and biochemically characterized. DpcA exhibited a unique temperature profile with exceptionally high activities at low temperatures. The psychrophilic properties of DpcA make this enzyme promising for various environmental applications.
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Bujacz, Anna, Maria Rutkiewicz-Krotewicz, Karolina Nowakowska-Sapota, and Marianna Turkiewicz. "Crystal structure and enzymatic properties of a broad substrate-specificity psychrophilic aminotransferase from the Antarctic soil bacteriumPsychrobactersp. B6." Acta Crystallographica Section D Biological Crystallography 71, no. 3 (February 26, 2015): 632–45. http://dx.doi.org/10.1107/s1399004714028016.

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Aminotransferases (ATs) are enzymes that are commonly used in the chemical and pharmaceutical industries for the synthesis of natural and non-natural amino acids by transamination reactions. Currently, the easily accessible enzymes from mesophilic organisms are most commonly used; however, for economical and ecological reasons the utilization of aminotransferases from psychrophiles would be more advantageous, as their optimum reaction temperature is usually significantly lower than for the mesophilic ATs. Here, gene isolation, protein expression, purification, enzymatic properties and structural studies are reported for the cold-active aromatic amino-acid aminotransferase (PsyArAT) fromPsychrobactersp. B6, a psychrotrophic, Gram-negative strain from Antarctic soil. Preliminary computational analysis indicated dual functionality of the enzyme through the ability to utilize both aromatic amino acids and aspartate as substrates. This postulation was confirmed by enzymatic activity tests, which showed that it belonged to the class EC 2.6.1.57. The first crystal structures of a psychrophilic aromatic amino-acid aminotransferase have been determined at resolutions of 2.19 Å for the native enzyme (PsyArAT) and 2.76 Å for its complex with aspartic acid (PsyArAT/D). Both types of crystals grew in the monoclinic space groupP21under slightly different crystallization conditions. ThePsyArAT crystals contained a dimer (90 kDa) in the asymmetric unit, which corresponds to the active form of this enzyme, whereas the crystals of thePsyArAT/D complex included four dimers showing different stages of the transamination reaction.
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Chessa, Jean-Pierre, Georges Feller, and Charles Gerday. "Purification and characterization of the heat-labile α-amylase secreted by the psychrophilic bacterium TAC 240B." Canadian Journal of Microbiology 45, no. 6 (July 15, 1999): 452–57. http://dx.doi.org/10.1139/w99-021.

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A total of 59 bacteria samples from Antarctic sea water were collected and screened for their ability to produce α-amylase. The highest activity was recorded from an isolate identified as an Alteromonas species. The purified α-amylase shows a molecular mass of about 50 000 Da and a pI of 5.2. The enzyme is stable from pH 7.5 to 9 and has a maximal activity at pH 7.5. Compared with other α-amylases from mesophiles and thermophiles, the "cold enzyme" displays a higher activity at low temperature and a lower stability at high temperature. The psychrophilic α-amylase requires both Cl-and Ca2+for its amylolytic activity. Br-is also quite effecient as an allosteric effector. The comparison of the amino acid composition with those of other α-amylases from various organisms shows that the cold α-amylase has the lowest content in Arg and Pro residues. This could be involved in the principle used by the psychrophilic enzyme to adapt its molecular structure to the low temperature of the environment. Key words: α-amylase, psychrophilic microorganisms, Antarctic.
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Benrezkallah, Djamila, Hayat Sediki, and Abdelghani Mohammed Krallafa. "The Structural Flexibility of Cold- and Warm-Adapted Enzymes (Endonucleases I) by Molecular Dynamics Simulation." Chemistry Proceedings 3, no. 1 (November 14, 2020): 128. http://dx.doi.org/10.3390/ecsoc-24-08387.

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The constraints exerted on the molecular edifices by different environmental parameters are not the same, which is translated by different adaptive strategies. Thus, for the extracellular and periplasmic enzymes of marine organisms which are directly exposed to environments in which large variations in temperature and salinity can occur, it is not an easy task to separate the adaptation of the enzyme to one of the two environmental parameters without the involvement of the other. In such a scenario, a comparative study of a marine psychrophilic and an estuarine mesophilic endonuclease I wasundertaken. The different salt optima of the enzymes were taken into consideration when the temperature-dependent enzymatic properties were characterized, but the results did not show an adaptive strategy at the molecular edifice. For that purpose, we employed multiple all-atom explicit solvent and ions molecular dynamics simulations, in conjunction with different temperatures at the nanosecond time scale to analyzethe structural flexibility of the cold adapted enzyme, endonuclease I psychrophile marine (VsEndA), and its mesophile homologous enzyme, endonuclease I mesophile estuarine (VcEndA). The Root Mean Square Fluctuation (RMSF) profiles of the two enzymes are almost similar with the most flexible residues located at the loop regions for both enzymes. We underlined a different trend against temperature for the two enzymes. The cold adapted enzyme was dominated by the lowest temperatures of T = 300 and T = 318 K, compared to its warm adapted homologous counterpart for which the highest temperature studiedwas T = 326 K as the dominantone. The lifetimes of the hydrogen bonding network of the most flexible residues of both enzymes correlate well with the RMSF of the considered enzymes.
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Dissertations / Theses on the topic "Psychrophilic enzyme"

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PASI, MARCO. "A dynamical perspective on cold-adapted enzymes at the molecolar level." Doctoral thesis, Università degli Studi di Milano-Bicocca, 2009. http://hdl.handle.net/10281/7729.

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Some organisms, especially unicellular, have adapted to extreme temperature conditions, and are capable of proliferating in such environments mainly thanks to the optimisation of their enzymatic repertoire. Cold-adapted (psychrophilic) enzymes are invariably characterised by high catalytic activity at low temperatures, necessary to endure the exponential reduction of the speed of chemical reactions in these conditions, and by low thermal stability. Numerous studies aimed at understanding the mechanisms of such adaptation at the molecular level agree that the high turnover observed for psychrophilic enzymes results from a decrease of the activation enthalpy of the catalysed reaction, which in turn is achieved structurally by decreasing the number and strength of the enthalpically stabilised interactions which must be broken to reach the transition state. Since these interactions are also involved in the stabilisation of the enzyme structure, their decrease has the effect of increasing structural flexibility, as reflected by the low thermal stability found for psychrophilic enzymes. Flexibility seems thus to have a fundamental role in enzymatic cold adaptation, and its study by means of Molecular Dynamics (MD) simulations provides a detailed description taking rigorously into account its dynamical character. I report the results of comparative MD studies performed on homologous mesophilic and psychrophilic enzymes, and mutants thereof, to investigate the molecular bases of cold adaptation. Long, multi-replica and explicit-solvent MD simulations have been compared in particular in terms of molecular flexibility and the dynamics of intramolecular interactions. Results show that differences in the dynamic character of the compared enzymes are found in loops surrounding the active site or substrate-binding cleft. In the case of chloride-dependent alpha-amylases, the comparison of the cold-active enzyme from Pseudoalteromonas Haloplanktis with its mesophilic porcine homologue shows that modulation of the size and flexibility of these loops cause the immediate surroundings of the active site to be comparatively more flexible in the psychrophilic enzyme. Detailed analysis of these enzymes active-site dynamics reveals that elements previously identified through X-ray crystallography as involved in substrate binding in both enzymes undergo concerted motions that may be linked to catalysis. The comparison of psychrophilic and mesophilic isoforms of trypsin from Salmo Salar shows that the cold-adapted enzyme presents fewer interdomain interactions and enhanced localised flexibility in regions close to the catalytic site. Notably, these regions fit well with the pattern of protein flexibility previously reported for psychrophilic elastases. These results indicate that specific sites within the serine-protease fold can be considered hot spots of cold-adaptation and that psychrophilic trypsins and elastases have independently discovered similar molecular strategies to optimise flexibility at low temperatures. This evidence of evolutionary convergence underlines the importance of extending intrafamiliar comparative studies to unveil general features of how enzymes adapt their dynamical properties low temperatures. Molecular dynamics studies using all-atomic models, as those presented herein, have proven their effectiveness in this context, but their computational requirement hampers their applicability as the size of the test set increases. For these reasons it would be relevant to devise a simplified ("coarse-grain") approach to perform comparative analyses at a higher throughput than is currently feasible. To evaluate the level of simplification most suitable for this application, a "coarse-grain" approach has been adopted to study the mechanical properties of trypsins, taking into account results obtained using all-atomic models. The results of these comparisons are driving the development of a multi-scale "coarse-grain" approach that combines the required efficiency and accuracy.
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De, Wijn Raphaël. "Application des nouvelles approches de cristallisation et de cristallographie sérielle à l’étude structurale de complexes enzymes : ARNt." Thesis, Strasbourg, 2018. http://www.theses.fr/2018STRAJ095/document.

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Cette thèse porte sur deux aspects complémentaires, le développement et l’implémentation de nouvelles approches de cristallisation et de cristallographie sérielle ainsi que leur mise en œuvre dans l’étude structurale de complexes enzymes : ARNt. La cristallographie est la méthode la plus employée en biologie structurale, mais elle présente encore des points délicats. Plusieurs méthodes avancées ont été déployées dans ce travail pour y pallier qui ont conduit à la résolution de la structure de l’ARNt nucléotidyltransférase du psychrophile Planococcus halocryophilus et à l’étude de son adaptation structurale au froid ; des puces microfluidiques de cristallisation qui ont servi à la résolution de plusieurs structures à température ambiante par cristallographie sérielle ; enfin le Xtal Controller utilisé pour l’étude d’évènements de nucléation et de croissance cristalline dans un but de préparation d’échantillons pour analyse sous rayonnement XFEL. Entre autres systèmes biologiques, cette thèse présente la caractérisation de deux familles d’inhibiteurs visant les aspartyl-ARNt synthétases, notamment du pathogène Pseudomonas aeruginosa
This thesis focuses on two complementary aspects, the development and implementation of new approaches of crystallization and of serial crystallography as well as their use in the structural study of enzymes/tRNA complexes. Crystallography is the most used method in structural biology, but it presents delicate points. Different methods were implemented in this work to overcome these points, which led to the resolution of the structure of the CCA-adding enzyme of the psychrophilic organism Planococcus halocryophilus and to the study of its structural adaptation to the cold; novel microfluidic crystallization chips that have been used for the resolution of several structures by serial crystallography at room-temperature; finally the Xtal Controller used for the study of nucleation and crystal growth events with the purpose of preparing samples for analysis under XFEL radiation. Among other biological systems, this thesis presents the study and characterization of two families of inhibitors targeting aspartyl-tRNA synthetases, including the one of the pathogenic organism Pseudomonas aeruginosa
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Van, Truong Le. "Characterization of the pectinolytic enzymes of the marine psychrophilic bacterium Pseudoalteromonas haloplanktis strain ANT-505." [S.l.] : [s.n.], 2006. http://deposit.ddb.de/cgi-bin/dokserv?idn=984430180.

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Violot, Sébastien. "Etudes fonctionnelles et structurales de la protéine EED, partenaire cellulaire du virus VIH-1 et de la cellulase « froide » Cel5G de Pseudoalteromonas haloplanktis." Phd thesis, Université Claude Bernard - Lyon I, 2005. http://tel.archives-ouvertes.fr/tel-00091916.

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La protéine humaine EED appartient à la famille des «Polycomb». Elle intervient dans la régulation génique. Elle jouerait aussi un rôle dans le cycle du virus de l'immunodéficience humaine (VIH-1) en participant au transport du complexe de préintégration et en facilitant la réaction d'intégration. EED a été surproduite afin d'être cristallisée seule et en complexe avec les protéines virales IN, MA et Nef. Un modèle de EED a été construit par homologie structurale. D'après nos expériences de « phage display », les régions susceptibles d'interagir avec les partenaires viraux se situent sur des boucles de ce modèle.
La bactérie psychrophile P. haloplanktis produit la cellulase Cel5G. Les structures de cette cellulase seule et en complexe avec le cellobiose, ont été déterminées à haute résolution par remplacement moléculaire. La cellulase Cel5A de la bactérie mésophile E. chrysanthemi a été utilisée comme modèle. Nos résultats permettent de mieux comprendre les déterminants structuraux responsables de l'adaptation des enzymes aux basses températures.
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[Verfasser], Le-Van-Truong. "Characterization of the pectinolytic enzymes of the marine psychrophilic bacterium Pseudoalteromonas haloplanktis strain ANT-505 / vorgelegt von Le Van Truong." 2006. http://d-nb.info/984430180/34.

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Books on the topic "Psychrophilic enzyme"

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Amthor, Kerstin. The activity of extracellular enzymes in starved and unstarved cells of a psychrophilic marine vibrio. 1989.

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Book chapters on the topic "Psychrophilic enzyme"

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Tutino, M. L., L. Birolo, B. Fontanella, K. Mainolfi, F. Vinci, G. Sannia, and G. Marino. "Aspartate aminotransferase from Moraxella TAC125: an unusual psychrophilic enzyme." In Cold-Adapted Organisms, 305–16. Berlin, Heidelberg: Springer Berlin Heidelberg, 1999. http://dx.doi.org/10.1007/978-3-662-06285-2_17.

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Collins, Tony, and Charles Gerday. "Enzyme Catalysis in Psychrophiles." In Psychrophiles: From Biodiversity to Biotechnology, 209–35. Cham: Springer International Publishing, 2017. http://dx.doi.org/10.1007/978-3-319-57057-0_10.

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D'amico, Salvino, Daphné Georlette, Tony Collins, Georges Feller, and Charles Gerday. "Microcalorimetry as Applied to Psychrophilic Enzymes." In Biocalorimetry 2, 231–40. Chichester, UK: John Wiley & Sons, Ltd, 2005. http://dx.doi.org/10.1002/0470011122.ch13.

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Roulling, Frédéric, Florence Piette, Alexandre Cipolla, Caroline Struvay, and Georges Feller. "Psychrophilic Enzymes: Cool Responses to Chilly Problems." In Extremophiles Handbook, 891–913. Tokyo: Springer Japan, 2011. http://dx.doi.org/10.1007/978-4-431-53898-1_43.

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Collins, Tony, Frédéric Roulling, Florence Piette, Jean-Claude Marx, Georges Feller, Charles Gerday, and Salvino D'Amico. "Fundamentals of Cold-Adapted Enzymes." In Psychrophiles: from Biodiversity to Biotechnology, 211–27. Berlin, Heidelberg: Springer Berlin Heidelberg, 2008. http://dx.doi.org/10.1007/978-3-540-74335-4_13.

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Barroca, Mário, Gustavo Santos, Charles Gerday, and Tony Collins. "Biotechnological Aspects of Cold-Active Enzymes." In Psychrophiles: From Biodiversity to Biotechnology, 461–75. Cham: Springer International Publishing, 2017. http://dx.doi.org/10.1007/978-3-319-57057-0_19.

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Huston, Adrienne L. "Biotechnological Aspects of Cold-Adapted Enzymes." In Psychrophiles: from Biodiversity to Biotechnology, 347–63. Berlin, Heidelberg: Springer Berlin Heidelberg, 2008. http://dx.doi.org/10.1007/978-3-540-74335-4_20.

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Arpigny, J. L., G. Feller, S. Davail, S. Génicot, E. Narinx, Z. Zekhnini, and Ch Gerday. "Molecular Adaptations of Enzymes from Thermophilic and Psychrophilic Organisms." In Advances in Comparative and Environmental Physiology, 269–95. Berlin, Heidelberg: Springer Berlin Heidelberg, 1994. http://dx.doi.org/10.1007/978-3-642-78598-6_6.

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Siddiqui, Khawar Sohail, Ahsan Mushir Shemsi, Gea Guerriero, Tahria Najnin, Taha, and Haluk Ertan. "Biotechnological Improvements of Cold-Adapted Enzymes: Commercialization via an Integrated Approach." In Psychrophiles: From Biodiversity to Biotechnology, 477–512. Cham: Springer International Publishing, 2017. http://dx.doi.org/10.1007/978-3-319-57057-0_20.

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Papaleo, Elena, Matteo Tiberti, and Gaetano Invernizzi. "Molecular Dynamics Simulations to Study Structure-Function Relationship in Psychrophilic Enzymes." In Biotechnology of Extremophiles:, 675–98. Cham: Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-13521-2_24.

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