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Relevant bibliographies by topics / Allosteric enzymes

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Academic literature on the topic 'Allosteric enzymes'

Author: Grafiati

Published: 4 June 2021

Last updated: 27 July 2024

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Journal articles on the topic "Allosteric enzymes"

1

Jiao, Wanting. "Computational investigations of allostery in aromatic amino acid biosynthetic enzymes." Biochemical Society Transactions 49, no. 1 (2021): 415–29. http://dx.doi.org/10.1042/bst20200741.

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Allostery, in which binding of ligands to remote sites causes a functional change in the active sites, is a fascinating phenomenon observed in enzymes. Allostery can occur either with or without significant conformational changes in the enzymes, and the molecular basis of its mechanism can be difficult to decipher using only experimental techniques. Computational tools for analyzing enzyme sequences, structures, and dynamics can provide insights into the allosteric mechanism at the atomic level. Combining computational and experimental methods offers a powerful strategy for the study of enzyme

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Kuznetsov, Aleksei, and Jaak Järv. "Ligand structure controlled allostery in cAMP-dependent protein kinase catalytic subunit." Open Life Sciences 4, no. 2 (2009): 131–41. http://dx.doi.org/10.2478/s11535-009-0012-6.

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AbstractProtein kinase A (cAMP dependent protein kinase catalytic subunit, EC 2.7.11.11) binds simultaneously ATP and a phosphorylatable peptide. These structurally dissimilar allosteric ligands influence the binding effectiveness of each other. The same situation is observed with substrate congeners, which reversibly inhibit the enzyme. In this review these allosteric effects are quantified using the interaction factor, which compares binding effectiveness of ligands with the free enzyme and the pre-loaded enzyme complex containing another ligand. This analysis revealed that the allosteric ef

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Jiao, Wanting, Yifei Fan, Nicola J. Blackmore, and Emily J. Parker. "A single amino acid substitution uncouples catalysis and allostery in an essential biosynthetic enzyme in Mycobacterium tuberculosis." Journal of Biological Chemistry 295, no. 19 (2020): 6252–62. http://dx.doi.org/10.1074/jbc.ra120.012605.

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Allostery exploits the conformational dynamics of enzymes by triggering a shift in population ensembles toward functionally distinct conformational or dynamic states. Allostery extensively regulates the activities of key enzymes within biosynthetic pathways to meet metabolic demand for their end products. Here, we have examined a critical enzyme, 3-deoxy-d-arabino-heptulosonate 7-phosphate synthase (DAH7PS), at the gateway to aromatic amino acid biosynthesis in Mycobacterium tuberculosis, which shows extremely complex dynamic allostery: three distinct aromatic amino acids jointly communicate o

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Akimoto, Madoka, Karla Martinez Pomier, Bryan VanSchouwen, Jung Ah Byun, Mariia Khamina, and Giuseppe Melacini. "Allosteric pluripotency: challenges and opportunities." Biochemical Journal 479, no. 7 (2022): 825–38. http://dx.doi.org/10.1042/bcj20210528.

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Allosteric pluripotency arises when the functional response of an allosteric receptor to an allosteric stimulus depends on additional allosteric modulators. Here, we discuss allosteric pluripotency as observed in the prototypical Protein Kinase A (PKA) as well as in other signaling systems, from typical multidomain signaling proteins to bacterial enzymes. We identify key drivers of pluripotent allostery and illustrate how hypothesizing allosteric pluripotency may solve apparent discrepancies currently present in the literature regarding the dual nature of known allosteric modulators. We also o

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Helmstaedt, Kerstin, Sven Krappmann, and Gerhard H. Braus. "Allosteric Regulation of Catalytic Activity:Escherichia coli Aspartate Transcarbamoylase versus Yeast Chorismate Mutase." Microbiology and Molecular Biology Reviews 65, no. 3 (2001): 404–21. http://dx.doi.org/10.1128/mmbr.65.3.404-421.2001.

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SUMMARY Allosteric regulation of key metabolic enzymes is a fascinating field to study the structure-function relationship of induced conformational changes of proteins. In this review we compare the principles of allosteric transitions of the complex classical model aspartate transcarbamoylase (ATCase) from Escherichia coli, consisting of 12 polypeptides, and the less complicated chorismate mutase derived from baker's yeast, which functions as a homodimer. Chorismate mutase presumably represents the minimal oligomerization state of a cooperative enzyme which still can be either activated or i

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Suplatov, D. А., and V. К. Švedas. "Study of Functional and Allosteric Sites in Protein Superfamilies." Acta Naturae 7, no. 4 (2015): 34–45. http://dx.doi.org/10.32607/20758251-2015-7-4-34-45.

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The interaction of proteins (enzymes) with a variety of low-molecular-weight compounds, as well as protein-protein interactions, is the most important factor in the regulation of their functional properties. To date, research effort has routinely focused on studying ligand binding to the functional sites of proteins (active sites of enzymes), whereas the molecular mechanisms of allosteric regulation, as well as binding to other pockets and cavities in protein structures, remained poorly understood. Recent studies have shown that allostery may be an intrinsic property of virtually all proteins.

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Zlobin, A. S., D. А. Suplatov, K. Е. Kopylov, and V. К. Švedas. "CASBench: A Benchmarking Set of Proteins with Annotated Catalytic and Allosteric Sites in Their Structures." Acta Naturae 11, no. 1 (2019): 74–80. http://dx.doi.org/10.32607/20758251-2019-11-1-74-80.

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In recent years, the phenomenon of allostery has witnessed growing attention driven by a fundamental interest in new ways to regulate the functional properties of proteins, as well as the prospects of using allosteric sites as targets to design novel drugs with lower toxicity due to a higher selectivity of binding and specificity of the mechanism of action. The currently available bioinformatic methods can sometimes correctly detect previously unknown ligand binding sites in protein structures. However, the development of universal and more efficient approaches requires a deeper understanding

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Kneuttinger, Andrea C., Stefanie Zwisele, Kristina Straub, et al. "Light-Regulation of Tryptophan Synthase by Combining Protein Design and Enzymology." International Journal of Molecular Sciences 20, no. 20 (2019): 5106. http://dx.doi.org/10.3390/ijms20205106.

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The spatiotemporal control of enzymes by light is of growing importance for industrial biocatalysis. Within this context, the photo-control of allosteric interactions in enzyme complexes, common to practically all metabolic pathways, is particularly relevant. A prominent example of a metabolic complex with a high application potential is tryptophan synthase from Salmonella typhimurium (TS), in which the constituting TrpA and TrpB subunits mutually stimulate each other via a sophisticated allosteric network. To control TS allostery with light, we incorporated the unnatural amino acid o-nitroben

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Chen, Zhen, Weiqian Meyer, Sugima Rappert, Jibin Sun, and An-Ping Zeng. "Coevolutionary Analysis Enabled Rational Deregulation of Allosteric Enzyme Inhibition in Corynebacterium glutamicum for Lysine Production." Applied and Environmental Microbiology 77, no. 13 (2011): 4352–60. http://dx.doi.org/10.1128/aem.02912-10.

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ABSTRACTProduct feedback inhibition of allosteric enzymes is an essential issue for the development of highly efficient microbial strains for bioproduction. Here we used aspartokinase fromCorynebacterium glutamicum(CgAK), a key enzyme controlling the biosynthesis of industrially important aspartate family amino acids, as a model to demonstrate a fast and efficient approach to the deregulation of allostery. In the last 50 years many researchers and companies have made considerable efforts to deregulate this enzyme from allosteric inhibition by lysine and threonine. However, only a limited numbe

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Verevka, Serhij. "ALLOSTERIC SITE OF SERINE PROTEINASES: LOCALIZATION, FUNCTIONAL ROLE AND MANIFESTATIONS IN VITRO." Grail of Science, no. 12-13 (May 25, 2022): 188–97. http://dx.doi.org/10.36074/grail-of-science.29.04.2022.029.

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The study of molecular mechanisms of regulation of biologically active molecules is a necessary condition for understanding the course of the processes mediated by them. Serine proteinases are a large group of enzymes that play a leading role in the regulation of numerous physiological and pathogenic processes. Like many enzymes, SP are allosteric ones. In addition to the active center, they contain the region, whose interaction with corresponding compound changes the activity of enzyme. Various compounds can act as allosteric effectors. They may be substrates, substrate-like compounds, and mi

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Dissertations / Theses on the topic "Allosteric enzymes"

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Marshall, Kristin Ann. "Group I aptazymes as genetic regulatory switches." Access restricted to users with UT Austin EID Full text (PDF) from UMI/Dissertation Abstracts International, 2001. http://wwwlib.umi.com/cr/utexas/fullcit?p3034980.

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María, Solano Miguel Ángel. "Computational studies of the conformational landscape of allosteric and enantioselective enzymes." Doctoral thesis, Universitat de Girona, 2021. http://hdl.handle.net/10803/671771.

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Enzymes are sophisticated biomacromolecules whose function is linked to its three-dimensional structure and conformational dynamics. Therefore, the understanding of enzyme conformational dynamics can be exploited to enhance enzyme efficiencies. First, we study alcohol dehydrogenase (ADH) enzymes in order to investigate the molecular basis of the reversion of enantioselectivity and thermo-adaptation displayed by laboratory-evolved enzyme variants towards non-natural substrates. In second place, we study the allosteric complex tryptophan synthase (TrpS) in order to decipher the allosteric

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Davies, Andrew. "Investigating the selectivity and mechanism of allosteric regulation in α-IPMS enzymes". Thesis, University of Canterbury. Department of Chemistry, 2015. http://hdl.handle.net/10092/10849.

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Enzymes are nature’s wizards: balanced delicately on the margin of order and entropy, they perform chemical reactions and syntheses at rates and yields human chemists can only dream of. Many possess exquisite control mechanisms to keep the flow of metabolites through our cells precisely regulated. This work explores the regulation mechanism of α-isopropylmalate synthase (α-IPMS). The branched-chain amino acid biosynthetic pathways in bacteria are of interest as novel antibiotic targets. α-IPMS catalyses the first committed step in the pathway to form leucine, an essential amino acid. It perfor

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Loftus, Katherine Marie. "Studies of the Structure and Function of E.coli Aspartate Transcarbamoylase." Thesis, Boston College, 2006. http://hdl.handle.net/2345/580.

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Thesis advisor: Evan R. Kantrowitz<br>E.coli Aspartate transcarbamoylase (ATCase) is the allosteric enzyme that catalyzes the committed step of the de novo pyrimidine biosynthesis pathway. ATCase facilitates the reaction between L-aspartate and carbamoyl phosphate to form N-carbamoyl-L-aspartate and inorganic phosphate. The holoenzyme is a dodecamer, consisting of two trimers of catalytic chains, and three dimers of regulatory chains. ATCase is regulated homotropically by its substrates, and heterotropically by the nucleotides ATP, CTP, and UTP. These nucleotides bind to the regulatory chains,

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Jurica, Melissa Sue. "I. Structures of intron encoded homing endonucleases ; and, II. Allosteric regulation of pyruvate kinase /." Thesis, Connect to this title online; UW restricted, 1999. http://hdl.handle.net/1773/5002.

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De, Zutter Julie Kelley. "Allosteric Regulation of Recombination Enzymes E. coli RecA and Human Rad51: A Dissertation." eScholarship@UMMS, 2000. https://escholarship.umassmed.edu/gsbs_diss/192.

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ATP plays a critical role in the regulation of many enzyme processes. In this work, I have focused on the ATP mediated regulation of the recombination processes catalyzed by the E. coliRecA and the human Rad51 proteins. The RecA protein is a multifunctional enzyme, which plays a central role in the processes of recombinational DNA repair, homologous genetic recombination and in the activation of the cellular SOS response to DNA damage. Each of these functions requires a common activating step, which is the formation of a RecA-ATP-ssDNA nucleoprotein filament. The binding of ATP results in the

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Pirrie, Lisa. "Development of novel active site and allosteric inhibitors of enzymes associated with cancer, neurodegenerative diseases and bacterial infections." Thesis, University of St Andrews, 2013. http://hdl.handle.net/10023/3471.

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The sirtuins are a family of NAD⁺-dependent deacetylase enzymes which are implicated in various illnesses including cancer and neurodegenerative diseases. Part I of this thesis describes the synthesis and biological evaluation of inhibitors of the SIRT1 and SIRT2 isoforms of this important family of enzymes. Chapter 1 gives an overview of sirtuin biology and the physiological roles of these enzymes. In particular the link between SIRT1 and cancer and SIRT2 and its role in the onset of neurodegenerative diseases is discussed. A review of the most potent and selective inhibitors of SIRT1 and SIR

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Liu, Xuying. "Structure and Regulation of Aspartate Pathway Enzymes and Deuteration Effects on Protein Structure." University of Toledo / OhioLINK, 2008. http://rave.ohiolink.edu/etdc/view?acc_num=toledo1207946924.

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Beuter, Dominik [Verfasser], and Hannes [Akademischer Betreuer] Link. "Construction of Enzymes with Synthetic Allosteric Regulation to Control Metabolic Pathways of Escherichia coli / Dominik Beuter ; Betreuer: Hannes Link." Marburg : Philipps-Universität Marburg, 2019. http://d-nb.info/1193177480/34.

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Verespy, Stephen S. III. "Probing Allosteric, Partial Inhibition of Thrombin Using Novel Anticoagulants." VCU Scholars Compass, 2016. http://scholarscompass.vcu.edu/etd/4431.

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Thrombin is the key protease that regulates hemostasis; the delicate balance between procoagulation and anticoagulation of blood. In clotting disorders, like deep vein thrombosis or pulmonary embolism, procoagulation is up-regulated, but propagation of clotting can be inhibited with drugs targeting the proteases involved, like thrombin. Such drugs however, have serious side effects (e.g., excessive bleeding) and some require monitoring during the course of treatment. The reason for these side effects is the mechanism by which the drugs’ act. The two major mechanisms are direct orthosteric and

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Books on the topic "Allosteric enzymes"

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Traut, Thomas. Allosteric Regulatory Enzymes. Springer US, 2008. http://dx.doi.org/10.1007/978-0-387-72891-9.

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Centro linceo interdisciplinare "Beniamino Segre.", Università degli studi di Roma "La Sapienza." Dipartimento di scienze biochimiche., and Instituto di biologia e patologia molecolari (Italy), eds. Allosteric proteins: 40 years with Monod-Wyman-Changeux : convegno internazionale : Roma, 24 maggio 2005. Accademia nazionale dei Lincei, 2006.

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Perutz, Max F. Mechanisms of cooperativity and allosteric regulation in proteins. Cambridge University Press, 1990.

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Energetics of biological macromolecules. Elsevier/Academic Press, 2004.

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1947-, Johnson Michael L., and Ackers Gary K, eds. Energetics of biological macromolecules. Academic Press, 2000.

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Allosteric enzymes. CRC Press, 1989.

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Herve, Guy. Allosteric Enzymes. Taylor & Francis Group, 2020.

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Herve, Guy. Allosteric Enzymes. Taylor & Francis Group, 2020.

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Herve, Guy. Allosteric Enzymes. Taylor & Francis Group, 2020.

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Herve, Guy. Allosteric Enzymes. Taylor & Francis Group, 2020.

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Book chapters on the topic "Allosteric enzymes"

1

Cohen, G. N. "Allosteric Enzymes." In Microbial Biochemistry. Springer Netherlands, 2010. http://dx.doi.org/10.1007/978-90-481-9437-7_5.

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Cohen, G. N. "Allosteric Enzymes." In Microbial Biochemistry. Springer Netherlands, 2014. http://dx.doi.org/10.1007/978-94-017-8908-0_5.

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Cohen, Georges N. "Allosteric Enzymes." In Microbial Biochemistry. Springer Netherlands, 2016. http://dx.doi.org/10.1007/978-94-017-7579-3_5.

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Cohen, Georges N. "Allosteric Enzymes." In Microbial Biochemistry. Springer Netherlands, 2004. http://dx.doi.org/10.1007/978-1-4020-2237-1_5.

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Lim, Wendell A., and Bruce J. Mayer. "Signaling Enzymes and Their Allosteric Regulation." In Cell Signaling, 2nd edition, 2nd ed. CRC Press, 2024. http://dx.doi.org/10.1201/9780429298844-3.

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Shafferman, A., A. Ordentlich, D. Barak, et al. "Molecular Aspects of Catalysis and of Allosteric Regulation of Aceytlcholinesterases." In Enzymes of the Cholinesterase Family. Springer US, 1995. http://dx.doi.org/10.1007/978-1-4899-1051-6_38.

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Daily, Michael D., Haibo Yu, George N. Phillips, and Qiang Cui. "Allosteric Activation Transitions in Enzymes and Biomolecular Motors: Insights from Atomistic and Coarse-Grained Simulations." In Dynamics in Enzyme Catalysis. Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/128_2012_409.

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Reinhart, Gregory D. "Continuing Inspiration: Gregorio Weber’s Influence on Understanding the Basis of Allosteric Regulation of Enzymes." In Perspectives on Fluorescence. Springer International Publishing, 2016. http://dx.doi.org/10.1007/4243_2016_20.

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Schafer, James R. A., David A. Fell, Douglas L. Rothman, and Robert G. Shulman. "Phosphorylation of Allosteric Enzymes Can Serve Homeostasis rather than Control Flux: The Example of Glycogen Synthase." In Metabolomics by In Vivo NMR. John Wiley & Sons, Ltd, 2005. http://dx.doi.org/10.1002/0470011505.ch5.

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Stadtman, E. R. "Allosteric Regulation of Enzyme Activity." In Advances in Enzymology - and Related Areas of Molecular Biology. John Wiley & Sons, Inc., 2006. http://dx.doi.org/10.1002/9780470122730.ch2.

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Conference papers on the topic "Allosteric enzymes"

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Zhuravlev, A. M., V. V. Aksenov, V. N. Gavrilyuk, A. B. Golovanov, and I. V. Ivanov. "ALLOSTERIC INHIBITORS OF ALOX15 BASED ON LIGANDS PROVIDING MULTIDIRECTIONAL REGULATION OF LINOLEIC AND ARACHIDONIC ACIDS." In X Международная конференция молодых ученых: биоинформатиков, биотехнологов, биофизиков, вирусологов и молекулярных биологов — 2023. Novosibirsk State University, 2023. http://dx.doi.org/10.25205/978-5-4437-1526-1-76.

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Mammalian 15-lipoxygenases (ALOX15) are enzymes of lipid peroxidation. The pathophysiological role of ALOX15 metabolites, linoleic acid and arachidonic acid derivatives, has made this enzyme a target for pharmacological studies. Several indole and benzimidazole derivatives inhibit the activity of ALOX15 in a substrate-specific manner, but the molecular basis of this allosteric inhibition remains unclear.

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Najdi, T. S., C. R. Yang, B. E. Shapiro, G. W. Hatfield, and B. E. Mjolsness. "Application of a generalized MWC model for the mathematical simulation of metabolic pathways regulated by allosteric enzymes." In 2005 IEEE Computational Systems Bioinformatics Conference (CSB'05). IEEE, 2005. http://dx.doi.org/10.1109/csb.2005.15.

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Gabrielli, Ângelo, Camila Sousa Bragunce Alves, Bruna Oliveira Bicalho, and Débora Pimenta Alves. "Benefits and Challenges of Cannabis Use in the Treatment of Refractory Epilepsy." In XIII Congresso Paulista de Neurologia. Zeppelini Editorial e Comunicação, 2021. http://dx.doi.org/10.5327/1516-3180.239.

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Introduction: Refractory epilepsy (RE) is a disease that causes continuous and debilitating seizures. Due to the ineffectiveness of antiepileptic therapies, there is a growing interest in drugs made with cannabidiol (CBD), a substance extracted from Cannabis. Objective: To point out benefits and challenges of the use of CBD in the treatment of RE. Methods: Literature review performed at PubMed, with the descriptors Epilepsy, Drug Therapy and Cannabis. Results: It is suggested that CBD is mediated by cannabinoid receptors coupled to protein G, by blockade of NMDA receptors, by GABAergic modulat

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Nowis, Dominika, Justyna Chlebowska, Pawel Gaj, et al. "Abstract 5347: SK053, a small molecule inhibitor of enzymes involved in allosteric disulfide bonds formation, shows potent anti-leukemic effects and induces differentiation of human AML cells." In Proceedings: AACR 106th Annual Meeting 2015; April 18-22, 2015; Philadelphia, PA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-7445.am2015-5347.

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Causa, F., Michele Costato, Marziale Milani, and Lorenzo Bolognani. "Allosteric ATPase behavior: the onset of laser-sustained enzyme cooperation." In Laser Applications in Life Sciences: 5th International Conference, edited by Pavel A. Apanasevich, Nikolai I. Koroteev, Sergei G. Kruglik, and Victor N. Zadkov. SPIE, 1995. http://dx.doi.org/10.1117/12.197473.

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Causa, F., Michele Costato, Marziale Milani, and A. Pozzi. "Allosteric enzyme behavior: the onset of oscillations EM field sustained." In Photonics West '95, edited by Steven L. Jacques. SPIE, 1995. http://dx.doi.org/10.1117/12.209923.

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Lyu, Zongyang, Lingmin Yuan, Katelyn M. Williams, James H. Atkison, and Shaun K. Olsen. "Abstract 4435: Molecular mechanism of a novel covalent allosteric inhibitor of SUMO E1 activating enzyme." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.sabcs18-4435.

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Lyu, Zongyang, Lingmin Yuan, Katelyn M. Williams, James H. Atkison, and Shaun K. Olsen. "Abstract 4435: Molecular mechanism of a novel covalent allosteric inhibitor of SUMO E1 activating enzyme." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.am2019-4435.

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