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Relevant bibliographies by topics / And enzyme kinetics

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Academic literature on the topic 'And enzyme kinetics'

Author: Grafiati

Published: 4 June 2021

Last updated: 7 February 2022

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Journal articles on the topic "And enzyme kinetics"

1

Moe, Owen, and Richard Cornelius. "Enzyme kinetics." Journal of Chemical Education 65, no. 2 (February 1988): 137. http://dx.doi.org/10.1021/ed065p137.

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WAGG, JONATHAN, and PETER H. SELLERS. "Enzyme Kinetics." Annals of the New York Academy of Sciences 779, no. 1 (April 1996): 272–78. http://dx.doi.org/10.1111/j.1749-6632.1996.tb44793.x.

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Herries, D. G. "Enzyme Kinetics." Biochemical Education 16, no. 3 (July 1988): 179–80. http://dx.doi.org/10.1016/0307-4412(88)90207-5.

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H.B.F.D. "Enzyme kinetics." Trends in Biochemical Sciences 13, no. 10 (October 1988): 411. http://dx.doi.org/10.1016/0968-0004(88)90200-9.

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Lloyd, Matthew D. "Steady-state enzyme kinetics." Biochemist 43, no. 3 (May 10, 2021): 40–45. http://dx.doi.org/10.1042/bio_2020_109.

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Steady-state enzyme kinetics is a cornerstone technique of biochemistry and related sciences since it allows the characterization and quantification of enzyme behaviour. Enzyme kinetics is widely used to investigate the physiological role of enzymes, determine the effects of mutations and characterize enzyme inhibitors. Well-known examples of enzyme inhibitors used to treat diseases include anti-infectives (e.g., penicillin, clavulanic acid and HIV protease inhibitors); anti-inflammatories (e.g., aspirin and ibuprofen); cholesterol-lowering statins; tyrosine kinase inhibitors used to treat cancer; and Viagra. Commonly, new disease treatments are discovered by using enzyme kinetics to identify the few active compounds residing within a large compound collection (‘high-throughput screening’). The subject of enzyme kinetics is typically introduced to first-year undergraduates with a mathematical description of behaviour. This Beginners Guide will give a brief overview of experimental enzyme kinetics and the characterization of enzyme inhibitors. Colorimetric assays using a microtitre plate will be considered, although most principles also apply to other assays.

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Guerrieri, Antonio, Rosanna Ciriello, Giuliana Bianco, Francesca De Gennaro, and Silvio Frascaro. "Allosteric Enzyme-Based Biosensors—Kinetic Behaviours of Immobilised L-Lysine-α-Oxidase from Trichoderma viride: pH Influence and Allosteric Properties." Biosensors 10, no. 10 (October 17, 2020): 145. http://dx.doi.org/10.3390/bios10100145.

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The present study describes the kinetics of L-lysine-α-oxidase (LO) from Trichoderma viride immobilised by co-crosslinking onto the surface of a Pt electrode. The resulting amperometric biosensor was able to analyse L-lysine, thus permitting a simple but thorough study of the kinetics of the immobilised enzyme. The kinetic study evidenced that LO behaves in an allosteric fashion and that cooperativity is strongly pH-dependent. Not less important, experimental evidence shows that cooperativity is also dependent on substrate concentration at high pH and behaves as predicted by the Monod-Wyman-Changeux model for allosteric enzymes. According to this model, the existence of two different conformational states of the enzyme was postulated, which differ in Lys species landing on LO to form the enzyme–substrate complex. Considerations about the influence of the peculiar LO kinetics on biosensor operations and extracorporeal reactor devices will be discussed as well. Not less important, the present study also shows the effectiveness of using immobilised enzymes and amperometric biosensors not only for substrate analysis, but also as a convenient tool for enzyme kinetic studies.

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Markin, C. J., D. A. Mokhtari, F. Sunden, M. J. Appel, E. Akiva, S. A. Longwell, C. Sabatti, D. Herschlag, and P. M. Fordyce. "Revealing enzyme functional architecture via high-throughput microfluidic enzyme kinetics." Science 373, no. 6553 (July 22, 2021): eabf8761. http://dx.doi.org/10.1126/science.abf8761.

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Systematic and extensive investigation of enzymes is needed to understand their extraordinary efficiency and meet current challenges in medicine and engineering. We present HT-MEK (High-Throughput Microfluidic Enzyme Kinetics), a microfluidic platform for high-throughput expression, purification, and characterization of more than 1500 enzyme variants per experiment. For 1036 mutants of the alkaline phosphatase PafA (phosphate-irrepressible alkaline phosphatase of Flavobacterium), we performed more than 670,000 reactions and determined more than 5000 kinetic and physical constants for multiple substrates and inhibitors. We uncovered extensive kinetic partitioning to a misfolded state and isolated catalytic effects, revealing spatially contiguous regions of residues linked to particular aspects of function. Regions included active-site proximal residues but extended to the enzyme surface, providing a map of underlying architecture not possible to derive from existing approaches. HT-MEK has applications that range from understanding molecular mechanisms to medicine, engineering, and design.

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Chisti, Yusuf. "Understanding enzyme kinetics." Biotechnology Advances 20, no. 5-6 (December 2002): 425–26. http://dx.doi.org/10.1016/s0734-9750(02)00028-9.

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Gutfreund, H. "Basic enzyme kinetics." FEBS Letters 212, no. 1 (February 9, 1987): 178. http://dx.doi.org/10.1016/0014-5793(87)81582-x.

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Louisot, P. "Basic enzyme kinetics." Biochimie 69, no. 5 (May 1987): 556–57. http://dx.doi.org/10.1016/0300-9084(87)90099-x.

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Dissertations / Theses on the topic "And enzyme kinetics"

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Zaman, Flora. "Kinetics of enzyme models." Thesis, University of Kent, 1998. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.263701.

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Qian, Yuhui. "Study of Basic Wood Decay Mechanisms and Their Biotechnological Applications." Fogler Library, University of Maine, 2008. http://www.library.umaine.edu/theses/pdf/QianY2008.pdf.

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Moore, Robert Goodwin Douglas C. "Towards the understanding of complex biochemical systems the significance of global protein structure and thorough parametric analysis /." Auburn, Ala, 2009. http://hdl.handle.net/10415/1766.

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Astier, Yann. "Enzyme kinetics and electrochemical polymer transistor detection of enzyme reactions." Thesis, University of Southampton, 2001. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.273800.

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Ekici, Özlem Doğan. "Design, synthesis, and evaluation of novel irreversible inhibitors for caspases." Available online, Georgia Institute of Technology, 2004:, 2003. http://etd.gatech.edu/theses/available/etd-04062004-164633/unrestricted/ekici%5Fozlem%5Fd%5F200312%5Fphd.pdf.

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Ekici, Ozlem Dogan. "Design, synthesis, and evaluation of novel irreversible inhibitors for caspases." Diss., Georgia Institute of Technology, 2003. http://hdl.handle.net/1853/5333.

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Kakkar, Tarundeep Singh. "Theoretical studies on enzyme inhibition kinetics." Diss., The University of Arizona, 1999. http://hdl.handle.net/10150/289017.

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Enzyme inhibition studies are conducted to characterize enzymes and to examine drug-drug interactions. To characterize the inhibitory process (competitive, non-competitive and uncompetitive) and to determine the inhibitory constant (Kᵢ), data analysis techniques (e.g., Dixon, Lineweaver-Burk, etc.) are used to linearize the inherently non-linear rate of substrate metabolism vs. substrate concentration data. These techniques were developed before the general use of computers. However, many investigators still rely on these techniques in spite of the easy availability of non-linear regression fitting programs. In Chapter 2, three methods (simultaneous nonlinear regression fit (SNLR); Dixon; non-simultaneous, nonlinear fit [K(m,app)]) were compared for estimating Ki from simulated data sets generated from a competitive inhibition model equation with 10% CV added random error to the data values. Of the three methods, the SNLR method was found to be the most robust, the fastest and easiest to implement. The K(m,app) method also gave good estimates but was more time-consuming. The Dixon method failed to give accurate and precise estimates of Kᵢ. The purpose of the study in Chapter 3 was to examine the minimal experimental design needed to obtain reliable and robust estimates of Kᵢ (as well as V(max) and K(m)). Four cases were examined. In the experimental design that relied upon the least amount of data, a control data set was fit simultaneously with one of the substrate-inhibitor pairs (25-10 or 250-100 μM). A total of 4 rate values were analyzed per fit (i.e., 3 control + 1 inhibitor value). A total of 100 data sets were fit per substrate-inhibitor pair. The preceding was repeated for a random error of 20 %CV. Thus, the total number of experiments was reduced from 108 (in Chapter 2) to 12 (in Chapter 3) (Case IV). Good estimates of the enzyme kinetic parameters were obtained. In Chapter 4, the ability of the SNLR method to identify the correct mechanism of inhibition was evaluated; competitive or noncompetitive enzyme-inhibition. Two experimental designs were examined ("conventional, non-optimal" and "semi-minimal"). The semi-minimal design was successful in discriminating between the two enzyme-inhibition mechanisms even for data with 30 %CV added random error.

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Bayram, Mustafa. "Computer algebra approaches to enzyme kinetics." Thesis, University of Bath, 1993. https://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.357810.

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Epstein, Todd Matthew. "Structural and kinetic studies of two enzymes catalyzing phospholipase A2 activity." Access to citation, abstract and download form provided by ProQuest Information and Learning Company; downloadable PDF file 2.39 Mb., 186 p, 2006. http://gateway.proquest.com/openurl?url_ver=Z39.88-2004&res_dat=xri:pqdiss&rft_val_fmt=info:ofi/fmt:kev:mtx:dissertation&rft_dat=xri:pqdiss:3200538.

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Tenney, Joel David. "The kinetics of the chlorine dioxide generation reaction." Thesis, Georgia Institute of Technology, 1988. http://hdl.handle.net/1853/10020.

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Books on the topic "And enzyme kinetics"

1

Cornish-Bowden, Athel. Enzyme kinetics. Oxford: IRL Press, 1988.

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Bisswanger, Hans. Enzyme Kinetics. Weinheim, Germany: Wiley-VCH Verlag GmbH & Co. KGaA, 2017. http://dx.doi.org/10.1002/9783527806461.

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Alberty, Robert A. Enzyme Kinetics. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2011. http://dx.doi.org/10.1002/9780470940020.

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W, Wharton Christopher, ed. Enzyme kinetics. Oxford: IRL Press, 1988.

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5

Leskovac, Vladimir. Comprehensive enzyme kinetics. New York: Kluwer Academic/Plenum Pub., 2003.

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6

Keleti, T. Basic enzyme kinetics. Budapest: Akadémiai Kiadó, 1986.

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7

Enzyme kinetics: From diastase to multi-enzyme systems. Cambridge: Cambridge University Press, 1994.

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8

Kuby, Stephen Allen. Enzyme catalysis, kinetics, and substrate binding. Boca Raton: CRC Press, 1991.

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9

1930-, Cleland W. W., ed. Enzyme kinetics and mechanism. New York: Taylor & Francis Group, 2007.

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Enzyme kinetics and mechanisms. Dordrecht: Kluwer Academic Pub., 2002.

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Book chapters on the topic "And enzyme kinetics"

1

Bagshaw, Clive R. "Enzyme Kinetics." In Biomolecular Kinetics, 89–114. Boca Raton : Taylor & Francis/CRC Press, 2017. | Series: Foundations of biochemistry and biophysics |: CRC Press, 2017. http://dx.doi.org/10.1201/9781315120355-4.

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Liu, Weijiu. "Enzyme Kinetics." In Introduction to Modeling Biological Cellular Control Systems, 11–36. Milano: Springer Milan, 2012. http://dx.doi.org/10.1007/978-88-470-2490-8_2.

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Alberty, Robert A. "Enzyme Kinetics." In Advances in Enzymology - and Related Areas of Molecular Biology, 1–64. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2006. http://dx.doi.org/10.1002/9780470122624.ch1.

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Gardner, Aaron, Wilko Duprez, Sarah Stauffer, Dewi Ayu Kencana Ungu, and Frederik Clauson-Kaas. "Enzyme Kinetics." In Labster Virtual Lab Experiments: Basic Biochemistry, 57–87. Berlin, Heidelberg: Springer Berlin Heidelberg, 2019. http://dx.doi.org/10.1007/978-3-662-58499-6_4.

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Fromm, Herbert J., and Mark S. Hargrove. "Enzyme Kinetics." In Essentials of Biochemistry, 81–122. Berlin, Heidelberg: Springer Berlin Heidelberg, 2011. http://dx.doi.org/10.1007/978-3-642-19624-9_5.

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Prinz, Heino. "Enzyme Kinetics." In Numerical Methods for the Life Scientist, 97–118. Berlin, Heidelberg: Springer Berlin Heidelberg, 2011. http://dx.doi.org/10.1007/978-3-642-20820-1_7.

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Smith, C. A., and E. J. Wood. "Enzyme kinetics." In Biological Molecules, 83–104. Dordrecht: Springer Netherlands, 1991. http://dx.doi.org/10.1007/978-94-011-3126-1_4.

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Mc Auley, Mark Tomás. "Enzyme Kinetics." In Computer Modelling for Nutritionists, 31–40. Cham: Springer International Publishing, 2019. http://dx.doi.org/10.1007/978-3-319-39994-2_3.

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De Blasio, Cataldo. "Enzyme Kinetics." In Fundamentals of Biofuels Engineering and Technology, 209–20. Cham: Springer International Publishing, 2019. http://dx.doi.org/10.1007/978-3-030-11599-9_15.

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Dutta, Rajiv. "Enzyme Kinetics." In Fundamentals of Biochemical Engineering, 8–49. Berlin, Heidelberg: Springer Berlin Heidelberg, 2008. http://dx.doi.org/10.1007/978-3-540-77901-8_2.

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Conference papers on the topic "And enzyme kinetics"

1

Ondruch, V., J. Krejci, and D. Krejcova. "Simple Electrochemical Analysis of Enzyme Kinetics." In 2005 IEEE Engineering in Medicine and Biology 27th Annual Conference. IEEE, 2005. http://dx.doi.org/10.1109/iembs.2005.1615490.

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Vojisavljevic, V., E. Pirogova, and I. Cosic. "Influence of Electromagnetic Radiation on Enzyme Kinetics." In 2007 29th Annual International Conference of the IEEE Engineering in Medicine and Biology Society. IEEE, 2007. http://dx.doi.org/10.1109/iembs.2007.4353468.

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Bashkirtseva, I., S. Zaitseva, and A. Pisarchik. "Noise-induced phantom attractor in the enzyme kinetics." In APPLICATION OF MATHEMATICS IN TECHNICAL AND NATURAL SCIENCES: 11th International Conference for Promoting the Application of Mathematics in Technical and Natural Sciences - AMiTaNS’19. AIP Publishing, 2019. http://dx.doi.org/10.1063/1.5130805.

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Lee, Alan I., and James P. Brody. "New assay for multiple single molecule enzyme kinetics." In Biomedical Optics 2005, edited by Dan V. Nicolau, Joerg Enderlein, Robert C. Leif, Daniel L. Farkas, and Ramesh Raghavachari. SPIE, 2005. http://dx.doi.org/10.1117/12.585110.

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Char, Bruce W., and Mark F. Russo. "Automatic identification of time scales in enzyme kinetics models." In the international symposium. New York, New York, USA: ACM Press, 1994. http://dx.doi.org/10.1145/190347.190369.

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Uhl, Volker, Goetz Pilarczyk, and Karl-Otto Greulich. "Enzyme kinetics on a molecular level with optical microscopy." In BiOS Europe '97, edited by Irving J. Bigio, Herbert Schneckenburger, Jan Slavik, Katarina Svanberg, and Pierre M. Viallet. SPIE, 1997. http://dx.doi.org/10.1117/12.297961.

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Robinson, Tom, Hugh B. Manning, Christopher Dunsby, Mark A. A. Neil, Geoff S. Baldwin, Andrew J. de Mello, and Paul M. W. French. "Investigating fast enzyme-DNA kinetics using multidimensional fluorescence imaging and microfluidics." In MOEMS-MEMS, edited by Holger Becker and Wanjun Wang. SPIE, 2010. http://dx.doi.org/10.1117/12.840035.

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Kar, Saurajyoti, Shankarsan Ganai, Abhishek Dutta, Debjani Dutta, Surabhi Chaudhuri, Swapan Paruya, Samarjit Kar, and Suchismita Roy. "A sensitivity analysis study of enzyme inhibition kinetics through Cellular Automata." In INTERNATIONAL CONFERENCE ON MODELING, OPTIMIZATION, AND COMPUTING (ICMOS 20110). AIP, 2010. http://dx.doi.org/10.1063/1.3516319.

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FENG, Y., R. H. DAVIES, and J. D. ANDRADE. "ENZYME KINETICS MODEL OF THE BACTERIAL LUCIFERASE REACTIONS FOR BIOSENSOR APPLICATIONS." In Bioluminescence and Chemiluminescence - Progress and Current Applications - 12th International Symposium on Bioluminescence (BL) and Chemiluminescence (CL). WORLD SCIENTIFIC, 2002. http://dx.doi.org/10.1142/9789812776624_0100.

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Alshbool, Mohammed. "Bernstein Polynomials Method to Solve Fractional Model of Basic Enzyme Kinetics." In 2nd International Conference on Advanced Research in Applied Science and Engineering. GLOBALKS, 2020. http://dx.doi.org/10.33422/2nd.rase.2020.03.93.

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Reports on the topic "And enzyme kinetics"

1

Sandermann, Heinrich, Duncan Jr., and Thomas M. Lipid-Dependent Membrane Enzymes. Kinetic Modelling of the Activation of Protein Kinase C by Phosphatidylserine. Fort Belvoir, VA: Defense Technical Information Center, January 1991. http://dx.doi.org/10.21236/ada302987.

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Chikwana, Vimbai. Discovery of Novel Amidotransferase Activity Involved In Archaeosine Biosynthesis and Structural and Kinetic Investigation of QueF, an Enzyme Involved in Queuosine Biosynthesis. Portland State University Library, January 2000. http://dx.doi.org/10.15760/etd.140.

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