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Journal articles on the topic 'Enzyme kinetics'

Author: Grafiati

Published: 4 June 2021

Last updated: 25 July 2025

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1

Guerrieri, Antonio, Rosanna Ciriello, Giuliana Bianco, Francesca De Gennaro та Silvio Frascaro. "Allosteric Enzyme-Based Biosensors—Kinetic Behaviours of Immobilised L-Lysine-α-Oxidase from Trichoderma viride: pH Influence and Allosteric Properties". Biosensors 10, № 10 (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-Ch

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2

Radeef, Ziyad K. "A Comparative Analysis of Michaelis-Menten, Hill, and Allosteric Models in Drug Metabolism." Iraqi Journal of Industrial Research 12, no. 1 (2025): 98–108. https://doi.org/10.53523/ijoirvol12i1id547.

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Background: Enzyme Kinetics it is a fundamental part of metabolic biochemistry because it helps to explore the mechanism of action and interaction of all substrates under the influence as well as environmental factors. Aim: The present study intends to compare the kinetic models that have been employed to assess their efficacy in pharmaceutical kinetics and drug-trans metabolizing enzymes and efficiency. Study Design: Methodology and Experimental Design: The data were collected for separate enzymes (CYP3A4, CYP2D6 and UDP-glucuronosyltransferase) at different substrate concentrations and fit c

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3

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

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4

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

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5

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

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6

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

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7

Lloyd, Matthew D. "Steady-state enzyme kinetics." Biochemist 43, no. 3 (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 can

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8

Markin, C. J., D. A. Mokhtari, F. Sunden, et al. "Revealing enzyme functional architecture via high-throughput microfluidic enzyme kinetics." Science 373, no. 6553 (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

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9

Martín, J., J. Pérez-Gil, C. Acebal, and R. Arche. "Theoretical approach to the steady-state kinetics of a bi-substrate acyl-transfer enzyme reaction that follows a hydrolysable-acyl-enzyme-based mechanism. Application to the study of lysophosphatidylcholine:lysophosphatidylcholine acyltransferase from rabbit lung." Biochemical Journal 266, no. 1 (1990): 47–53. http://dx.doi.org/10.1042/bj2660047.

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A kinetic model is proposed for catalysis by an enzyme that has several special characteristics: (i) it catalyses an acyl-transfer bi-substrate reaction between two identical molecules of substrate, (ii) the substrate is an amphiphilic molecule that can be present in two physical forms, namely monomers and micelles, and (iii) the reaction progresses through an acyl-enzyme-based mechanism and the covalent intermediate can react also with water to yield a secondary hydrolytic reaction. The theoretical kinetic equations for both reactions were deduced according to steady-state assumptions and the

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10

Meilany, Diah, Efri Mardawati, Made Tri Ari Penia Kresnowati, and Tjandra Setiadi. "KINETIC STUDY OF OIL PALM EMPTY FRUIT BUNCH ENZYMATIC HYDROLYSIS." Reaktor 17, no. 4 (2018): 197. http://dx.doi.org/10.14710/reaktor.17.4.197-202.

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As lignocellulosic biomass, Oil Palm Empty Fruit Bunch (OPEFB) can be used as the source of xylose that can be further utilized as the raw material for xylitol production. The processing of OPEFB to xylose comprises of pretreatment and hydrolysis that can be performed enzymatically. This process offers the advantages of moderate operation conditions and more environmentally friendly. This article describes the kinetic study of enzymatic hydrolysis process of OPEFB for producing xylose using self-prepared and commercial xylanase enzymes. Despite the possible mass transfer limitation, the Michae

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11

WU, Jia-Wei, Zhi-Xin WANG, and Jun-Mei ZHOU. "Inactivation kinetics of dihydrofolate reductase from Chinese hamster during urea denaturation." Biochemical Journal 324, no. 2 (1997): 395–401. http://dx.doi.org/10.1042/bj3240395.

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The kinetic theory of substrate reaction during modification of enzyme activity has been applied to the study of inactivation kinetics of Chinese hamster dihydrofolate reductase by urea [Tsou (1988) Adv. Enzymol. Relat. Areas Mol. Biol. 61, 381–436]. On the basis of the kinetic equation of substrate reaction in the presence of urea, all microscopic kinetic constants for the free enzyme and enzyme–substrate binary and ternary complexes have been determined. The results of the present study indicate that the denaturation of dihydrofolate reductase by urea follows single-phase kinetics, and chang

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12

Tang, J. Y. "On the relationships between Michaelis–Menten kinetics, reverse Michaelis–Menten kinetics, Equilibrium Chemistry Approximation kinetics and quadratic kinetics." Geoscientific Model Development Discussions 8, no. 9 (2015): 7663–91. http://dx.doi.org/10.5194/gmdd-8-7663-2015.

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Abstract. The Michaelis–Menten kinetics and the reverse Michaelis–Menten kinetics are two popular mathematical formulations used in many land biogeochemical models to describe how microbes and plants would respond to changes in substrate abundance. However, the criteria of when to use which of the two are often ambiguous. Here I show that these two kinetics are special approximations to the Equilibrium Chemistry Approximation kinetics, which is the first order approximation to the quadratic kinetics that solves the equation of enzyme-substrate complex exactly for a single enzyme single substra

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13

Fink, A. M. "Optimal control in liver kinetics." Journal of the Australian Mathematical Society. Series B. Applied Mathematics 27, no. 3 (1986): 361–69. http://dx.doi.org/10.1017/s0334270000004987.

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AbstractWe solve a minimization problem in liver kinetics posed by Bass, et al., in this journal, (1984), pages 538–562. The problem is to choose the density functions for the location of two enzymes, in order to minimize the concentration of an intermediate form of a substance at the outlet of the liver. This form may be toxic to the rest of the body, but the second enzyme renders it harmless. It seems natural that the second enzyme should be downstream from the first. However, we can show that the minimum problem is sometimes solved by an overlap of the supports of the two density functions.

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14

Dusíková, Adriána, Timea Baranová, Ján Krahulec, et al. "Electrochemical Impedance Spectroscopy for the Sensing of the Kinetic Parameters of Engineered Enzymes." Sensors 24, no. 8 (2024): 2643. http://dx.doi.org/10.3390/s24082643.

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The study presents a promising approach to enzymatic kinetics using Electrochemical Impedance Spectroscopy (EIS) to assess fundamental parameters of modified enteropeptidases. Traditional methods for determining these parameters, while effective, often lack versatility and convenience, especially under varying environmental conditions. The use of EIS provides a novel approach that overcomes these limitations. The enteropeptidase underwent genetic modification through the introduction of single amino acid modifications to assess their effect on enzyme kinetics. However, according to the one-sam

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15

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

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16

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

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17

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

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18

Cornish-Bowden, Athel. "Encyclopaedic enzyme kinetics." Trends in Biochemical Sciences 19, no. 3 (1994): 142. http://dx.doi.org/10.1016/0968-0004(94)90211-9.

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19

Khan, Khushal, and Muhammad Farooq. "Kinetic and Thermodynamic Analysis of Enzyme-Catalyzed Reactions in Biochemical Systems." International Journal of Emerging Trends in Chemistry (IJETC) 1, no. 2 (2025): 1–15. https://doi.org/10.64056/h9gd6a33.

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Enzymes are biological catalysts that significantly enhance the rates of biochemical reactions by lowering the activation energy barriers. The study of enzyme-catalyzed reactions from both kinetic and thermodynamic perspectives is crucial to understanding their function in metabolic pathways, drug design, and industrial applications. This research explores the fundamental principles governing enzyme kinetics, such as Michaelis-Menten and allosteric models, and delves into thermodynamic parameters like Gibbs free energy, enthalpy, and entropy changes during enzyme-substrate interactions. Using

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20

Tang, J. Y. "On the relationships between the Michaelis–Menten kinetics, reverse Michaelis–Menten kinetics, equilibrium chemistry approximation kinetics, and quadratic kinetics." Geoscientific Model Development 8, no. 12 (2015): 3823–35. http://dx.doi.org/10.5194/gmd-8-3823-2015.

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Abstract. The Michaelis–Menten kinetics and the reverse Michaelis–Menten kinetics are two popular mathematical formulations used in many land biogeochemical models to describe how microbes and plants would respond to changes in substrate abundance. However, the criteria of when to use either of the two are often ambiguous. Here I show that these two kinetics are special approximations to the equilibrium chemistry approximation (ECA) kinetics, which is the first-order approximation to the quadratic kinetics that solves the equation of an enzyme–substrate complex exactly for a single-enzyme and

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21

Schnell, S. "Enzyme Kinetics at High Enzyme Concentration." Bulletin of Mathematical Biology 62, no. 3 (2000): 483–99. http://dx.doi.org/10.1006/bulm.1999.0163.

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22

Pyne, N. J., M. E. Cooper, and M. D. Houslay. "Identification and characterization of both the cytosolic and particulate forms of cyclic GMP-stimulated cyclic AMP phosphodiesterase from rat liver." Biochemical Journal 234, no. 2 (1986): 325–34. http://dx.doi.org/10.1042/bj2340325.

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Two enzymes displaying cyclic GMP-stimulated cyclic AMP phosphodiesterase activity were purified from rat liver to apparent homogeneity: a ‘particulate enzyme’ found as an integral membrane protein associated with the plasma membrane, and a ‘soluble’ enzyme found in the cytosol. The physical properties of these enzymes were very similar, being dimers of Mr 134,000, composed in each instance of two subunits of Mr = 66,000-67,000. Both enzymes showed similar kinetics for cyclic AMP hydrolysis. They are both high-affinity enzymes, with kinetic constants for the particulate enzyme of Km = 34 micro

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23

Wang, Z. X., H. B. Wu, X. C. Wang, H. M. Zhou, and C. L. Tsou. "Kinetics of the course of inactivation of aminoacylase by 1,10-phenanthroline." Biochemical Journal 281, no. 1 (1992): 285–90. http://dx.doi.org/10.1042/bj2810285.

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The kinetic theory of the substrate reaction during modification of enzyme activity previously described [Tsou (1988) Adv. Enzymol. Relat. Areas Mol. Biol. 61, 381-436] has been applied to a study on the kinetics of the course of inactivation of aminoacylase by 1,10-phenanthroline. Upon dilution of the enzyme that had been incubated with 1,10-phenanthroline into the reaction mixture, the activity of the inhibited enzyme gradually increased, indicating dissociation of a reversible enzyme–1,10-phenanthroline complex. The kinetics of the substrate reaction with different concentrations of the sub

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24

Blackmore, R. S., T. Brittain, and C. Greenwood. "An analysis of the reaction kinetics of the hexahaem nitrite reductase of the anaerobic rumen bacterium Wolinella succinogenes." Biochemical Journal 271, no. 2 (1990): 457–61. http://dx.doi.org/10.1042/bj2710457.

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The reduction kinetics of both the resting and redox-cycled forms of the nitrite reductase from the anaerobic rumen bacterium Wolinella succinogenes were studied by stopped-flow reaction techniques. Single-turnover reduction of the enzyme by dithionite occurs in two kinetic phases for both forms of the enzyme. When the resting form of the enzyme is subjected to a single-turnover reduction by dithionite, the slower of the two kinetic phases exhibits a hyperbolic dependence of the rate constant on the square root of the reductant concentration, the limiting value of which (approximately 4 s-1) i

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25

Crabbe, M. James C., and Derek Goode. "Nonlinear steady-state kinetics of chloramphenicol acetyltransferase." Biochemistry and Cell Biology 69, no. 9 (1991): 630–34. http://dx.doi.org/10.1139/o91-093.

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Steady-state kinetic analysis of chloramphenicol acetyltransferase showed that medium effects (higher temperatures or pH, higher ionic strengths, or lower values for dielectric constant) altered the kinetic behaviour of the enzyme with acetyl-CoA as substrate, but did not significantly affect behaviour with chloramphenicol. This was manifest as an increase in the degree of the rate equation to a 2:2 function. This is interpreted in terms of perturbations to the enzyme at or near the acetyl-CoA binding region of the enzyme.Key words: acetyl coenzyme A, chloramphenicol, antibiotics, enzyme kinet

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26

DE ATAURI, Pedro, Luis ACERENZA, Boris N. KHOLODENKO, et al. "Occurrence of paradoxical or sustained control by an enzyme when overexpressed: necessary conditions and experimental evidence with regard to hepatic glucokinase." Biochemical Journal 355, no. 3 (2001): 787–93. http://dx.doi.org/10.1042/bj3550787.

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It is widely assumed that the control coefficient of an enzyme on pathway flux decreases as the concentration of enzyme increases. However, it has been shown [Kholodenko and Brown (1996) Biochem. J. 314, 753–760] that enzymes with sigmoidal kinetics can maintain or even gain control with an increase in enzyme activity or concentration. This has been described as ‘paradoxical control’. Here we formulate the general requirements for allosteric enzyme kinetics to display this behaviour. We show that a necessary condition is that the Hill coefficient of the enzyme should increase with an increase

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27

Romaní, A. M. "Characterization of extracellular enzyme kinetics in two Mediterranean streams." Fundamental and Applied Limnology 148, no. 1 (2000): 99–117. http://dx.doi.org/10.1127/archiv-hydrobiol/148/2000/99.

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28

Duskey, Jason Thomas, Federica da Ros, Ilaria Ottonelli, et al. "Enzyme Stability in Nanoparticle Preparations Part 1: Bovine Serum Albumin Improves Enzyme Function." Molecules 25, no. 20 (2020): 4593. http://dx.doi.org/10.3390/molecules25204593.

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Enzymes have gained attention for their role in numerous disease states, calling for research for their efficient delivery. Loading enzymes into polymeric nanoparticles to improve biodistribution, stability, and targeting in vivo has led the field with promising results, but these enzymes still suffer from a degradation effect during the formulation process that leads to lower kinetics and specific activity leading to a loss of therapeutic potential. Stabilizers, such as bovine serum albumin (BSA), can be beneficial, but the knowledge and understanding of their interaction with enzymes are not

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29

WANG, Ming-Hua, Zhi-Xin WANG, and Kang-Yuan ZHAO. "Kinetics of inactivation of bovine pancreatic ribonuclease A by bromopyruvic acid." Biochemical Journal 320, no. 1 (1996): 187–92. http://dx.doi.org/10.1042/bj3200187.

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The kinetic theory of substrate reaction during the modification of enzyme activity [Duggleby (1986) J. Theor. Biol. 123, 67–80; Wang and Tsou (1990) J. Theor. Biol. 142, 531–549] has been applied to a study of the inactivation kinetics of ribonuclease A by bromopyruvic acid. The results show that irreversible inhibition belongs to a non-competitive complexing type inhibition. On the basis of the kinetic equation of substrate reaction in the presence of the inhibitor, all microscopic kinetic constants for the free enzyme, the enzyme–substrate complex and the enzyme–product complex have been de

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30

Johnson, Eachan, and Luet-Lok Wong. "Partial fusion of a cytochrome P450 system by carboxy-terminal attachment of putidaredoxin reductase to P450cam (CYP101A1)." Catalysis Science & Technology 2016, no. 6 (2016): 7549–60. https://doi.org/10.1039/C6CY01042C.

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Cytochrome P450 (CYP) enzymes catalyze the insertion of oxygen into carbon–hydrogen bonds and have great potential for enzymatic synthesis. Application development of class I CYPs is hampered by their dependence on two redox partners (a ferredoxin and ferredoxin reductase), slowing catalysis compared to self-sufficient CYPs such as CYP102A1 (P450BM3). Previous attempts to address this have fused all three components in several permutations and geometries, with much reduced activity compared to the native system. We report here the new approach of fusing putidaredoxin reductase (PdR) to the car

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31

Valchev, Ivo, Nikolay Yavorov, and Stoyko Petrin. "Topochemical kinetic mechanism of cellulase hydrolysis on fast-growing tree species. COST Action FP1105." Holzforschung 70, no. 12 (2016): 1147–53. http://dx.doi.org/10.1515/hf-2016-0030.

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Abstract Optimization of the lignocellulosic bioconversion by cellulolytic enzymes requires good knowledge of reaction kinetics. In the present paper, the investigations of the kinetics have been performed on the fast-growing tree species of poplar, paulownia, willow and black locust, which were pretreated by steam explosion (SE), and bleached kraft pulp (BKP) made of a hardwood mixture. The applicability of different kinetic equations referring to diffusion, topochemical and other heterogeneous catalytic processes was examined, and it was found that the enzyme process is best described by the

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32

Vannoy, Kathryn J., Andrey Ryabykh, Andrei I. Chapoval, and Jeffrey E. Dick. "Single enzyme electroanalysis." Analyst 146, no. 11 (2021): 3413–21. http://dx.doi.org/10.1039/d1an00230a.

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Traditional enzymology relies on the kinetics of millions of enzymes, an experimental approach that may wash out heterogeneities between individual enzymes. Electrochemical methods have emerged in the last 5 years to probe single enzyme reactivity.

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33

Kawinwit, Kuntida, Sanoe Koonprasert, and Akapak Charoenloedmongkhon. "THREE TYPES OF KINETICS AND INSTABILITY FOR ENZYMATIC GLUCOSE FUEL CELL MODELS." COMPUSOFT: An International Journal of Advanced Computer Technology 09, no. 05 (2020): 3690–97. https://doi.org/10.5281/zenodo.14935868.

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Mathematical modeling plays an important role in biochemistry having various enzymatic fuel cell problems. Enzymes are the basis of life activities and involved in almost all chemical reactions in organisms. The metabolic system of many anabolic and catabolic reactions under the catalysis of enzymes, which the study of the chemical reactions that are catalyzed by enzymes is called enzyme kinetics. This paper aims to discuss the enzyme kinetics term of the enzymatic glucose fuel cells. We apply three types of enzyme kinetics including the Michaelis Menten equation, the Morrison equation (Quadra

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34

O., Garuba Emmanuel, Yekini Fatima Ajoke, and Owoseni Ibukunoluwa Iyanuoluwa. "Biophysical Properties of Thermostable Amidase Produced by Aspergillus fumigatus in Submerged Fermentation." Biotechnology Journal International 28, no. 5 (2024): 49–58. http://dx.doi.org/10.9734/bji/2024/v28i5741.

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Amidases, also known as amidohydrolases (EC 3.5.1.4), are enzymes within the nitrilase superfamily or amidase signature family. They hydrolyze amides and nitriles into their corresponding acids while releasing ammonia. These enzymes are widely used in biotechnology and industry. However, their production is limited to a few organisms, which cannot meet industrial demand. Therefore, exploring new amidase sources is crucial. This study focuses on purifying and characterizing amidase from Aspergillus fumigatus using cold acetone precipitation and column chromatography with Sephadex G-100. The eff

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35

Goel, Rajeev, Takashi Mino, Hiroyasu Satoh, and Tomonori Matsuo. "Comparison of hydrolytic enzyme systems in pure culture and activated sludge under different electron acceptor conditions." Water Science and Technology 37, no. 4-5 (1998): 335–43. http://dx.doi.org/10.2166/wst.1998.0659.

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Enzymatic hydrolysis under different electron acceptor conditions in nutrient removal activated sludge treatment processes is a weak link in the Activated Sludge Model no. 2 (Henze et al., 1995). An experimental study was undertaken to gain insight into the hydrolysis process with specific focus on hydrolysis kinetics and rates under different electron acceptor conditions. Two pure cultures, Bacillus amyloliquefaciens (Gram positive) and Pseudomonas saccharophila (Gram negative) were chosen for the study. In addition, activated sludge grown in an anaerobic-aerobic system was tested for enzymat

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36

Altıok, Evren, and Maya Mahfuz. "Software Development with the R Programming Language for Studying Tyrosinase Enzyme Kinetics in Giresun Chanterelle Mushrooms." Karadeniz Fen Bilimleri Dergisi 14, no. 4 (2024): 2069–81. https://doi.org/10.31466/kfbd.1518620.

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In this study, a software application for enzyme kinetics analysis was developed using the R programming language. The software was designed utilizing the kinetic measurement values of tyrosinase enzyme from Giresun chanterelle (Cantharellus cibarius) mushrooms. Detailed step-by-step documentation of the software development process is provided. The program includes statistical evaluations and applies the Michaelis-Menten enzyme kinetics model to describe the enzyme kinetics of Giresun chanterelle. Initial reaction rate values were determined with a high correlation and regression coefficient

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37

Kazura, Evan, Ray Mernaugh, and Franz Baudenbacher. "A Capillary-Perfused, Nanocalorimeter Platform for Thermometric Enzyme-Linked Immunosorbent Assay with Femtomole Sensitivity." Biosensors 10, no. 6 (2020): 71. http://dx.doi.org/10.3390/bios10060071.

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Enzyme-catalyzed chemical reactions produce heat. We developed an enclosed, capillary-perfused nanocalorimeter platform for thermometric enzyme-linked immunosorbent assay (TELISA). We used catalase as enzymes to model the thermal characteristics of the micromachined calorimeter. Model-assisted signal analysis was used to calibrate the nanocalorimeter and to determine reagent diffusion, enzyme kinetics, and enzyme concentration. The model-simulated signal closely followed the experimental signal after selecting for the enzyme turnover rate (kcat) and the inactivation factor (InF), using a known

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38

Ovádi, J., P. Tompa, B. Vértessy, F. Orosz, T. Keleti, and G. R. Welch. "Transient-time analysis of substrate-channelling in interacting enzyme systems." Biochemical Journal 257, no. 1 (1989): 187–90. http://dx.doi.org/10.1042/bj2570187.

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The kinetics of dynamically interacting enzyme systems is examined, in the light of increasing evidence attesting to the widespread occurrence of this mode of organization in vivo. The transient time, a key phenomenological parameter for the coupled reaction, is expressed as a function of the lifetime of the intermediate substrate. The relationships between the transient time and the pseudo-first-order rate constants for the coupled reaction by the complexed and uncomplexed enzyme species are indicative of the mechanism of intermediate transfer (‘channelling’). In a dynamically interacting enz

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39

McDonald, A. G. "Implications of enzyme kinetics." Biochemical Society Transactions 31, no. 3 (2003): 719–22. http://dx.doi.org/10.1042/bst0310719.

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Of the many examples of oscillatory kinetic behaviour known, several are briefly reviewed, including those of glycolysis, the peroxidase–oxidase reaction and oscillations in cellular calcium concentration. It is shown that simple mathematical models employing allosteric rate laws are sufficient to explain the instability of the steady state and the appearance of sustained oscillations. The cAMP-signalling systems of cellular slime moulds and the dynamics of intracellular calcium oscillations illustrate the importance of such oscillophores to inter- and intra-cellular communication and differen

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40

HAPPEL, JOHN, and PETER H. SELLERS. "ENZYME MECHANISM AND KINETICS*." Chemical Engineering Communications 152-153, no. 1 (1996): 433–68. http://dx.doi.org/10.1080/00986449608936577.

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41

Alberty, Robert A. "Rapid-Equilibrium Enzyme Kinetics." Journal of Chemical Education 85, no. 8 (2008): 1136. http://dx.doi.org/10.1021/ed085p1136.

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42

Selwyn, MJ. "Fundamentals of enzyme kinetics." Biochemical Education 24, no. 1 (1996): 63. http://dx.doi.org/10.1016/s0307-4412(96)80014-8.

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43

DAGANI, RON. "STRAIGHTENING OUT ENZYME KINETICS." Chemical & Engineering News Archive 81, no. 24 (2003): 26. http://dx.doi.org/10.1021/cen-v081n024.p026.

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44

Byerley, Jennifer, Jin Zhou, and Aaron Teitelbaum. "UGT1A8: Atypical enzyme kinetics." Drug Metabolism and Pharmacokinetics 33, no. 1 (2018): S54. http://dx.doi.org/10.1016/j.dmpk.2017.11.185.

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45

Maxwell, A. "In focus: Enzyme kinetics." FEBS Letters 238, no. 1 (1988): 217–18. http://dx.doi.org/10.1016/0014-5793(88)80262-x.

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46

Zimmerman, James. "Enzyme kinetics and mechanism." Biochemistry and Molecular Biology Education 35, no. 5 (2007): 387. http://dx.doi.org/10.1002/bmb.88.

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Rodriguez, Jon-Marc G., and Marcy H. Towns. "Analysis of student reasoning about Michaelis–Menten enzyme kinetics: mixed conceptions of enzyme inhibition." Chemistry Education Research and Practice 20, no. 2 (2019): 428–42. http://dx.doi.org/10.1039/c8rp00276b.

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Student understanding regarding topics in upper-division courses, such as biochemistry, is not well represented in the literature. Herein we describe a study that investigated students’ reasoning about Michaelis–Menten enzyme kinetics and enzyme inhibition. Our qualitative study involved semistructured interviews with fourteen second-year students enrolled in an introductory biochemistry course. During the interviews students were provided an enzyme kinetics graph, which they were prompted to describe. Students were asked to look for patterns and trends in the data and interpret the graph to d

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Brooks, S. P. J. "Equilibrium enzymes in metabolic pathways." Biochemistry and Cell Biology 74, no. 3 (1996): 411–16. http://dx.doi.org/10.1139/o96-044.

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It is commonly believed that certain reactions in a metabolic sequence may be at or close to equilibrium because of the large excess of catalytic capacity compared to the flux through these enzyme loci. Simple algebraic manipulations can show that the equilibrium and steady state conditions are mutually exclusive. However, solution of the complete reaction schemes for model "equilibrium" reactions shows that they can remain far from equilibrium even though the ratio of enzyme flux to steady state flux through the overall pathway is high. These calculations show that a reaction's proximity to e

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WU, Jia-Wei, and Zhi-Xin WANG. "Activation mechanism and modification kinetics of Chinese hamster dihydrofolate reductase by p-chloromercuribenzoate." Biochemical Journal 335, no. 1 (1998): 181–89. http://dx.doi.org/10.1042/bj3350181.

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Substrate effects on the activation kinetics of Chinese hamster dihydrofolate reductase by p-chloromercuribenzoate (pCMB) have been studied. On the basis of the kinetic equation of substrate reaction in the presence of pCMB, all modification kinetic constants for the free enzyme and enzyme–substrate binary and ternary complexes have been determined. The results of the present study indicate that the modification of Chinese hamster dihydrofolate reductase by pCMB shows single-phase kinetics, and that changes in the enzyme activity and tertiary structure proceed simultaneously during the modific

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Klinman, Judith P., and Amnon Kohen. "Evolutionary Aspects of Enzyme Dynamics." Journal of Biological Chemistry 289, no. 44 (2014): 30205–12. http://dx.doi.org/10.1074/jbc.r114.565515.

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The role of evolutionary pressure on the chemical step catalyzed by enzymes is somewhat enigmatic, in part because chemistry is not rate-limiting for many optimized systems. Herein, we present studies that examine various aspects of the evolutionary relationship between protein dynamics and the chemical step in two paradigmatic enzyme families, dihydrofolate reductases and alcohol dehydrogenases. Molecular details of both convergent and divergent evolution are beginning to emerge. The findings suggest that protein dynamics across an entire enzyme can play a role in adaptation to differing phys

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