Enzyme Kinetics_.pptx
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Here you can find out the information about a very important topic of Biochemistry i.e. Enzyme Kinetics. I have elaborated how enzymes kinetics works . The most important equation Michaelis-menten equation, and Burk plot. #enzymes #biochemistry
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Enzyme kinetics and inhibition
This document discusses enzyme kinetics and inhibition. It describes how enzymes exert kinetic control over metabolic pathways and reactions. It aims to determine the maximum velocity, substrate affinity, and inhibitor affinity of enzymes. This can provide information about metabolic pathway flow, substrate utilization, and how to manipulate metabolic events. The document also discusses Michaelis-Menten kinetics, Lineweaver-Burk plots, competitive and non-competitive inhibition, and how inhibitors can be used to study enzyme mechanism and regulation.
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This document provides an overview of enzymes including:
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This document summarizes key concepts about enzyme kinetics and regulation:
1) Enzyme kinetics follows Michaelis-Menten models where the initial reaction rate (V0) increases with substrate concentration until reaching the maximum rate (Vmax) when enzyme sites are saturated.
2) Values like Km, Vmax, and Kcat/Km characterize enzyme-substrate binding affinity and catalytic efficiency. Km is the substrate concentration when V0 is half Vmax.
3) Reactions can involve single or multiple substrates through sequential or ping-pong mechanisms. Allosteric enzymes have cooperative binding between subunits and may be regulated by pathway end-products.
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Enzyme kinetics can provide information about enzyme activity under different conditions. The Michaelis-Menten approach models enzyme-catalyzed reactions and describes reaction rates with the Michaelis-Menten constant (Km) and maximum reaction rate (Vmax). Enzymes can be inhibited reversibly or irreversibly by inhibitors that reduce reaction rates. Different types of reversible inhibition include competitive, uncompetitive, and mixed inhibition. Temperature, pH, and allosteric effectors can regulate enzymatic activity through various mechanisms.
Effect of pH and temperature on enzyme activity notes
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Asst. Prof., Dept. of Biotechnology
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S.P.G.C.Nagar, Virudhunagar, Tamilnadu, India
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1) The document discusses enzyme kinetics and the Michaelis-Menten model of enzyme kinetics.
2) It introduces key concepts such as the Michaelis constant Km and maximum velocity Vmax, and derives the Michaelis-Menten equation relating substrate concentration, reaction rate, Km and Vmax.
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This document provides an overview of enzymes including:
- Their historical background, properties, nomenclature and classification. Enzymes are protein catalysts that increase reaction rates.
- Enzyme kinetics and the Michaelis-Menten constant (Km) which indicates the substrate concentration required for half maximal velocity.
- Factors that influence enzyme activity such as substrate and enzyme concentration, temperature, pH, and inhibitors. Optimum activity occurs within a narrow range of conditions.
- Different plots used to study enzyme kinetics including Michaelis-Menten and Lineweaver-Burk plots.
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The document discusses enzyme kinetics models including the Michaelis-Menten model and Lineweaver-Burk double reciprocal plot. The Michaelis-Menten model relates reaction rate to substrate concentration using kinetic constants Km and Vmax. It describes the enzyme-substrate reaction mechanism. The Lineweaver-Burk plot is a graphical representation that transforms the Michaelis-Menten equation into a straight line to determine Km and Vmax. It can distinguish competitive and noncompetitive enzyme inhibition patterns.
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This document summarizes key concepts about enzyme kinetics and regulation:
1) Enzyme kinetics follows Michaelis-Menten models where the initial reaction rate (V0) increases with substrate concentration until reaching the maximum rate (Vmax) when enzyme sites are saturated.
2) Values like Km, Vmax, and Kcat/Km characterize enzyme-substrate binding affinity and catalytic efficiency. Km is the substrate concentration when V0 is half Vmax.
3) Reactions can involve single or multiple substrates through sequential or ping-pong mechanisms. Allosteric enzymes have cooperative binding between subunits and may be regulated by pathway end-products.
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Enzyme kinetics can provide information about enzyme activity under different conditions. The Michaelis-Menten approach models enzyme-catalyzed reactions and describes reaction rates with the Michaelis-Menten constant (Km) and maximum reaction rate (Vmax). Enzymes can be inhibited reversibly or irreversibly by inhibitors that reduce reaction rates. Different types of reversible inhibition include competitive, uncompetitive, and mixed inhibition. Temperature, pH, and allosteric effectors can regulate enzymatic activity through various mechanisms.
Effect of pH and temperature on enzyme activity notes
Effect of pH and temperature on enzyme activity notesDepartment of Biotechnology, Kamaraj college of engineering and technology
Dr.S.Karthikumar
Asst. Prof., Dept. of Biotechnology
Kamaraj College of Engineering and Technology
S.P.G.C.Nagar, Virudhunagar, Tamilnadu, India
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The rate of a chemical reaction is described by the number of molecules of reactant(s) that are converted into the product(s) in a specified time period.
Numerous factors affect the rate of enzyme-catalyzed reactions.
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This document provides an overview of enzyme kinetics. It defines important terms like rate constant, substrate concentration, enzyme unit, and Michaelis constant. It describes models used to study enzyme kinetics like the Michaelis-Menten equations and Lineweaver-Burk, Hanes-Woolf, and Eadie-Hofstee plots. It discusses factors that affect reaction rates like pH, temperature, and inhibitors. The document also covers cooperative enzyme systems and multireactant reactions.
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Enzyme kinetics is the study of enzyme-catalyzed reaction rates. The Michaelis-Menten equation relates reaction velocity to substrate concentration and kinetic parameters. It describes the hyperbolic relationship between velocity and substrate concentration. The equation can be linearized into the Lineweaver-Burk plot for easier analysis. Enzyme inhibition studies help understand reaction mechanisms and are important for drug development, as most drugs function by inhibiting specific enzymes.
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This document discusses key concepts in enzyme kinetics including:
Vmax represents the maximum initial rate of a catalyzed reaction when all enzyme is saturated with substrate. Km is the substrate concentration at which the reaction rate is at half of Vmax, and 50% of enzyme is bound to substrate. A Line-Weaver Burk plot can be used to determine Km and Vmax values from experimental data by taking the inverse of reaction rates and substrate concentrations.
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2) The Michaelis-Menten model describes this relationship through kinetic parameters like Km (the substrate concentration when V0 is half of Vmax) and Vmax.
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This document discusses enzyme kinetics and provides details about key concepts. It introduces enzymes and their role in catalyzing reactions. It then describes enzyme kinetics as the study of reaction rates of enzyme-catalyzed reactions under varying conditions. Several key aspects of enzyme kinetics are summarized, including parametric analysis of enzyme catalysis, enzyme specificity, the lock and key model, and the Michaelis-Menten kinetics model. This model describes how reaction rates increase with substrate concentration until reaching a maximum rate Vmax as the enzyme becomes saturated.
Mechanisms involved at catalytic site
This document summarizes various catalytic mechanisms used by enzymes, including acid-base catalysis, covalent catalysis, metal ion catalysis, electrostatic catalysis, proximity and orientation effects, and preferential transition state binding. It provides examples of each mechanism, such as acid-base catalysis lowering the transition state energy of hydrolysis reactions and coenzymes functioning as covalent catalysts. Metal ions are involved in substrate orientation, oxidation-reduction reactions, and stabilizing charges. Enzyme active sites optimize proximity, orientation and transition state binding to greatly increase reaction rates.
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Some of the enzyme possess additional sites, known as allosteric sites besides the active site . Such as know as allosteric enzyme. The allosteric sites are unique place on the enzyme molecules allosteric enzyme have one or more allosteric site.
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Effector may be positive or negative, this effector regulate the enzyme activity . The enzyme activity is increased when a positive allosteric effector binds at the allosteric site known as activator site. On the other hand negative allosteric effector bind at the allosteric site called inhibitor site and inhibit the enzyme activity
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2) The Michaelis-Menten model describes this relationship through kinetic parameters like Km (the substrate concentration when V0 is half of Vmax) and Vmax.
3) Various plots like Lineweaver-Burk, Eadie-Hofstee, and Hanes-Woolf plots can be used to
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Enzyme assays are laboratory methods used to measure enzymatic activity. There are two main types - continuous assays that provide continuous readings of activity, and discontinuous assays where samples are taken and reactions stopped to determine substrate/product concentrations. Common continuous assay methods include spectrophotometric, fluorometric, calorimetric, and chemiluminescent assays, while discontinuous assays include radiometric and chromatographic methods. Proper controls must be established to account for factors like temperature, pH, substrate saturation, and salt/crowding effects. Specific examples provided are NADH oxidation, beta-galactosidase, and MTT/FDA hydrolysis assays.
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This document discusses enzyme kinetics and provides details about key concepts. It introduces enzymes and their role in catalyzing reactions. It then describes enzyme kinetics as the study of reaction rates of enzyme-catalyzed reactions under varying conditions. Several key aspects of enzyme kinetics are summarized, including parametric analysis of enzyme catalysis, enzyme specificity, the lock and key model, and the Michaelis-Menten kinetics model. This model describes how reaction rates increase with substrate concentration until reaching a maximum rate Vmax as the enzyme becomes saturated.
Mechanisms involved at catalytic site
This document summarizes various catalytic mechanisms used by enzymes, including acid-base catalysis, covalent catalysis, metal ion catalysis, electrostatic catalysis, proximity and orientation effects, and preferential transition state binding. It provides examples of each mechanism, such as acid-base catalysis lowering the transition state energy of hydrolysis reactions and coenzymes functioning as covalent catalysts. Metal ions are involved in substrate orientation, oxidation-reduction reactions, and stabilizing charges. Enzyme active sites optimize proximity, orientation and transition state binding to greatly increase reaction rates.
Allosteric enzymes
Some of the enzyme possess additional sites, known as allosteric sites besides the active site . Such as know as allosteric enzyme. The allosteric sites are unique place on the enzyme molecules allosteric enzyme have one or more allosteric site.
HISTRY
The term allosteric has been introduced by the two Noble Laureates JACOB AND MONOD to denote an enzyme site different from the active site which non competitively bands molecule other than the substrate and may influence the enzyme activity.
Properties of allosteric enzyme
Effector may be positive or negative, this effector regulate the enzyme activity . The enzyme activity is increased when a positive allosteric effector binds at the allosteric site known as activator site. On the other hand negative allosteric effector bind at the allosteric site called inhibitor site and inhibit the enzyme activity
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This document discusses allosteric enzymes, which have additional binding sites called allosteric sites that are distinct from the active site. Molecules that bind to these allosteric sites, called effectors, can cause a conformational change in the enzyme's structure that increases or decreases its catalytic activity. There are two main models that describe the mechanism of allostery: the concerted model proposed by Monod, Wyman, and Changeux and the sequential model proposed by Koshland, Nemethy, and Filmer. Allosteric effectors can be positive or negative, and allosteric regulation can be homotropic, involving the substrate, or heterotropic, involving a different molecule. Allo
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Kinetics of multi substrate enzyme catalyzed reaction
Enzyme kinetics is the study of enzyme-catalyzed chemical reactions. Enzymes lower the activation energy of reactions by binding substrates to their active sites. Multi-substrate reactions can follow sequential or non-sequential mechanisms. In sequential mechanisms, both substrates must bind before any product is released, while non-sequential mechanisms allow product release before all substrates bind. Ping-pong mechanisms are a type of non-sequential mechanism where the enzyme is temporarily modified between substrate bindings.
Immobilization of enzymes
Enzyme immobilization involves confining enzyme molecules to a distinct phase separate from the reaction substrates and products. This protects enzymes and allows for continuous use. Common immobilization methods include adsorption, ionic binding, covalent binding, cross-linking, and entrapment. Adsorption and ionic binding rely on weak interactions, while covalent binding forms stronger covalent bonds. Entrapment encloses enzymes within a semi-permeable polymer membrane or matrix. Immobilization can increase enzyme stability but may also reduce activity depending on the method used and how it affects enzyme structure and substrate binding/product release.
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1. Enzyme kinetics is the study of enzymatic reaction rates in response to experimental parameters like substrate concentration and inhibitors. It expresses chemical reactions mathematically.
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This document discusses enzyme kinetics and inhibition. It begins by defining factors that affect the rate of enzyme-catalyzed reactions, including enzyme concentration, substrate concentration, pH, temperature, and inhibitors. It then describes the Michaelis-Menten model of enzyme kinetics and how the Lineweaver-Burk plot can be used to analyze reaction data. Finally, it discusses different types of enzyme inhibition, including competitive, noncompetitive, and uncompetitive inhibition and how inhibitors impact kinetic parameters like Vmax and KM.
Enzymes
Enzymes are macromolecular biological catalysts that are proteins. They catalyze reactions by lowering the activation energy. Enzymes have several key properties - they are catalytic, colloidal in nature, highly specific, sensitive to temperature and pH changes. Enzymes are classified based on the type of reaction they catalyze into six main classes. The factors that affect enzyme activity include enzyme and substrate concentration, temperature, pH, and product concentration. Enzyme activity is highest at its optimal temperature and pH.
enzyyyyyyyymessss.pdf
The document discusses several key factors that affect enzyme activity: enzyme concentration, substrate concentration, temperature, pH, product concentration, presence of activators, time, and light/radiation. It explains how increasing or decreasing each factor can increase or decrease the reaction rate. For example, increasing enzyme concentration or an optimal temperature can increase the reaction rate, while too high or low of a pH can decrease it. The Michaelis-Menten equation and Lineweaver-Burk plots are also introduced to model enzyme kinetics.
Michaelis - Menten Curve of Enzyme Kinetic.pptx
The document discusses enzyme kinetics and inhibition. It describes how the reaction rate increases with substrate concentration until the enzyme becomes saturated. It also discusses the Michaelis-Menten equation and how the Michaelis constant (Km) represents the substrate concentration required for half maximal velocity. Further, it describes competitive, uncompetitive, and noncompetitive inhibition and how they differ in their effects on Km and Vmax.
enzyme kinetics.pptx
The key factors that affect enzyme activity are the concentration of the enzyme and substrate, temperature, pH, product concentration, and presence of activators. The maximum velocity of the reaction increases with higher enzyme and substrate concentrations up to a point. Temperature and pH also affect activity, with optimal rates usually around body temperature and neutral pH. Products can inhibit the enzyme as they accumulate. Certain metals are required as cofactors for some enzymes to function properly.
enzyme.pptx
The document discusses factors that affect the rate of enzyme action, including enzyme concentration, substrate concentration, temperature, pH, concentration of coenzymes and activators, time, and inhibitors. It provides details on how each factor influences the reaction rate. Specifically, it explains that enzyme activity is highest when substrate concentration is saturating but not excessive, and when other conditions like temperature and pH are optimal. The document also describes Michaelis-Menten kinetics and how reversible and irreversible inhibition can decrease reaction rates.
7.29.10 enzymes (kinetics) coloso
The document discusses enzyme kinetics and the Michaelis-Menten model. It explains that enzymes convert substrates to products over time in three phases: an initial rapid increase, then a steady state. The Michaelis-Menten model describes enzyme velocity as a function of substrate concentration using the constants KM and Vmax. KM represents the substrate concentration at half Vmax. Inhibitors are also discussed, including competitive and noncompetitive inhibition and how they affect the kinetic parameters.
enzyme_class2.ppt
Enzymes are globular proteins that function as biological catalysts, lowering the activation energy of chemical reactions without being changed themselves. They speed up reactions via an active site where substrates bind. Enzyme activity depends on structure and is highly specific. Factors like temperature, pH, substrate and enzyme concentration can affect reaction rate. Enzymes use various mechanisms like lock-and-key and induced fit to catalyze reactions. Inhibition studies help understand metabolic pathways and develop drugs. There are three main types of reversible inhibition - competitive, non-competitive, and uncompetitive - which are distinguished by their effects on Km and Vmax values.
enzyme biochemistry classification regulation
Enzymes are globular proteins that function as biological catalysts, lowering the activation energy of chemical reactions without being changed themselves. They speed up reactions via an active site where substrates bind. Enzyme activity depends on structure and is highly specific. Factors like temperature, pH, substrate and enzyme concentration can affect reaction rate. Enzymes use various mechanisms like lock-and-key and induced fit to catalyze reactions. Inhibition studies help understand metabolic pathways and develop drugs. There are three main types of reversible inhibition - competitive, non-competitive, and uncompetitive - which are distinguished by their effects on Km and Vmax values.
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Enzyme kinetics, factors and mechanism of enzyme activity
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11.1 Role of physical biological in deterioration of grains.pdf
Storagedeteriorationisanyformoflossinquantityandqualityofbio-materials.
Themajorcausesofdeteriorationinstorage
•Physical
•Biological
•Mechanical
•Chemical
Storageonlypreservesquality.Itneverimprovesquality.
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Farming systems analysis: what have we learnt?.pptx
Presentation given at the official farewell of Prof Ken Gillet at Wageningen on 13 June 2024
Compexometric titration/Chelatorphy titration/chelating titration
Classification
Metal ion ion indicators
Masking and demasking reagents
Estimation of Magnisium sulphate
Calcium gluconate
Complexometric Titration/ chelatometry titration/chelating titration, introduction, Types-
1.Direct Titration
2.Back Titration
3.Replacement Titration
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Masking agent, Demasking agents
formation of complex
comparition between masking and demasking agents,
Indicators/Metal ion indicators/ Metallochromic indicators/pM indicators,
Visual Technique,PM indicators (metallochromic), Indicators of pH, Redox Indicators
Instrumental Techniques-Photometry
Potentiometry
Miscellaneous methods.
Complex titration with EDTA.
在线办理(salfor毕业证书)索尔福德大学毕业证毕业完成信一模一样
学校原件一模一样【微信：741003700 】《(salfor毕业证书)索尔福德大学毕业证》【微信：741003700 】学位证，留信认证（真实可查，永久存档）原件一模一样纸张工艺/offer、雅思、外壳等材料/诚信可靠,可直接看成品样本，帮您解决无法毕业带来的各种难题！外壳，原版制作，诚信可靠，可直接看成品样本。行业标杆！精益求精，诚心合作，真诚制作！多年品质 ,按需精细制作，24小时接单,全套进口原装设备。十五年致力于帮助留学生解决难题，包您满意。
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SDSS1335+0728: The awakening of a ∼ 106M⊙ black hole⋆
Context. The early-type galaxy SDSS J133519.91+072807.4 (hereafter SDSS1335+0728), which had exhibited no prior optical variations during the preceding two decades, began showing significant nuclear variability in the Zwicky Transient Facility (ZTF) alert stream from December 2019 (as ZTF19acnskyy). This variability behaviour, coupled with the host-galaxy properties, suggests that SDSS1335+0728 hosts a ∼ 106M⊙ black hole (BH) that is currently in the process of ‘turning on’. Aims. We present a multi-wavelength photometric analysis and spectroscopic follow-up performed with the aim of better understanding the origin of the nuclear variations detected in SDSS1335+0728. Methods. We used archival photometry (from WISE, 2MASS, SDSS, GALEX, eROSITA) and spectroscopic data (from SDSS and LAMOST) to study the state of SDSS1335+0728 prior to December 2019, and new observations from Swift, SOAR/Goodman, VLT/X-shooter, and Keck/LRIS taken after its turn-on to characterise its current state. We analysed the variability of SDSS1335+0728 in the X-ray/UV/optical/mid-infrared range, modelled its spectral energy distribution prior to and after December 2019, and studied the evolution of its UV/optical spectra. Results. From our multi-wavelength photometric analysis, we find that: (a) since 2021, the UV flux (from Swift/UVOT observations) is four times brighter than the flux reported by GALEX in 2004; (b) since June 2022, the mid-infrared flux has risen more than two times, and the W1−W2 WISE colour has become redder; and (c) since February 2024, the source has begun showing X-ray emission. From our spectroscopic follow-up, we see that (i) the narrow emission line ratios are now consistent with a more energetic ionising continuum; (ii) broad emission lines are not detected; and (iii) the [OIII] line increased its flux ∼ 3.6 years after the first ZTF alert, which implies a relatively compact narrow-line-emitting region. Conclusions. We conclude that the variations observed in SDSS1335+0728 could be either explained by a ∼ 106M⊙ AGN that is just turning on or by an exotic tidal disruption event (TDE). If the former is true, SDSS1335+0728 is one of the strongest cases of an AGNobserved in the process of activating. If the latter were found to be the case, it would correspond to the longest and faintest TDE ever observed (or another class of still unknown nuclear transient). Future observations of SDSS1335+0728 are crucial to further understand its behaviour. Key words. galaxies: active– accretion, accretion discs– galaxies: individual: SDSS J133519.91+072807.4
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The shorelines of Titan’s hydrocarbon seas trace flooded erosional landforms such as river valleys; however, it isunclear whether coastal erosion has subsequently altered these shorelines. Spacecraft observations and theo-retical models suggest that wind may cause waves to form on Titan’s seas, potentially driving coastal erosion,but the observational evidence of waves is indirect, and the processes affecting shoreline evolution on Titanremain unknown. No widely accepted framework exists for using shoreline morphology to quantitatively dis-cern coastal erosion mechanisms, even on Earth, where the dominant mechanisms are known. We combinelandscape evolution models with measurements of shoreline shape on Earth to characterize how differentcoastal erosion mechanisms affect shoreline morphology. Applying this framework to Titan, we find that theshorelines of Titan’s seas are most consistent with flooded landscapes that subsequently have been eroded bywaves, rather than a uniform erosional process or no coastal erosion, particularly if wave growth saturates atfetch lengths of tens of kilometers.
The cost of acquiring information by natural selection
This is a short talk that I gave at the Banff International Research Station workshop on Modeling and Theory in Population Biology. The idea is to try to understand how the burden of natural selection relates to the amount of information that selection puts into the genome.
It's based on the first part of this research paper:
The cost of information acquisition by natural selection
Ryan Seamus McGee, Olivia Kosterlitz, Artem Kaznatcheev, Benjamin Kerr, Carl T. Bergstrom
bioRxiv 2022.07.02.498577; doi: https://doi.org/10.1101/2022.07.02.498577
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Thematic analysis in qualitative research is a time-consuming and systematic task, typically done using teams. Team members must ground their activities on common understandings of the major concepts underlying the thematic analysis, and define criteria for its development. However, conceptual misunderstandings, equivocations, and lack of adherence to criteria are challenges to the quality and speed of this process. Given the distributed and uncertain nature of this process, we wondered if the tasks in thematic analysis could be supported by readily available artificial intelligence chatbots. Our early efforts point to potential benefits: not just saving time in the coding process but better adherence to criteria and grounding, by increasing triangulation between humans and artificial intelligence. This tutorial will provide a description and demonstration of the process we followed, as two academic researchers, to develop a custom ChatGPT to assist with qualitative coding in the thematic data analysis process of immersive learning accounts in a survey of the academic literature: QUAL-E Immersive Learning Thematic Analysis Helper. In the hands-on time, participants will try out QUAL-E and develop their ideas for their own qualitative coding ChatGPT. Participants that have the paid ChatGPT Plus subscription can create a draft of their assistants. The organizers will provide course materials and slide deck that participants will be able to utilize to continue development of their custom GPT. The paid subscription to ChatGPT Plus is not required to participate in this workshop, just for trying out personal GPTs during it.
Randomised Optimisation Algorithms in DAPHNE
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Aleš Zamuda: Randomised Optimisation Algorithms in DAPHNE .
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https://ashpc.eu/
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Enzyme Kinetics_.pptx
- 1. Name – Ankur Kumar M.Sc. Microbiology ENZYME KINETICS Central University of Haryana
- 2. Enzyme Kinetics Quantitative study of enzyme catalysis. Measures the reaction rate and the affinity of enzymes for substrate and inhibitors. Factors that affect these rates . “T he st udy of t he rat es of enzyme cat alyzed react ions and affinit y for subst rat e and inhibit ors is called Enzyme kinet ics .”
- 3. Rate of reaction Rate of reaction is proportional to the products of concentration of each reactants. K is rate constent. F and g are stoichiometry .
- 4. Kinetics of Enzyme catalyzed Reactions • Rate(velocity) of enzyme catalyzes reaction depends on the substrate conc. • Initial velocity (V0) increases linearly with increase in substrate concentration . [S] • At high substrate conc., (V0) becomes virtually independent of substance conc. and approaches a maximal limit.(Vmax) V0=Vmax
- 5. . In the lower region of curve, showing first order reaction because rate proportional to substrate conc . In the upper region of curve the reaction is zero order reaction because rate of reaction becomes independent of substrate conc. This behaviour is called Saturation effect. . V0=Vmax
- 6. Michaelis-menten Approach • Since enzyme kinetics is a mixture of more than one kinetics and to represent it overall . • A particularly useful model for the kinetics of enzyme-catalyzed reactions was devised in 1913 by Leonor Michaelis and Maud Menten. The initial velocity (V0) of an enzyme catalyzed reaction is determined by two constents (Vmax), ( KM ) and initial conc. of substrate[S] • Fundamental equation for the enzyme kinetics.
- 7. KM • When the rate of the reaction is half its maximum value, the substrate concentration is equal to the Michaelis constant. From the Michaelis-menten equation
- 8. Significance of Km • Used to measure the [S].or the affinity for the enzyme. • Small the value of Michaelis menten constent means it will bind more tightly to enzyme and saturate the enzyme. Assumptions made - • [S]>[E] • The rate of formation of ES is equal to that of breakdown of ES .[steady state assumption] • Ignored any back reaction by which EP might form ES .
- 9. Lineweaver-Burk plot • Graphical representation of Lineweaver Burk Equation of enzyme kinetics. • From the Michaelis-menten equation • Reciprocal the both sides. • Now eq. has the form of a straight line Y m x c
- 10. . Y =mx+c 1/ V0 takes the place of Y coordinate and 1/S takes the place of x coordinate The slope of the line ,(m) is KM /Vmax and the y intercept (c) is 1/Vmax Significance--- More accurate determination of Vmax and also KM . Useful in distinguishing between certain types of enzymatics rxn mechanism.
- 11. References Principles of Biochemistry, Lehninger 6th ed. Biochemistry by Lubert Stryer. https://nios.ac.in Pathfinder Life science 7th Ed.