Chapter 3
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Enzymes are proteins that catalyze biochemical reactions and can require cofactors like prosthetic groups or coenzymes to function properly. The rate of an enzyme's reaction is affected by substrate and enzyme concentration, temperature, and pH. Enzymes can be inhibited by certain molecules and feedback inhibition regulates enzymatic pathways.
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Enzymes revision
Enzymes are protein molecules that act as biological catalysts, speeding up chemical reactions. They have an active site that binds to specific substrate molecules. The "lock and key" hypothesis states that enzymes and substrates fit together precisely, while the induced fit hypothesis is that they can slightly change shape to better fit. Enzymes lower the activation energy of reactions, allowing substrates to more easily convert to products. The rate of enzyme-catalyzed reactions depends on temperature, enzyme and substrate concentrations, and can be inhibited by other molecules binding to the enzyme. Immobilizing enzymes allows them to be reused for reactions.
Enzyme induction and repression
Enzyme induction and repression are important regulatory processes in molecular biology. Enzyme induction occurs when a molecule binds to a repressor and prevents it from blocking transcription of a gene encoding a specific enzyme. This allows increased production of the enzyme when needed. Enzyme repression is the default state, where a repressor binds to DNA and blocks transcription of enzyme genes. Understanding these processes is essential for analyzing drug reactions and metabolism.
Revision
This document provides definitions and key terms for monomers, polymers, amino acids, monosaccharides, condensation reactions, peptide bonds, glycosidic bonds, and triglycerides related to carbohydrates, proteins, and lipids. It matches each term with its correct definition and provides examples of where different biomolecules are found in the body and what functions they serve. The document also includes fill-in-the-blank questions and homework instructions for creating a revision resource on proteins, lipids, or carbohydrates.
Enzyme inhibition AND ITS TYPES
This document discusses enzyme inhibition. It defines inhibitors as substances that bind to enzymes and interfere with their activity, preventing the formation of enzyme-substrate complexes or their breakdown into products. There are two main types of inhibitors - reversible inhibitors, which bind non-covalently and can dissociate, and irreversible inhibitors, which bind covalently and permanently inactivate the enzyme. Reversible inhibition is further divided into competitive, uncompetitive and non-competitive inhibition based on whether the inhibitor binds the enzyme, enzyme-substrate complex, or both. Irreversible inhibitors permanently alter the enzyme's active site groups essential for activity. Examples of different types of inhibitors are provided.
Effects of Temperature and pH on Enzyme Activity and Deactivation.
This document summarizes how temperature and pH affect enzyme activity. It explains that enzymes have an optimal temperature and pH range where their activity is highest. Above or below this range, increases in temperature or changes in pH can cause the enzyme to denature by changing its shape, making the active site no longer complementary to the substrate. The rate of enzyme-catalyzed reactions is thus dependent on maintaining temperatures and pH near their respective optimal levels for that enzyme.
Enzyme
Enzymes are protein catalysts that speed up biochemical reactions. They work by lowering the activation energy of reactions through their specific three-dimensional structure. This structure complements that of substrates, facilitating the formation of enzyme-substrate complexes. Factors like temperature, pH, enzyme and substrate concentrations can affect reaction rates by impacting enzyme shapes and complex formation. Inhibitors also regulate enzymes by competing for or altering their active sites.
Factors affec enz act. 3
The document discusses factors that influence enzymatic reactions, including pH, temperature, and substrate concentration. It states that enzymes have an optimum pH and temperature at which their activity is highest. Both higher and lower pH and temperatures can decrease enzyme activity or even denature the enzyme. The initial reaction rate increases with substrate concentration until the enzyme reaches saturation, at which point further increases in substrate have no effect. The Michaelis-Menten theory postulates that at low substrate concentrations the reaction rate is not at its maximum velocity due to lack of enzyme saturation.
Factors affecting enzyme activity SlideShare
This document discusses enzymes and how various factors affect their activity. It explains that enzymes are proteins that act as biological catalysts, and that their activity is influenced by temperature, pH, substrate and enzyme concentration. The optimum temperature and pH are described as well as how rises or falls from these can impact activity. Isoenzymes, which are variants of the same enzyme found in different tissues, are also covered. The concept of rate-limiting enzymes, which determine the overall rate of a metabolic pathway, is defined.
Recommended
Enzymes revision
Enzymes are protein molecules that act as biological catalysts, speeding up chemical reactions. They have an active site that binds to specific substrate molecules. The "lock and key" hypothesis states that enzymes and substrates fit together precisely, while the induced fit hypothesis is that they can slightly change shape to better fit. Enzymes lower the activation energy of reactions, allowing substrates to more easily convert to products. The rate of enzyme-catalyzed reactions depends on temperature, enzyme and substrate concentrations, and can be inhibited by other molecules binding to the enzyme. Immobilizing enzymes allows them to be reused for reactions.
Enzyme induction and repression
Enzyme induction and repression are important regulatory processes in molecular biology. Enzyme induction occurs when a molecule binds to a repressor and prevents it from blocking transcription of a gene encoding a specific enzyme. This allows increased production of the enzyme when needed. Enzyme repression is the default state, where a repressor binds to DNA and blocks transcription of enzyme genes. Understanding these processes is essential for analyzing drug reactions and metabolism.
Revision
This document provides definitions and key terms for monomers, polymers, amino acids, monosaccharides, condensation reactions, peptide bonds, glycosidic bonds, and triglycerides related to carbohydrates, proteins, and lipids. It matches each term with its correct definition and provides examples of where different biomolecules are found in the body and what functions they serve. The document also includes fill-in-the-blank questions and homework instructions for creating a revision resource on proteins, lipids, or carbohydrates.
Enzyme inhibition AND ITS TYPES
This document discusses enzyme inhibition. It defines inhibitors as substances that bind to enzymes and interfere with their activity, preventing the formation of enzyme-substrate complexes or their breakdown into products. There are two main types of inhibitors - reversible inhibitors, which bind non-covalently and can dissociate, and irreversible inhibitors, which bind covalently and permanently inactivate the enzyme. Reversible inhibition is further divided into competitive, uncompetitive and non-competitive inhibition based on whether the inhibitor binds the enzyme, enzyme-substrate complex, or both. Irreversible inhibitors permanently alter the enzyme's active site groups essential for activity. Examples of different types of inhibitors are provided.
Effects of Temperature and pH on Enzyme Activity and Deactivation.
This document summarizes how temperature and pH affect enzyme activity. It explains that enzymes have an optimal temperature and pH range where their activity is highest. Above or below this range, increases in temperature or changes in pH can cause the enzyme to denature by changing its shape, making the active site no longer complementary to the substrate. The rate of enzyme-catalyzed reactions is thus dependent on maintaining temperatures and pH near their respective optimal levels for that enzyme.
Enzyme
Enzymes are protein catalysts that speed up biochemical reactions. They work by lowering the activation energy of reactions through their specific three-dimensional structure. This structure complements that of substrates, facilitating the formation of enzyme-substrate complexes. Factors like temperature, pH, enzyme and substrate concentrations can affect reaction rates by impacting enzyme shapes and complex formation. Inhibitors also regulate enzymes by competing for or altering their active sites.
Factors affec enz act. 3
The document discusses factors that influence enzymatic reactions, including pH, temperature, and substrate concentration. It states that enzymes have an optimum pH and temperature at which their activity is highest. Both higher and lower pH and temperatures can decrease enzyme activity or even denature the enzyme. The initial reaction rate increases with substrate concentration until the enzyme reaches saturation, at which point further increases in substrate have no effect. The Michaelis-Menten theory postulates that at low substrate concentrations the reaction rate is not at its maximum velocity due to lack of enzyme saturation.
Factors affecting enzyme activity SlideShare
This document discusses enzymes and how various factors affect their activity. It explains that enzymes are proteins that act as biological catalysts, and that their activity is influenced by temperature, pH, substrate and enzyme concentration. The optimum temperature and pH are described as well as how rises or falls from these can impact activity. Isoenzymes, which are variants of the same enzyme found in different tissues, are also covered. The concept of rate-limiting enzymes, which determine the overall rate of a metabolic pathway, is defined.
Enzyme induction and repression
This document defines and provides examples of enzyme induction and enzyme repression. It explains that enzyme induction occurs when a molecule like a drug binds to and increases the metabolic activity of an enzyme. This can increase clearance of a concomitantly administered drug and reduce its efficacy. Enzyme repression occurs when effectors alter the configuration of the operator so that polymerase binding is less efficient or prevented. Understanding enzyme induction and repression is important for analyzing drug reactions, studying toxicity, and understanding various body reactions and hormone production or depletion.
Factors affecting enzyme activity
This document discusses 5 key factors that affect enzyme activity: the concentration of the enzyme and substrate, temperature, pH, and the presence of activators. It notes that enzyme activity increases with higher enzyme and substrate concentrations up to a maximum point, and with temperature up to 40ยฐC, beyond which the enzyme denatures. Activity also increases with pH up to an optimum level, and some enzymes require metal ions or other ions to function at optimal levels. Maintaining optimal levels of these factors is important to control enzyme activity.
Enzyme inhibition
Enzyme introduction, Enzyme inhibition, Irreversible inhibition, reversible inhibition, competitive inhibition, noncompetitive inhibition, uncompetitive inhibition, examples for different types of inhibition, uses of enzyme inhibition in medicinal purpose, allosteric enzymes, allosteric activation, allosteric inhibition, pictorial explanation, graphical explanation.
Enzymes
Enzymes speed up chemical reactions in cells by lowering the activation energy needed for reactions to occur. They are protein catalysts that are highly specific to their substrate. The induced fit theory updated the lock and key concept of enzyme-substrate binding by proposing that enzymes change shape upon substrate binding to stabilize the transition state of the reaction. Factors like pH, temperature, and enzyme denaturation can affect enzyme activity levels.
Enzymes 2018
Enzymes are biological catalysts that speed up chemical reactions without being changed or used up themselves. They are protein molecules with an active site that attaches to a specific substrate molecule. The key properties of enzymes are that they are specific, and their activity is affected by temperature and pH levels. The optimum temperature and pH are the levels at which an enzyme works best - outside these levels the enzyme can become denatured and lose its shape/function.
Enzymes
This powerpoint presentation talks about enzymes, specifically its functions, the different types according to its function, and the definition of enzyme activator and inhibitor. A picture diagram is also included to show the process of enzyme activity and as well as a table differentiating apoenzyme and coenzyme. The different factors that affects the enzyme activity are also explained and lastly, the other uses of enzyme in medicine, food and etc.The content of the powerpoint presentation has undergone a research through internet and the best answers has been selected for better understanding. The resources of all the research made that was in this presentation are acknowledged as shown in the Reference part of the slide.
Enzyme inhibition
Enzyme inhibition is explained with its kinetics, animations showing mechanism of inhibitors action, examples of inhibitors are explained in detail with Enzyme inhibited.
by Dr. N. Sivaranjani, MD
Factor effecting the rate enzyme catalysed reactions
This document discusses the effects of pH, substrate, and temperature on enzyme-catalyzed reactions. It explains that pH can alter the shape of the enzyme and substrate, preventing them from interacting. Each enzyme works best at its optimum pH. Higher substrate concentrations lead to more frequent collisions and higher reaction rates, up to saturation. Temperature initially increases reaction rate by providing more kinetic energy, but excessive heat can denature the enzyme permanently by altering its shape.
ัะตัะผะตะฝั ะฑะฐ ัาฏาฏะฝะธะน าฏะนะป ะฐะถะธะปะปะฐะณะฐะฐ Enzyme activity
Enzymes are globular proteins that act as biological catalysts to speed up metabolic reactions. They have an active site that fits a specific substrate perfectly. The active site binds the substrate and forms an enzyme-substrate complex to lower the activation energy needed for the reaction. An enzyme's activity and stability depend on factors like temperature, pH, enzyme concentration, and substrate concentration. Changes in these factors can affect the enzyme's shape and ability to bind substrates. Inhibitors also impact enzyme function by binding to the active site or elsewhere on the enzyme.
6 enzyme notes
Enzymes are proteins that act as catalysts to speed up chemical reactions by lowering their activation energy. They work through a lock-and-key mechanism where the enzyme and substrate physically fit together. This binding allows the enzyme to facilitate the reaction. Enzyme function can be inhibited through competitive inhibitors, which bind to the active site, or noncompetitive inhibitors, which induce a conformational change in the enzyme preventing substrate binding. Environmental factors like temperature, pH, and salt concentration can also impact an enzyme's activity by causing it to denature.
3ero 4 enzymes mine
Enzymes are proteins that act as biological catalysts and speed up chemical reactions by lowering their activation energy. They have an active site that binds specifically to substrate molecules. The lock and key hypothesis states that the shape of the active site matches that of the substrate. Enzymes only work on specific substrates and are not used up in reactions. They are denatured and unable to function if the conditions of temperature or pH move outside their optimum ranges.
3.6 Enzymes
Enzymes are proteins that act as catalysts to speed up chemical reactions, having an active site that binds to substrates. The rate of enzyme-catalyzed reactions is affected by factors like temperature, pH, and substrate concentration that can impact the enzyme's structure and activity. Enzyme inhibitors interact with enzymes to reduce or stop their catalytic activity through competitive, noncompetitive, and end-product inhibition mechanisms.
Enzymes
Enzymes are protein molecules that act as biological catalysts. They specifically bind with substrate molecules to form enzyme-substrate complexes. Enzymes are not consumed in reactions but can be used repeatedly by lowering the activation energy required. Without enzymes, reactions would occur slowly as they require energy to break and reform chemical bonds. Enzymes achieve catalysis through an induced-fit model where the active site is flexible and molds closer to the substrate.
Enzymology
Enzymes are proteins that act as catalysts to accelerate chemical reactions in living organisms without being consumed in the process. They are highly specific and can only catalyze certain reactions. Most enzymes are proteins with tertiary and quaternary structures, while some complex enzymes also contain non-protein cofactors. Enzymes work by lowering the activation energy of reactions, making the conversion of reactants to products thermodynamically favorable.
Enzyme Inhibition
This document discusses enzyme inhibition and its classification. It describes that inhibitors bind to enzymes and interfere with their activity, classifying inhibition as reversible or irreversible. Reversible inhibition is further divided into competitive, non-competitive, and uncompetitive types depending on whether the inhibitor binds to the free enzyme or the enzyme-substrate complex. Irreversible inhibitors bind covalently and permanently destroy the active site.
Presentation of Enzyme inhibitaion
This document discusses different types of enzyme inhibition. It describes irreversible inhibitors that permanently block the active site through covalent bonding. Reversible inhibitors are further divided into competitive inhibitors that resemble the substrate and bind the active site, non-competitive inhibitors that bind elsewhere and induce conformational changes, and uncompetitive inhibitors that only bind the enzyme-substrate complex. Examples of each type are provided.
Physical CHEMISTRY
This document summarizes a seminar on enzymes presented by Miss. Neha Milind Dhansekhar. It defines enzymes and their role in accelerating chemical reactions. It describes the three main types of enzyme inhibitors - competitive, non-competitive, and uncompetitive - and provides graphs illustrating their effects. The document also discusses how pH and metal ions can affect enzyme activity, and defines regulatory enzymes which do not follow standard Michaelis-Menten kinetics.
Factors affecting enzyme activity
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.
Enzyme activity
This document discusses enzymes and their catalytic properties. It begins by explaining that enzymes are protein catalysts that speed up biochemical reactions by lowering their activation energy. It then discusses the chemical nature of enzymes as proteins made of amino acid chains. The document covers several factors that affect enzyme activity, such as temperature, pH, and concentration of enzymes and substrates. It also discusses enzyme specificity and inhibition. Key terms related to enzymes and their reactions are defined.
4 factors affecting enzyme action
This document discusses factors that affect enzyme action and rates of enzyme reactions. It covers several key points:
1) Enzyme reaction rates depend on substrate and product concentrations, temperature, pH, the presence of activators or inhibitors, and time.
2) Most enzymes follow Michaelis-Menten kinetics, where the affinity of the enzyme for the substrate is represented by the Michaelis constant Km.
3) Temperature, pH, substrate and product concentrations can all influence the shape of curves describing enzyme kinetics like Michaelis-Menten. Optimal temperatures and pH levels vary between enzymes.
4) Methods like double reciprocal plots, Dixon plots, and the Hill equation are used to further study
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Causes and treatment of chd
Coronary arteries supply blood to the heart muscles which require nutrients to contract and relax properly. Blockage of coronary arteries causes coronary heart disease, the leading cause of death, which can result in heart attacks, heart failure, or cardiac arrest. Risk factors for heart disease include smoking, poor diet, obesity, stress, high cholesterol, blood pressure, age, and physical inactivity. Treatment options are drug therapy with aspirin, surgical procedures like stents, angioplasty, or bypass surgery to reopen blocked arteries.
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Enzyme induction and repression
This document defines and provides examples of enzyme induction and enzyme repression. It explains that enzyme induction occurs when a molecule like a drug binds to and increases the metabolic activity of an enzyme. This can increase clearance of a concomitantly administered drug and reduce its efficacy. Enzyme repression occurs when effectors alter the configuration of the operator so that polymerase binding is less efficient or prevented. Understanding enzyme induction and repression is important for analyzing drug reactions, studying toxicity, and understanding various body reactions and hormone production or depletion.
Factors affecting enzyme activity
This document discusses 5 key factors that affect enzyme activity: the concentration of the enzyme and substrate, temperature, pH, and the presence of activators. It notes that enzyme activity increases with higher enzyme and substrate concentrations up to a maximum point, and with temperature up to 40ยฐC, beyond which the enzyme denatures. Activity also increases with pH up to an optimum level, and some enzymes require metal ions or other ions to function at optimal levels. Maintaining optimal levels of these factors is important to control enzyme activity.
Enzyme inhibition
Enzyme introduction, Enzyme inhibition, Irreversible inhibition, reversible inhibition, competitive inhibition, noncompetitive inhibition, uncompetitive inhibition, examples for different types of inhibition, uses of enzyme inhibition in medicinal purpose, allosteric enzymes, allosteric activation, allosteric inhibition, pictorial explanation, graphical explanation.
Enzymes
Enzymes speed up chemical reactions in cells by lowering the activation energy needed for reactions to occur. They are protein catalysts that are highly specific to their substrate. The induced fit theory updated the lock and key concept of enzyme-substrate binding by proposing that enzymes change shape upon substrate binding to stabilize the transition state of the reaction. Factors like pH, temperature, and enzyme denaturation can affect enzyme activity levels.
Enzymes 2018
Enzymes are biological catalysts that speed up chemical reactions without being changed or used up themselves. They are protein molecules with an active site that attaches to a specific substrate molecule. The key properties of enzymes are that they are specific, and their activity is affected by temperature and pH levels. The optimum temperature and pH are the levels at which an enzyme works best - outside these levels the enzyme can become denatured and lose its shape/function.
Enzymes
This powerpoint presentation talks about enzymes, specifically its functions, the different types according to its function, and the definition of enzyme activator and inhibitor. A picture diagram is also included to show the process of enzyme activity and as well as a table differentiating apoenzyme and coenzyme. The different factors that affects the enzyme activity are also explained and lastly, the other uses of enzyme in medicine, food and etc.The content of the powerpoint presentation has undergone a research through internet and the best answers has been selected for better understanding. The resources of all the research made that was in this presentation are acknowledged as shown in the Reference part of the slide.
Enzyme inhibition
Enzyme inhibition is explained with its kinetics, animations showing mechanism of inhibitors action, examples of inhibitors are explained in detail with Enzyme inhibited.
by Dr. N. Sivaranjani, MD
Factor effecting the rate enzyme catalysed reactions
This document discusses the effects of pH, substrate, and temperature on enzyme-catalyzed reactions. It explains that pH can alter the shape of the enzyme and substrate, preventing them from interacting. Each enzyme works best at its optimum pH. Higher substrate concentrations lead to more frequent collisions and higher reaction rates, up to saturation. Temperature initially increases reaction rate by providing more kinetic energy, but excessive heat can denature the enzyme permanently by altering its shape.
ัะตัะผะตะฝั ะฑะฐ ัาฏาฏะฝะธะน าฏะนะป ะฐะถะธะปะปะฐะณะฐะฐ Enzyme activity
Enzymes are globular proteins that act as biological catalysts to speed up metabolic reactions. They have an active site that fits a specific substrate perfectly. The active site binds the substrate and forms an enzyme-substrate complex to lower the activation energy needed for the reaction. An enzyme's activity and stability depend on factors like temperature, pH, enzyme concentration, and substrate concentration. Changes in these factors can affect the enzyme's shape and ability to bind substrates. Inhibitors also impact enzyme function by binding to the active site or elsewhere on the enzyme.
6 enzyme notes
Enzymes are proteins that act as catalysts to speed up chemical reactions by lowering their activation energy. They work through a lock-and-key mechanism where the enzyme and substrate physically fit together. This binding allows the enzyme to facilitate the reaction. Enzyme function can be inhibited through competitive inhibitors, which bind to the active site, or noncompetitive inhibitors, which induce a conformational change in the enzyme preventing substrate binding. Environmental factors like temperature, pH, and salt concentration can also impact an enzyme's activity by causing it to denature.
3ero 4 enzymes mine
Enzymes are proteins that act as biological catalysts and speed up chemical reactions by lowering their activation energy. They have an active site that binds specifically to substrate molecules. The lock and key hypothesis states that the shape of the active site matches that of the substrate. Enzymes only work on specific substrates and are not used up in reactions. They are denatured and unable to function if the conditions of temperature or pH move outside their optimum ranges.
3.6 Enzymes
Enzymes are proteins that act as catalysts to speed up chemical reactions, having an active site that binds to substrates. The rate of enzyme-catalyzed reactions is affected by factors like temperature, pH, and substrate concentration that can impact the enzyme's structure and activity. Enzyme inhibitors interact with enzymes to reduce or stop their catalytic activity through competitive, noncompetitive, and end-product inhibition mechanisms.
Enzymes
Enzymes are protein molecules that act as biological catalysts. They specifically bind with substrate molecules to form enzyme-substrate complexes. Enzymes are not consumed in reactions but can be used repeatedly by lowering the activation energy required. Without enzymes, reactions would occur slowly as they require energy to break and reform chemical bonds. Enzymes achieve catalysis through an induced-fit model where the active site is flexible and molds closer to the substrate.
Enzymology
Enzymes are proteins that act as catalysts to accelerate chemical reactions in living organisms without being consumed in the process. They are highly specific and can only catalyze certain reactions. Most enzymes are proteins with tertiary and quaternary structures, while some complex enzymes also contain non-protein cofactors. Enzymes work by lowering the activation energy of reactions, making the conversion of reactants to products thermodynamically favorable.
Enzyme Inhibition
This document discusses enzyme inhibition and its classification. It describes that inhibitors bind to enzymes and interfere with their activity, classifying inhibition as reversible or irreversible. Reversible inhibition is further divided into competitive, non-competitive, and uncompetitive types depending on whether the inhibitor binds to the free enzyme or the enzyme-substrate complex. Irreversible inhibitors bind covalently and permanently destroy the active site.
Presentation of Enzyme inhibitaion
This document discusses different types of enzyme inhibition. It describes irreversible inhibitors that permanently block the active site through covalent bonding. Reversible inhibitors are further divided into competitive inhibitors that resemble the substrate and bind the active site, non-competitive inhibitors that bind elsewhere and induce conformational changes, and uncompetitive inhibitors that only bind the enzyme-substrate complex. Examples of each type are provided.
Physical CHEMISTRY
This document summarizes a seminar on enzymes presented by Miss. Neha Milind Dhansekhar. It defines enzymes and their role in accelerating chemical reactions. It describes the three main types of enzyme inhibitors - competitive, non-competitive, and uncompetitive - and provides graphs illustrating their effects. The document also discusses how pH and metal ions can affect enzyme activity, and defines regulatory enzymes which do not follow standard Michaelis-Menten kinetics.
Factors affecting enzyme activity
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.
Enzyme activity
This document discusses enzymes and their catalytic properties. It begins by explaining that enzymes are protein catalysts that speed up biochemical reactions by lowering their activation energy. It then discusses the chemical nature of enzymes as proteins made of amino acid chains. The document covers several factors that affect enzyme activity, such as temperature, pH, and concentration of enzymes and substrates. It also discusses enzyme specificity and inhibition. Key terms related to enzymes and their reactions are defined.
4 factors affecting enzyme action
This document discusses factors that affect enzyme action and rates of enzyme reactions. It covers several key points:
1) Enzyme reaction rates depend on substrate and product concentrations, temperature, pH, the presence of activators or inhibitors, and time.
2) Most enzymes follow Michaelis-Menten kinetics, where the affinity of the enzyme for the substrate is represented by the Michaelis constant Km.
3) Temperature, pH, substrate and product concentrations can all influence the shape of curves describing enzyme kinetics like Michaelis-Menten. Optimal temperatures and pH levels vary between enzymes.
4) Methods like double reciprocal plots, Dixon plots, and the Hill equation are used to further study
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Factor effecting the rate enzyme catalysed reactions
Factor effecting the rate enzyme catalysed reactions
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ัะตัะผะตะฝั ะฑะฐ ัาฏาฏะฝะธะน าฏะนะป ะฐะถะธะปะปะฐะณะฐะฐ Enzyme activity
ัะตัะผะตะฝั ะฑะฐ ัาฏาฏะฝะธะน าฏะนะป ะฐะถะธะปะปะฐะณะฐะฐ Enzyme activity
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Soil is formed through the weathering of parent material such as bedrock. There are different types of parent material including residual material composed of igneous, sedimentary, and metamorphic rocks still located where they were formed. Transported parent material has been moved from its origin by forces like water, wind, glaciers or gravity. Soil formation breaks down parent material through weathering and adds organic matter over time to create distinct soil horizons capable of supporting plant growth.
Respiration
Respiration is a series of enzyme-controlled oxidation and reduction reactions where carbohydrates produced during photosynthesis are oxidized to carbon dioxide and oxygen is reduced to water. There are two types of respiration: aerobic respiration, which occurs in the presence of oxygen, and anaerobic respiration, which occurs in the absence of oxygen. Anaerobic respiration has two types - lactic acid fermentation and alcoholic fermentation. Glycolysis is the first step of respiration, occurring with or without oxygen. The Krebs cycle is another step where pyruvic acid from glycolysis undergoes further oxidation, producing carbon dioxide, NADH, FADH2, and ATP. The electron transport chain uses carriers like cytoch
Inflorescence 2
This document defines and describes different types of inflorescences (arrangements of flowers on a floral axis). It discusses solitary flowers, simple and compound inflorescences, racemose and cymose arrangements, and specific types including racemes, corymbs, umbels, spikes, catkins, heads, and more. Diagrams and examples are provided to illustrate the different inflorescence structures found across plant species.
Root morphology
Roots have several functions including anchoring the plant, absorbing water and minerals, storing food, and in some cases reproduction. There are two main types of roots - tap roots which elongate from the radicle and adventitious roots which arise from other parts of the plant like the stem. Tap roots can be fibrous, tuberous, or conical/napiform depending on characteristics like branching or swelling. Adventitious roots include subterranean, partly subterranean like stilt or prop roots, aerial roots which function in clinging or absorption, parasitic roots which absorb nutrients from a host plant, and aquatic roots.
Cycas
Cycas is a gymnosperm that reproduces both vegetatively and sexually. Vegetative reproduction occurs through adventitious buds on the stem base that develop into new plants. Sexual reproduction involves separate male and female plants that produce cones. Pollen from the male cone is transferred to female cones by wind. After fertilization, the ovule develops into a seed protected by a fleshy outer layer and stony middle layer. The seed germinates by rupturing at the micropyle and producing a radicle and plumule to form a new sporophyte plant.
Meiosis...
Meiosis is the cell cycle process by which germ cells divide to form gametes. It involves two rounds of cell division: Meiosis I and Meiosis II. During Meiosis I, homologous chromosomes pair and undergo recombination through crossover. The homologous chromosomes then separate, reducing the chromosome number by half. Meiosis II involves the separation of sister chromatids, resulting in four haploid daughter cells each with half the number of chromosomes of the original cell.
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Mule event processing models | MuleSoft Mysore Meetup #47
Mule event processing models | MuleSoft Mysore Meetup #47
Event Link:- https://meetups.mulesoft.com/events/details/mulesoft-mysore-presents-mule-event-processing-models/
Agenda
โ What is event processing in MuleSoft?
โ Types of event processing models in Mule 4
โ Distinction between the reactive, parallel, blocking & non-blocking processing
For Upcoming Meetups Join Mysore Meetup Group - https://meetups.mulesoft.com/mysore/YouTube:- youtube.com/@mulesoftmysore
Mysore WhatsApp group:- https://chat.whatsapp.com/EhqtHtCC75vCAX7gaO842N
Speaker:-
Shivani Yasaswi - https://www.linkedin.com/in/shivaniyasaswi/
Organizers:-
Shubham Chaurasia - https://www.linkedin.com/in/shubhamchaurasia1/
Giridhar Meka - https://www.linkedin.com/in/giridharmeka
Priya Shaw - https://www.linkedin.com/in/priya-shaw
Bossa Nโ Roll Records by Ismael Vazquez.
Bossa N Roll Records presentation by Izzy Vazquez for Music Retail and Distribution class at Full Sail University
Philippine Edukasyong Pantahanan at Pangkabuhayan (EPP) Curriculum
(๐๐๐ ๐๐๐) (๐๐๐ฌ๐ฌ๐จ๐ง ๐)-๐๐ซ๐๐ฅ๐ข๐ฆ๐ฌ
๐๐ข๐ฌ๐๐ฎ๐ฌ๐ฌ ๐ญ๐ก๐ ๐๐๐ ๐๐ฎ๐ซ๐ซ๐ข๐๐ฎ๐ฅ๐ฎ๐ฆ ๐ข๐ง ๐ญ๐ก๐ ๐๐ก๐ข๐ฅ๐ข๐ฉ๐ฉ๐ข๐ง๐๐ฌ:
- Understand the goals and objectives of the Edukasyong Pantahanan at Pangkabuhayan (EPP) curriculum, recognizing its importance in fostering practical life skills and values among students. Students will also be able to identify the key components and subjects covered, such as agriculture, home economics, industrial arts, and information and communication technology.
๐๐ฑ๐ฉ๐ฅ๐๐ข๐ง ๐ญ๐ก๐ ๐๐๐ญ๐ฎ๐ซ๐ ๐๐ง๐ ๐๐๐จ๐ฉ๐ ๐จ๐ ๐๐ง ๐๐ง๐ญ๐ซ๐๐ฉ๐ซ๐๐ง๐๐ฎ๐ซ:
-Define entrepreneurship, distinguishing it from general business activities by emphasizing its focus on innovation, risk-taking, and value creation. Students will describe the characteristics and traits of successful entrepreneurs, including their roles and responsibilities, and discuss the broader economic and social impacts of entrepreneurial activities on both local and global scales.
Chapter wise All Notes of First year Basic Civil Engineering.pptx
Chapter wise All Notes of First year Basic Civil Engineering
Syllabus
Chapter-1
Introduction to objective, scope and outcome the subject
Chapter 2
Introduction: Scope and Specialization of Civil Engineering, Role of civil Engineer in Society, Impact of infrastructural development on economy of country.
Chapter 3
Surveying: Object Principles & Types of Surveying; Site Plans, Plans & Maps; Scales & Unit of different Measurements.
Linear Measurements: Instruments used. Linear Measurement by Tape, Ranging out Survey Lines and overcoming Obstructions; Measurements on sloping ground; Tape corrections, conventional symbols. Angular Measurements: Instruments used; Introduction to Compass Surveying, Bearings and Longitude & Latitude of a Line, Introduction to total station.
Levelling: Instrument used Object of levelling, Methods of levelling in brief, and Contour maps.
Chapter 4
Buildings: Selection of site for Buildings, Layout of Building Plan, Types of buildings, Plinth area, carpet area, floor space index, Introduction to building byelaws, concept of sun light & ventilation. Components of Buildings & their functions, Basic concept of R.C.C., Introduction to types of foundation
Chapter 5
Transportation: Introduction to Transportation Engineering; Traffic and Road Safety: Types and Characteristics of Various Modes of Transportation; Various Road Traffic Signs, Causes of Accidents and Road Safety Measures.
Chapter 6
Environmental Engineering: Environmental Pollution, Environmental Acts and Regulations, Functional Concepts of Ecology, Basics of Species, Biodiversity, Ecosystem, Hydrological Cycle; Chemical Cycles: Carbon, Nitrogen & Phosphorus; Energy Flow in Ecosystems.
Water Pollution: Water Quality standards, Introduction to Treatment & Disposal of Waste Water. Reuse and Saving of Water, Rain Water Harvesting. Solid Waste Management: Classification of Solid Waste, Collection, Transportation and Disposal of Solid. Recycling of Solid Waste: Energy Recovery, Sanitary Landfill, On-Site Sanitation. Air & Noise Pollution: Primary and Secondary air pollutants, Harmful effects of Air Pollution, Control of Air Pollution. . Noise Pollution Harmful Effects of noise pollution, control of noise pollution, Global warming & Climate Change, Ozone depletion, Greenhouse effect
Text Books:
1. Palancharmy, Basic Civil Engineering, McGraw Hill publishers.
2. Satheesh Gopi, Basic Civil Engineering, Pearson Publishers.
3. Ketki Rangwala Dalal, Essentials of Civil Engineering, Charotar Publishing House.
4. BCP, Surveying volume 1
Andreas Schleicher presents PISA 2022 Volume III - Creative Thinking - 18 Jun...
Andreas Schleicher, Director of Education and Skills at the OECD presents at the launch of PISA 2022 Volume III - Creative Minds, Creative Schools on 18 June 2024.
Level 3 NCEA - NZ: A Nation In the Making 1872 - 1900 SML.ppt
The History of NZ 1870-1900.
Making of a Nation.
From the NZ Wars to Liberals,
Richard Seddon, George Grey,
Social Laboratory, New Zealand,
Confiscations, Kotahitanga, Kingitanga, Parliament, Suffrage, Repudiation, Economic Change, Agriculture, Gold Mining, Timber, Flax, Sheep, Dairying,
BรI TแบฌP Dแบ Y THรM TIแบพNG ANH LแปP 7 Cแบข NฤM FRIENDS PLUS SรCH CHรN TRแปI SรNG Tแบ O ...
BรI TแบฌP Dแบ Y THรM TIแบพNG ANH LแปP 7 Cแบข NฤM FRIENDS PLUS SรCH CHรN TRแปI SรNG Tแบ O ...Nguyen Thanh Tu Collection
https://app.box.com/s/qhtvq32h4ybf9t49ku85x0n3xl4jhr15ย
How to deliver Powerpoint Presentations.pptx
"How to make and deliver dynamic presentations by making it more interactive to captivate your audience attention"
Wound healing PPT
This document provides an overview of wound healing, its functions, stages, mechanisms, factors affecting it, and complications.
A wound is a break in the integrity of the skin or tissues, which may be associated with disruption of the structure and function.
Healing is the bodyโs response to injury in an attempt to restore normal structure and functions.
Healing can occur in two ways: Regeneration and Repair
There are 4 phases of wound healing: hemostasis, inflammation, proliferation, and remodeling. This document also describes the mechanism of wound healing. Factors that affect healing include infection, uncontrolled diabetes, poor nutrition, age, anemia, the presence of foreign bodies, etc.
Complications of wound healing like infection, hyperpigmentation of scar, contractures, and keloid formation.
skeleton System.pdf (skeleton system wow)
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ุฏ ุงูุฐูุจู ๐๐
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ุตุญู ุงููุฑุงุกุงุช ุงูุนุดุฑ ุฃุนุฏ ุฃุญุฑู ุงูุฎูุงู ุณู
ูุฑ ุจุณูููู.pdf
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ุตุญู ุงููุฑุงุกุงุช ุงูุนุดุฑ ุฃุนุฏ ุฃุญุฑู ุงูุฎูุงู ุณู
ูุฑ ุจุณูููู.pdfุณู
ูุฑ ุจุณูููู
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ุตุญู ุฃุญุฑู ุงูุฎูุงู ูููุฑุงุก ุงูุนุดุฑุฉุฃุนุฏ ุฃุญุฑู ุงูุฎูุงู ุจุงูุชูููู ูุตูุง ุณู
ูุฑ ุจุณูููู ุบูุฑ ุงููู ููย
Geography as a Discipline Chapter 1 __ Class 11 Geography NCERT _ Class Notes...
Geography as discipline
Beyond Degrees - Empowering the Workforce in the Context of Skills-First.pptx
Ivรกn Bornacelly, Policy Analyst at the OECD Centre for Skills, OECD, presents at the webinar 'Tackling job market gaps with a skills-first approach' on 12 June 2024
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ย
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ุตุญู ุงููุฑุงุกุงุช ุงูุนุดุฑ ุฃุนุฏ ุฃุญุฑู ุงูุฎูุงู ุณู
ูุฑ ุจุณูููู.pdf
ู
ุตุญู ุงููุฑุงุกุงุช ุงูุนุดุฑ ุฃุนุฏ ุฃุญุฑู ุงูุฎูุงู ุณู
ูุฑ ุจุณูููู.pdf
ย
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Chapter 3
- 3. Enzymes
- 4. cofactor
- 6. Haem portion as cofactor
- 7. Mechanism of enzyme action
- 8. Models of enzyme action Lock and Key model
- 10. Factor effecting rate of enzyme action ๏ต Substrate concentration ๏ต Enzyme concentration ๏ต Effect of temperature ๏ต Effect of pH
- 12. Inhibitors
- 14. Related video