Topic 4 chapter 5 part 3 enzymes - limiting factors
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This document discusses limiting factors in enzyme activity. It provides two examples: 1) As substrate concentration increases, the reaction rate increases until all enzyme sites are occupied. Then the substrate becomes the limiting factor. 2) Doubling the enzyme concentration doubles the reaction rate. Beyond the point where all substrate is bound, the enzyme becomes the limiting factor. The key points are that a limiting factor is the component that determines the reaction rate, and this can change from substrate to enzyme depending on their relative concentrations.
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FACTORS AFFECTING ENZYME ACTIVITY
Enzymes are proteins that catalyze chemical reactions and increase reaction rates. Several factors affect enzyme function, including enzyme concentration, substrate concentration, temperature, pH, inhibitors, activators, and salinity. Enzyme activity is highest when conditions are optimal for maintaining the enzyme's three-dimensional structure. Temperature and pH that are too high or low can cause enzymes to denature by disrupting bonds and changing their shape. Inhibitors also decrease reaction rates by competing with substrates or altering the enzyme's structure.
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Enzymes have optimal conditions for activity, including temperature and pH. At their optimal temperature, usually 37°C for human enzymes, and pH, around 7.4 for enzymes in the body, enzymes show the highest reaction rates. Deviating from these optimal conditions, such as increasing or decreasing the temperature or changing the pH, reduces the enzyme's activity and reaction rate. Factors like substrate concentration and inhibitors can also affect an enzyme's reaction rate.
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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.
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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
FACTOR AFFECTING ENZYME -CATALYZED REACTION
PREPARED BY: MUHAMMAD ARIFF B. MAHDZUB
BACHELOR MEDICINE AND SURGERY (MBBS)
UNIVERSITY COLLEGE SHAHPUTRA, KUANTAN
Enzymalogy Factors affecting enzyme activity and kinetics
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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.
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The document summarizes key concepts in cell biology related to enzymes. It defines important terms like metabolism, enzyme, substrate, and coenzyme. It describes the roles of enzymes in biochemical reactions and factors that affect their activity, such as pH, temperature, substrate concentration, and inhibitors. Lastly, it discusses experimental design and the scientific method.
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FACTORS AFFECTING ENZYME ACTIVITY
Enzymes are proteins that catalyze chemical reactions and increase reaction rates. Several factors affect enzyme function, including enzyme concentration, substrate concentration, temperature, pH, inhibitors, activators, and salinity. Enzyme activity is highest when conditions are optimal for maintaining the enzyme's three-dimensional structure. Temperature and pH that are too high or low can cause enzymes to denature by disrupting bonds and changing their shape. Inhibitors also decrease reaction rates by competing with substrates or altering the enzyme's structure.
CHM 105-16_8 Factors Affecting Enzyme Activity
Enzymes have optimal conditions for activity, including temperature and pH. At their optimal temperature, usually 37°C for human enzymes, and pH, around 7.4 for enzymes in the body, enzymes show the highest reaction rates. Deviating from these optimal conditions, such as increasing or decreasing the temperature or changing the pH, reduces the enzyme's activity and reaction rate. Factors like substrate concentration and inhibitors can also affect an enzyme's reaction rate.
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
FACTOR AFFECTING ENZYME -CATALYZED REACTION
PREPARED BY: MUHAMMAD ARIFF B. MAHDZUB
BACHELOR MEDICINE AND SURGERY (MBBS)
UNIVERSITY COLLEGE SHAHPUTRA, KUANTAN
Enzymalogy Factors affecting enzyme activity and kinetics
A comprehensive presentation on Factors affecting enzyme activity & Kinetics of Enzymes for MBBS ,BDS, B Pharm & Biotechnology students to facilitate self- study.
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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.
Enzymes
The document summarizes key concepts in cell biology related to enzymes. It defines important terms like metabolism, enzyme, substrate, and coenzyme. It describes the roles of enzymes in biochemical reactions and factors that affect their activity, such as pH, temperature, substrate concentration, and inhibitors. Lastly, it discusses experimental design and the scientific method.
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The document discusses key concepts about enzymes and catalysts including:
1. Catalysts speed up chemical reactions without being changed themselves. Enzymes are biological catalysts that help break down or build up molecules in living things.
2. Each enzyme has a unique 3D shape that allows it to bind specifically to one substrate. The active site is where this binding occurs.
3. Enzymes can catalyze both breakdown reactions, which break large molecules into smaller ones, and synthesis reactions, which build small molecules into larger ones.
4. The optimum temperature and pH are the conditions under which an enzyme works best. Changing conditions can cause the enzyme to denature and lose its shape/
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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 catalysts to speed up biological reactions by lowering the activation energy needed. They have specific active sites that substrates bind to, either breaking substrates apart or joining them together. The structure of the active site determines the specific substrate an enzyme can act on. While the lock and key model depicted a simple binding, the induced fit model better explains how enzymes and substrates may slightly change shape to promote reactions. Environmental factors like temperature, pH, and cofactors can impact an enzyme's activity by potentially denaturing its structure.
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 40°C, 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.
factors affecting enzyme activity
This document discusses the effects of various factors on enzyme activity. It describes how raising the temperature increases reaction rates by increasing kinetic energy until the enzyme denatures. Most human enzymes are stable up to 35-40°C while thermophilic bacterial enzymes can withstand over 100°C. It also discusses how pH, substrate concentration, enzyme concentration, product concentration, and inhibitors like competitive and noncompetitive inhibitors affect reaction rates. Competitive inhibitors bind the active site while noncompetitive inhibitors bind elsewhere and decrease Vmax. Examples of drug inhibitors are also provided.
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This document summarizes key concepts about enzymes including:
1) Enzymes work as catalysts to lower the activation energy of biochemical reactions and increase reaction rates. They specifically bind to substrates in their active sites.
2) Environmental factors like temperature and pH can impact enzyme activity by causing enzyme denaturation at extreme levels.
3) Enzyme activity is regulated by various mechanisms including allosteric regulation, covalent modification through phosphorylation, and proteolytic activation of zymogens to active enzymes.
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.
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The key factors that affect enzyme activity are the concentrations of the enzyme and substrate, temperature, pH, and presence of inhibitors or activators. Specifically, enzyme activity increases with higher enzyme and substrate concentrations up to a point, works best within a narrow temperature and pH range, and can be reduced by excess reaction products or radiation exposure. Certain enzymes also require metal ions like magnesium or zinc to function properly.
Enzymes
- Enzymes are biological catalysts made of proteins that speed up chemical reactions without being changed themselves. They work by lowering the activation energy required for reactions.
- Enzymes have an active site where substrates bind specifically. The enzyme-substrate complex leads to products. Enzyme activity is affected by temperature and pH. They are most active at optimal temperatures and pH levels.
- Enzymes catalyze both the breaking down of large molecules and building up of complex molecules from simpler ones. They are required in small amounts and can catalyze reversible reactions.
Bisubstrate reactions enzyme kinetics
This document discusses two types of bisubstrate reactions: sequential or single-displacement reactions and ping-pong or double-displacement reactions. Sequential reactions involve both substrates binding to the enzyme before products are released, and can be ordered or random. Ping-pong reactions involve one substrate binding and being modified, then releasing one product before the second substrate binds and the second product is released, regenerating the original enzyme. Examples of each type of reaction are provided to illustrate the mechanisms.
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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.
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.
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Enzymes regulate chemical pathways in cells and lower the activation energy of reactions, increasing reaction rates. Enzymes have an active site that binds to substrates, catalyzing the reaction to form products. Factors like pH, temperature, and inhibitors can impact an enzyme's activity by changing its shape. Feedback inhibition regulates metabolic pathways by inhibiting enzymes when product concentrations are high.
Chapter 5 enzymes
Enzymes are proteins that catalyze chemical reactions without being altered themselves. They speed up reactions by lowering activation energy. Enzymes work most efficiently at a specific temperature and pH, and require cofactors to function. Enzyme activity is affected by substrate, temperature, pH, and other limiting factors. Enzymes are classified based on the type of reaction they catalyze, such as hydrolysis or oxidation-reduction.
Enzymes powerpoint for 27th may y12 bio
Enzymes are biological catalysts that speed up chemical reactions without being used up in the process. They do this by lowering the activation energy of reactions, allowing substrates to more easily bind and undergo chemical transformations into product molecules. Enzymes have an active site that binds specifically to substrates and induces a shape change that brings reactants together to form new compounds.
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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.
Enzymes IBDP HL
Enzymes are protein molecules that catalyze biological reactions. They work by lowering the activation energy of reactions, allowing more molecules to react. Enzymes are highly specific and their tertiary structure forms an active site that binds substrates. Inhibitors can bind the active site and prevent substrate binding (competitive) or bind elsewhere and alter the enzyme shape (non-competitive). The rate of enzyme reactions saturates at high substrate concentrations as active sites fill.
INHIBITION OF ENZYME ACTION
CONTENT :-
1.Introduction
2.What is Enzymes ?
3.Enzyme activation by metal ion derivations & graphs
4.What is Regulate ?
5.Enzyme Regulation
6.Types of Regulation
7. Regulatory Enzymes derivations & graphs.
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The document discusses factors that affect enzyme-catalyzed reactions, including substrate concentration, inhibitors, pH, temperature, and pressure. It explains how the reaction rate depends on substrate and enzyme concentrations and can be influenced by activators and inhibitors. It also describes how each enzyme has an optimal pH range and temperature, and discusses how temperature affects reaction rates, microbial growth rates, and thermal inactivation of enzymes.
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The document discusses key concepts about enzymes and catalysts including:
1. Catalysts speed up chemical reactions without being changed themselves. Enzymes are biological catalysts that help break down or build up molecules in living things.
2. Each enzyme has a unique 3D shape that allows it to bind specifically to one substrate. The active site is where this binding occurs.
3. Enzymes can catalyze both breakdown reactions, which break large molecules into smaller ones, and synthesis reactions, which build small molecules into larger ones.
4. The optimum temperature and pH are the conditions under which an enzyme works best. Changing conditions can cause the enzyme to denature and lose its shape/
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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.
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Enzymes are protein molecules that act as catalysts to speed up biological reactions by lowering the activation energy needed. They have specific active sites that substrates bind to, either breaking substrates apart or joining them together. The structure of the active site determines the specific substrate an enzyme can act on. While the lock and key model depicted a simple binding, the induced fit model better explains how enzymes and substrates may slightly change shape to promote reactions. Environmental factors like temperature, pH, and cofactors can impact an enzyme's activity by potentially denaturing its structure.
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 40°C, 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.
factors affecting enzyme activity
This document discusses the effects of various factors on enzyme activity. It describes how raising the temperature increases reaction rates by increasing kinetic energy until the enzyme denatures. Most human enzymes are stable up to 35-40°C while thermophilic bacterial enzymes can withstand over 100°C. It also discusses how pH, substrate concentration, enzyme concentration, product concentration, and inhibitors like competitive and noncompetitive inhibitors affect reaction rates. Competitive inhibitors bind the active site while noncompetitive inhibitors bind elsewhere and decrease Vmax. Examples of drug inhibitors are also provided.
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This document summarizes key concepts about enzymes including:
1) Enzymes work as catalysts to lower the activation energy of biochemical reactions and increase reaction rates. They specifically bind to substrates in their active sites.
2) Environmental factors like temperature and pH can impact enzyme activity by causing enzyme denaturation at extreme levels.
3) Enzyme activity is regulated by various mechanisms including allosteric regulation, covalent modification through phosphorylation, and proteolytic activation of zymogens to active enzymes.
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.
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The key factors that affect enzyme activity are the concentrations of the enzyme and substrate, temperature, pH, and presence of inhibitors or activators. Specifically, enzyme activity increases with higher enzyme and substrate concentrations up to a point, works best within a narrow temperature and pH range, and can be reduced by excess reaction products or radiation exposure. Certain enzymes also require metal ions like magnesium or zinc to function properly.
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- Enzymes are biological catalysts made of proteins that speed up chemical reactions without being changed themselves. They work by lowering the activation energy required for reactions.
- Enzymes have an active site where substrates bind specifically. The enzyme-substrate complex leads to products. Enzyme activity is affected by temperature and pH. They are most active at optimal temperatures and pH levels.
- Enzymes catalyze both the breaking down of large molecules and building up of complex molecules from simpler ones. They are required in small amounts and can catalyze reversible reactions.
Bisubstrate reactions enzyme kinetics
This document discusses two types of bisubstrate reactions: sequential or single-displacement reactions and ping-pong or double-displacement reactions. Sequential reactions involve both substrates binding to the enzyme before products are released, and can be ordered or random. Ping-pong reactions involve one substrate binding and being modified, then releasing one product before the second substrate binds and the second product is released, regenerating the original enzyme. Examples of each type of reaction are provided to illustrate the mechanisms.
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.
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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.
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Enzymes regulate chemical pathways in cells and lower the activation energy of reactions, increasing reaction rates. Enzymes have an active site that binds to substrates, catalyzing the reaction to form products. Factors like pH, temperature, and inhibitors can impact an enzyme's activity by changing its shape. Feedback inhibition regulates metabolic pathways by inhibiting enzymes when product concentrations are high.
Chapter 5 enzymes
Enzymes are proteins that catalyze chemical reactions without being altered themselves. They speed up reactions by lowering activation energy. Enzymes work most efficiently at a specific temperature and pH, and require cofactors to function. Enzyme activity is affected by substrate, temperature, pH, and other limiting factors. Enzymes are classified based on the type of reaction they catalyze, such as hydrolysis or oxidation-reduction.
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Enzymes are biological catalysts that speed up chemical reactions without being used up in the process. They do this by lowering the activation energy of reactions, allowing substrates to more easily bind and undergo chemical transformations into product molecules. Enzymes have an active site that binds specifically to substrates and induces a shape change that brings reactants together to form new compounds.
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Definition, Classification, Models of enzyme activity, Enzyme specificity, Factors affecting enzyme activity, Enzyme inhibition, Isoenzyme, Allosteric enzyme, Application, etc.
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.
Enzymes IBDP HL
Enzymes are protein molecules that catalyze biological reactions. They work by lowering the activation energy of reactions, allowing more molecules to react. Enzymes are highly specific and their tertiary structure forms an active site that binds substrates. Inhibitors can bind the active site and prevent substrate binding (competitive) or bind elsewhere and alter the enzyme shape (non-competitive). The rate of enzyme reactions saturates at high substrate concentrations as active sites fill.
INHIBITION OF ENZYME ACTION
CONTENT :-
1.Introduction
2.What is Enzymes ?
3.Enzyme activation by metal ion derivations & graphs
4.What is Regulate ?
5.Enzyme Regulation
6.Types of Regulation
7. Regulatory Enzymes derivations & graphs.
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Apec workshop 2 presentation 5 e apec workshop mexico capture technologies ...
Apec workshop 2 presentation 5 e apec workshop mexico capture technologies ...
Principles pertaining to limiting factors and ecological assessment
Principles pertaining to limiting factors and ecological assessment
Similar to Topic 4 chapter 5 part 3 enzymes - limiting factors
BIOLOGY FORM 4 CHAPTER 4 - CHEMICAL COMPOSITION OF THE CELL PART 2
1. Enzymes speed up chemical reactions in cells by lowering the activation energy needed, allowing reactions to occur more quickly.
2. They are highly specific and each enzyme catalyzes only one reaction. Enzymes have an active site that allows only specific substrates to bind.
3. Many factors can affect enzyme activity, including temperature, pH, substrate and enzyme concentration, and presence of cofactors or inhibitors. Enzymes function best within a limited range of conditions.
ENZYME INHIBITION & FACTORS AFFECTING THE VELOCITY OF ENZYME ACTION
This document discusses several key factors that affect enzyme activity:
1. Enzyme and substrate concentration - Reaction rate increases with increasing concentrations of enzyme and substrate up to a maximum.
2. Temperature and pH - Enzymes have optimal temperatures and pH levels for activity. Outside these ranges, activity decreases.
3. Inhibitors and activators - Substances that bind enzymes can inhibit or activate their activity, altering reaction rates. Common types of inhibitors are competitive, non-competitive, and uncompetitive.
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.
biology-presentation.pdf
Increasing the concentration of substrate while keeping the concentration of enzymes fixed leads to an increased reaction rate and more products being created. A higher substrate concentration means more opportunities for effective collisions between substrate and enzyme molecules. The reaction rate increases until it reaches a maximum level where all of the enzyme active sites are saturated with substrate and further increases in substrate concentration will not impact the reaction rate.
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.
100 10enzyme kineticscomm
1. The document discusses favorite winter activities like skiing, snowball fights, and building snowmen and forts.
2. It also mentions flying south as an option.
3. The document provides a brief list of winter activities but does not analyze them in detail.
ENZYMES
This document provides an introduction and overview of enzymes. It defines enzymes as biocatalysts that increase the rate of chemical reactions without being changed themselves. It classifies enzymes into six main categories and lists some key properties of enzymes. The document then discusses several factors that can affect enzyme activity, such as concentration, pH, temperature, and substrate concentration. It also describes the active site of enzymes and the lock and key model and induced fit hypothesis for the mechanism of enzyme action. Finally, it outlines some common applications of enzymes in medical, analytical, manipulative, and industrial uses.
2 Enzymes lec .ppt
Enzymes catalyze chemical reactions through their active sites, which bind specifically to substrate molecules. The "lock and key" and "induced fit" models describe this binding. The basic mechanism involves formation of an enzyme-substrate complex, followed by product release. Enzyme activity is affected by concentration, temperature, pH, and inhibitors. Optimum activity occurs within a limited range for each factor to prevent denaturation. Inhibitors can be competitive, noncompetitive, or uncompetitive, and reversible or irreversible.
2.Enzymjvohxutzohcoyfpufoyfpuffpupfoyf85s0utdputses I II.pptx
This document discusses enzymes and their regulation. It defines enzymes as proteins that catalyze biochemical reactions without being consumed in the process. Enzymes contain an active site where substrates bind and reactions occur. Several cofactors like coenzymes and metal ions can be involved. Enzyme activity is affected by factors like temperature, pH, and substrate and inhibitor concentrations. The Michaelis-Menten kinetics describe how reaction velocity changes with substrate levels. Enzymes are regulated through various mechanisms like allosteric regulation, covalent modification, and controlling enzyme synthesis. Feedback inhibition allows pathways to regulate their end products.
2.Enzymjvohxutzohcoyfpufoyfpuffpupfoyf85s0utdputses I II.pptx
This document discusses enzymes and their regulation. It defines enzymes as proteins that catalyze biochemical reactions without being consumed in the process. Enzymes contain an active site where substrates bind and reactions occur. Several cofactors like coenzymes and metal ions can be involved. Enzyme activity is affected by factors like temperature, pH, and substrate and inhibitor concentrations. The Michaelis-Menten kinetics describe how reaction velocity changes with substrate levels. Enzymes are regulated through various mechanisms like allosteric regulation, covalent modification, and controlling enzyme synthesis. Feedback inhibition allows pathways to regulate their end products.
Enzyme kinetics
1) Chemical kinetics describes relationships between reaction rates and concentrations of reactants and products. Enzyme kinetics follows Michaelis-Menten kinetics which describes reaction rates at varying substrate concentrations.
2) The Michaelis-Menten equation models reaction rates as substrate concentration increases, with an initial linear increase until reaching the maximum reaction rate (Vmax) at substrate saturation.
3) The Michaelis constant KM represents the substrate concentration at half Vmax and indicates an enzyme's affinity for its substrate. Lower KM means higher affinity.
enzme kinetics.pptx
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.
3) It also discusses factors that affect enzyme activity such as temperature, pH, and enzyme inhibitors, distinguishing between competitive, uncompetitive, and noncompetitive inhibition.
Biochemistry lab reporttt
This document is a lab report that examines the effect of substrate concentration on enzyme kinetics. The introduction provides background on how enzyme concentration and reaction order affect the reaction rate. Specifically, it explains that a zero-order reaction rate is independent of substrate concentration. The methods section describes the experiment, which used potato as an enzyme source to catalyze the breakdown of hydrogen peroxide at different substrate concentrations. Results are presented in a graph, and the discussion section analyzes how enzymes function as catalysts to speed chemical reactions.
225377 lecture 19 20
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.
1. Enzyme chemistrynnnnnnnnjjjnjnnnnn.ppt
Enzymes are protein catalysts that accelerate chemical reactions by lowering their activation energy. They are highly specific and function most efficiently at their optimal temperature and pH. Some enzymes require cofactors like coenzymes to function. Enzyme activity can be regulated by inhibitors and allosteric regulation. Enzymes speed up reactions but are not consumed in the process, allowing them to catalyze many turns of a reaction.
Enzyme kinetics by Pranjal Sharma
The document discusses enzymes kinetics and provides details about enzymes. It defines enzymes as proteins that act as biological catalysts and accelerate chemical reactions. It describes the lock and key theory and induced fit theory of how enzymes bind to substrates. It explains the three phases of enzyme kinetics - pre-steady state, steady state, and post-steady state. It also discusses factors that affect enzyme activity like substrate concentration, temperature, and pH. The Michaelis-Menten kinetics model and equation are explained. Finally, it provides examples of applications of studying enzyme kinetics.
L4 Enzymes_c0ce65815f13d03a89ba6bc6e59f7ab4.pptx
Catalase is an enzyme that catalyzes the decomposition of hydrogen peroxide into oxygen and water. Hydrogen peroxide is a harmful byproduct produced through normal metabolic processes. Catalase works at its optimum temperature of 37°C to quickly convert hydrogen peroxide before it can cause damage. If the temperature is increased above 100°C, catalase activity and the reaction rate would decrease due to enzyme denaturation at high temperatures.
Chapter 5 Enzymes Lesson 2 - Characteristics of enzymes
Enzymes found in biological washing powders help clean clothes by breaking down stains. Enzymes work best within a certain temperature and pH range, and can become denatured outside of this range, losing their effectiveness. Different enzymes have different optimal conditions, so washing powders may contain enzymes that function at higher temperatures to remove tougher stains.
KGF-Chapter 2-Kinetics.pptx
This document provides an introduction to chemical kinetics. It defines chemical kinetics as the study of reaction rates and mechanisms. Reaction rates are measured as changes in concentration over time and can be determined by monitoring reactants or products. The rate of a reaction is affected by factors like temperature, concentration, catalysts, and surface area. Rate laws relate the rate of reaction to concentrations and are determined experimentally. Elementary reactions make up reaction mechanisms, and the slowest step is rate-determining. The Arrhenius equation models the temperature dependence of reaction rates. Hess's law allows calculating enthalpy changes indirectly. Surfactants reduce surface tension and stabilize bubbles and emulsions.
Factors affecting enzymatic activities of substrate
Factors which affect enzymatic functioning [1:37 am, 16/02/2024] Ajmal: Uncouplers of Oxidative
Phosphorylation:
• Uncouplers can
be defined as A substance
that uncouples phosphorylation of ADP from electron
transfer. • Uncoupling agents are compounds which dissociate the synthesis of ATP from the transport of electrons
through the cytochrome system. • This means that the electron transport continues to function, leading to oxygen consumption but
phosphorylation of ADP is inhibited.
[1:38 am, 16/02/2024] Ajmal: 2,4-Dinitrophenol:
• A classic uncoupler of oxidative phosphorylation.
• was used as a weight-loss agent in the 1930s • The substance carries protons across the inner mitochondria
membrane. • In the presence of these uncouplers, electron transport from NADH to O, proceeds normally, but ATP is not formed by the
nitochondria.
• Body temperature is elevated as a result of hyper metabolism. • When phosphorylation is uncoupled from electron flow, a decrease in the proton gradient across the inner mitochondrial
membrane and, therefore, impaired ATP synthesis is expected. • In an attempt to compensate for this defect in energy capture,
metabolism and electron flow to oxygen is increased. • This hyper metabolism will be accompanied by elevated body temperature be cause the energy in fuels is largely wasted,
appearing as heat.
[1:38 am, 16/02/2024] Ajmal: Dicoumarol (Vitamin.K analogue):
• Used as anticoagulant.
Calcium:
• Transport of Cat ion into mitochondria can cause uncoupling. • Mitochondrial transport of Cat is energetically coupled to
oxidative phosphorylation.
• It is coupled with uptake of pi
• When calcium is
transported into mitochondria, electron transport can proceed but energy is required to pump the4 Ca+2
into the mitochondria. Hence, no energy is stored as ATP.
CCCP (Chloro carbonyl cyanide phenyl hydrazone):
• Most active uncoupler • These lipid soluble substances can carry protons across the inner
mitochondrial membrane.
[1:39 am, 16/02/2024] Ajmal: Dicoumarol (Vitamin.K analogue):
• Used as anticoagulant.
Calcium:
• Transport of Cat ion into mitochondria can cause uncoupling. • Mitochondrial transport of Cat is energetically coupled to
oxidative phosphorylation.
• It is coupled with uptake of pi
• When calcium is
transported into mitochondria, electron transport can proceed but energy is required to pump the4 Ca+2
into the mitochondria. Hence, no energy is stored as ATP.
CCCP (Chloro carbonyl cyanide phenyl hydrazone):
• Most active uncoupler • These lipid soluble substances can carry protons across the inner
mitochondrial membrane
Similar to Topic 4 chapter 5 part 3 enzymes - limiting factors (20)
BIOLOGY FORM 4 CHAPTER 4 - CHEMICAL COMPOSITION OF THE CELL PART 2
BIOLOGY FORM 4 CHAPTER 4 - CHEMICAL COMPOSITION OF THE CELL PART 2
ENZYME INHIBITION & FACTORS AFFECTING THE VELOCITY OF ENZYME ACTION
ENZYME INHIBITION & FACTORS AFFECTING THE VELOCITY OF ENZYME ACTION
2.Enzymjvohxutzohcoyfpufoyfpuffpupfoyf85s0utdputses I II.pptx
2.Enzymjvohxutzohcoyfpufoyfpuffpupfoyf85s0utdputses I II.pptx
2.Enzymjvohxutzohcoyfpufoyfpuffpupfoyf85s0utdputses I II.pptx
2.Enzymjvohxutzohcoyfpufoyfpuffpupfoyf85s0utdputses I II.pptx
Chapter 5 Enzymes Lesson 2 - Characteristics of enzymes
Chapter 5 Enzymes Lesson 2 - Characteristics of enzymes
Factors affecting enzymatic activities of substrate
Factors affecting enzymatic activities of substrate
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Molecular genetics 1 win q
The document describes the process of inserting a human insulin gene into bacterial DNA through genetic engineering. First, the insulin gene is cut from human DNA using a restriction enzyme, leaving "sticky ends." A plasmid from bacteria is also cut with the same enzyme. The insulin gene and plasmid are mixed and joined together with the enzyme DNA ligase. The combined DNA is then inserted into E. coli bacteria through applying heat or electric shock to open pores in the bacterial membrane, allowing the plasmid to enter. The engineered bacteria now contains the human insulin gene and can produce human insulin protein.
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Chapter 10 respiration II
This document provides information about respiration and the effects of tobacco smoke on health. It begins by stating the learning objectives which are to describe the effect of lactic acid in muscles during exercise and the effects of tobacco smoke and its components (nicotine, tar, carbon monoxide) on health. It then discusses the differences between aerobic and anaerobic respiration, where they occur in the body, and what happens when muscles carry out anaerobic respiration due to not receiving enough oxygen during vigorous exercise. The document also describes how the body removes lactic acid and the harmful effects of tobacco smoke, such as chronic bronchitis, emphysema, and chronic obstructive pulmonary disease.
Chapter 10 respiration
Respiration is the process by which living cells break down food molecules like glucose to release energy. Aerobic respiration uses oxygen to completely oxidize glucose, producing more energy than anaerobic respiration which does not require oxygen. The human respiratory system evolved to efficiently bring oxygen into the body from the air and remove carbon dioxide through a network of organs including the lungs, trachea, and diaphragm.
Chapter 10 respiration
Respiration is the process by which living cells break down food molecules to release energy. Aerobic respiration requires oxygen and releases carbon dioxide, while anaerobic respiration does not require oxygen. Humans have developed respiratory systems to facilitate the exchange of these gases between the environment and cells. The human respiratory system includes the trachea, lungs, diaphragm, and other structures. Breathing is driven by contractions of the diaphragm and ribs, which increase the thoracic cavity's volume and draw air into the lungs. Exhalation occurs when these structures relax and the cavity's volume decreases, pushing air back out.
Chapter 9 transport in plants lecture
1) Water and minerals are transported from the roots to the leaves through xylem tissue. Water enters root hair cells through osmosis and moves cell to cell through the root cortex and xylem vessels up the stem.
2) Photosynthates are transported from the leaves to the rest of the plant through phloem tissue. Phloem is made of sieve tube cells that transport sugars and amino acids.
3) Xylem and phloem are arranged in vascular bundles in stems and leaves, and alternate with each other in roots. Transpiration through the stomata of leaves creates a transpiration pull that draws water up the xylem against gravity.
Transport in humans
The circulatory system transports blood, nutrients, gases, and wastes throughout the body. It consists of the heart, blood vessels, and blood. The heart has four chambers that pump blood through two circuits - pulmonary circulation to the lungs and systemic circulation to the rest of the body. Blood flows through the heart in a double circulation, passing through the heart twice with each complete circuit. The cardiac cycle involves the coordinated contraction and relaxation of the heart's chambers. Blood pressure varies within the heart and arteries over the cardiac cycle and between individuals based on factors like age and activity level.
Chapter 7 plant nutrition
Photosynthesis is the process by which plants convert light energy, carbon dioxide, and water into glucose and oxygen. It occurs in two stages: the light-dependent stage where light energy is absorbed by chlorophyll to split water into hydrogen and oxygen, and the light-independent stage where carbon dioxide and water are converted into glucose using the chemical energy produced in the first stage. Photosynthesis takes place in the chloroplasts located in the palisade mesophyll cells of leaves. The glucose produced can then be used by the plant for energy, converted into other organic compounds, or transported to other parts of the plant for storage.
4 digestion ppt lesson 4
The document discusses the process of assimilation and transport of digested food throughout the body. It defines assimilation as the distribution and use of digested food as an energy source or to build new cells. It describes how sugars, amino acids, and fats are transported via the hepatic portal vein to the liver and then throughout the body. It specifically explains that glucose is used by cells for energy, excess is stored as glycogen in the liver, and insulin stimulates the conversion of glucose to glycogen.
3 animal nutrition -_ppt_lesson_3_edited_2
The inner wall of the small intestine contains folds, villi, and microvilli that increase the surface area for absorption of nutrients. Blood capillaries transport sugars and amino acids away from the small intestine, while lacteals transport fatty acids and glycerol. The colon absorbs water and mineral salts from undigested materials, the rectum temporarily stores feces, and the anus expels feces through defecation.
2 animal nutrition -_lesson2_ppt_final (2)
The document describes the roles of the stomach, pancreas, liver, gallbladder, and sections of the small intestine in digesting nutrients and absorbing them. It explains that the stomach contains enzymes like pepsin that break down proteins and the pancreas and intestinal glands produce enzymes that further break down carbohydrates, proteins, and lipids in the small intestine. Finally, it states that the liver produces bile which is stored in the gallbladder and released to emulsify fats during digestion in the small intestine.
1 animal nutrition lesson1 new
Here are 3 key things I learned:
1. The digestive system breaks down food into smaller molecules through physical and chemical digestion to prepare nutrients for absorption into bloodstream.
2. The main organs of the digestive system include the mouth, esophagus, stomach, small intestine, pancreas, liver, gallbladder and large intestine.
3. Peristalsis is the wave-like contractions of muscles in the gut wall that help mix food with digestive juices and propel food along the alimentary canal.
I'm still a bit unsure about the specific enzymes involved in digesting each macronutrient (carbs, proteins, fats) in different parts of the digestive system. Reviewing that table
Topic 4 chapter 5 part 2 enzymes - characteristics of enzymes
Enzymes have several key characteristics:
1) They speed up chemical reactions by lowering the activation energy needed.
2) They are required in minute amounts and remain unchanged after reactions.
3) They are highly specific, with each enzyme having a unique three-dimensional structure that only binds complementary substrates.
Their activity is also affected by temperature and pH - they have optimal temperatures and pH levels at which they are most active, and are deactivated outside these ranges. Some enzymes also require co-factors to function or can catalyze reversible reactions.
Topic 4 chapter 5 part 1 enzymes - biological catalysts
This document discusses enzymes and their functions. It begins by defining enzymes as biological catalysts that are mainly proteins produced by living cells. Enzymes speed up chemical reactions without being changed themselves. The document then discusses how enzymes lower the activation energy of reactions, allowing reactions to proceed more quickly and efficiently at normal body temperatures. It provides examples of enzyme-catalyzed anabolic and catabolic reactions, including protein synthesis, photosynthesis, digestion, and cellular respiration. Finally, it classifies enzymes into hydrolases and oxidation-reduction enzymes and provides examples of each.
Topic 3 chapter 4 part 1 nutrients - full
1) The document discusses nutrients and their importance for organisms. It focuses on carbohydrates, fats, and proteins.
2) Carbohydrates include sugars, starches, and fibers and serve as energy sources. They are broken down through hydrolysis. Fats also provide energy and insulation. Proteins are made of amino acids and are essential for growth and repair.
3) Tests are described to identify carbohydrates, sugars, and fats in food. The properties and functions of nutrients are explained at the molecular level.
Chap3 movement of substances
Here are my thoughts on the scenarios:
Scenario 1: No, throwing the severed finger in the Coke drink is not the right thing to do. Coke is highly acidic and sugary, which would damage tissues and cells in the finger, preventing it from being reattached successfully. The best thing would be to wrap the finger in a clean cloth or sterile dressing and get it to the hospital as quickly as possible on ice to preserve it until a doctor can reattach it.
Scenario 2: No, drinking seawater is not the right thing to do and would be dangerous. Seawater contains a high concentration of salt, which would cause the body to lose more water through osmosis as it tries to dilute the salt
Cells
Cells are the basic units of life and come in two main types - animal cells and plant cells. Cells have several organelles that allow them to carry out essential functions. Organelles include the nucleus, cytoplasm, mitochondria, chloroplasts and cell membrane. In multicellular organisms, cells combine to form tissues like muscle and epithelial tissue. Multiple tissue types combine to create organs such as the heart and liver. Organ systems such as the circulatory and respiratory systems are made of different organs working together. The human body contains many organ systems that function as a whole to form a living organism.
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Topic 4 chapter 5 part 2 enzymes - characteristics of enzymes
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SAM4U, an SAP complimentary software asset management tool for customers, delivers a detailed and well-structured overview of license inventory and usage with a user-friendly interface. We offer a hosted, cost-effective, and performance-optimized SAM4U setup in the Skybuffer Cloud environment. You retain ownership of the system and data, while we manage the ABAP 7.58 infrastructure, ensuring fixed Total Cost of Ownership (TCO) and exceptional services through the SAP Fiori interface.
Main news related to the CCS TSI 2023 (2023/1695)
An English 🇬🇧 translation of a presentation to the speech I gave about the main changes brought by CCS TSI 2023 at the biggest Czech conference on Communications and signalling systems on Railways, which was held in Clarion Hotel Olomouc from 7th to 9th November 2023 (konferenceszt.cz). Attended by around 500 participants and 200 on-line followers.
The original Czech 🇨🇿 version of the presentation can be found here: https://www.slideshare.net/slideshow/hlavni-novinky-souvisejici-s-ccs-tsi-2023-2023-1695/269688092 .
The videorecording (in Czech) from the presentation is available here: https://youtu.be/WzjJWm4IyPk?si=SImb06tuXGb30BEH .
Ocean lotus Threat actors project by John Sitima 2024 (1).pptx
Ocean Lotus cyber threat actors represent a sophisticated, persistent, and politically motivated group that poses a significant risk to organizations and individuals in the Southeast Asian region. Their continuous evolution and adaptability underscore the need for robust cybersecurity measures and international cooperation to identify and mitigate the threats posed by such advanced persistent threat groups.
Fueling AI with Great Data with Airbyte Webinar
This talk will focus on how to collect data from a variety of sources, leveraging this data for RAG and other GenAI use cases, and finally charting your course to productionalization.
Artificial Intelligence for XMLDevelopment
In the rapidly evolving landscape of technologies, XML continues to play a vital role in structuring, storing, and transporting data across diverse systems. The recent advancements in artificial intelligence (AI) present new methodologies for enhancing XML development workflows, introducing efficiency, automation, and intelligent capabilities. This presentation will outline the scope and perspective of utilizing AI in XML development. The potential benefits and the possible pitfalls will be highlighted, providing a balanced view of the subject.
We will explore the capabilities of AI in understanding XML markup languages and autonomously creating structured XML content. Additionally, we will examine the capacity of AI to enrich plain text with appropriate XML markup. Practical examples and methodological guidelines will be provided to elucidate how AI can be effectively prompted to interpret and generate accurate XML markup.
Further emphasis will be placed on the role of AI in developing XSLT, or schemas such as XSD and Schematron. We will address the techniques and strategies adopted to create prompts for generating code, explaining code, or refactoring the code, and the results achieved.
The discussion will extend to how AI can be used to transform XML content. In particular, the focus will be on the use of AI XPath extension functions in XSLT, Schematron, Schematron Quick Fixes, or for XML content refactoring.
The presentation aims to deliver a comprehensive overview of AI usage in XML development, providing attendees with the necessary knowledge to make informed decisions. Whether you’re at the early stages of adopting AI or considering integrating it in advanced XML development, this presentation will cover all levels of expertise.
By highlighting the potential advantages and challenges of integrating AI with XML development tools and languages, the presentation seeks to inspire thoughtful conversation around the future of XML development. We’ll not only delve into the technical aspects of AI-powered XML development but also discuss practical implications and possible future directions.
June Patch Tuesday
Ivanti’s Patch Tuesday breakdown goes beyond patching your applications and brings you the intelligence and guidance needed to prioritize where to focus your attention first. Catch early analysis on our Ivanti blog, then join industry expert Chris Goettl for the Patch Tuesday Webinar Event. There we’ll do a deep dive into each of the bulletins and give guidance on the risks associated with the newly-identified vulnerabilities.
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Topic 4 chapter 5 part 3 enzymes - limiting factors
- 1. Topic 4: Chapter 5 EnzymesEnzymes –– Part 3Part 3 Limiting Factors Limiting Factors
- 2. What is a limiting factor? Any factor that directly affects the rate of reaction at which a process occurs if its quantity is changed The value of this factor has to be increased in order to increase the rate of the process
- 3. Factors affecting enzyme activity 1) Temperature 2) pH 3) Substrate Concentration 4) Enzyme Concentration
- 5. Example 1 • Independent Variable: Substrate concentration • LIMITING FACTOR IS Substrate concentration From 0 to Point XFrom 0 to Point X Description Explanation As the [substrate] increases, the rate of reaction increases until Point X when rate of reaction reaches its maximum. At any [substrate] before Point X, there are more enzyme molecules than substrate molecules At Point X, all the enzyme active sites are occupied by substrate molecules
- 6. Example 1 • Independent Variable: Substrate concentration • LIMITING FACTOR IS Enzyme concentration Beyond Point XBeyond Point X Description Explanation Graph remains constant / becomes a plateau after Point X. Maximum rate of reaction After point X, the rate of reaction does not increase even when [substrate] increases. This is because all the enzyme molecule’s active sites are being occupied at any one time. That is, all the enzyme molecules are saturated. Amount of products formed per unit time remains constant
- 7. Example 2 0.4moldm-3 Enzyme 0.2moldm-3 Enzyme RateofReaction Substrate Concentration / Arbitrary Units (A) (B) X Y
- 8. Example 2 • Independent Variable: Substrate concentration From 0 to Point YFrom 0 to Point Y Description Explanation Rate of reaction increases as [Substrate] increases for both Graphs A and B. At any [Substrate] before Point Y, there are more enzymes than substrate molecules. At Point X, all the enzyme active sites are occupied by substrate molecules Rate of reaction of (B) is double that of (A) There are double the number of enzyme molecules in (B). Double the frequency of collision between Enzyme and Substrate molecules in (B) LIMITING FACTOR Substrate Concentration
- 9. Example 2 • Independent Variable: Enzyme concentration Beyond Point YBeyond Point Y LIMITING FACTOR Enzyme Concentration Description Explanation Graph remains constant / becomes a plateau after Point X. Maximum rate of reaction After point X, the rate of reaction does not increase even when [substrate] increases. This is because all the enzyme molecule’s active sites are being occupied at any one time. That is, all the enzyme molecules are saturated. Amount of products formed per unit time remains constant Rate of reaction of (B) is double that of (A) Double the number of enzyme molecules in (B). Double the number of E-S complex formed per unit time. Therefore, double the amount of products formed
- 10. Example 2 • Independent Variable: Enzyme concentration Beyond Point YBeyond Point Y LIMITING FACTOR Enzyme Concentration Description Explanation Graph remains constant / becomes a plateau after Point X. Maximum rate of reaction After point X, the rate of reaction does not increase even when [substrate] increases. This is because all the enzyme molecule’s active sites are being occupied at any one time. That is, all the enzyme molecules are saturated. Amount of products formed per unit time remains constant Rate of reaction of (B) is double that of (A) Double the number of enzyme molecules in (B). Double the number of E-S complex formed per unit time. Therefore, double the amount of products formed