Enzyme kinetics presentation
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This document discusses enzyme kinetics and provides details about key concepts. It introduces enzymes and their role in catalyzing reactions. It then describes enzyme kinetics as the study of reaction rates of enzyme-catalyzed reactions under varying conditions. Several key aspects of enzyme kinetics are summarized, including parametric analysis of enzyme catalysis, enzyme specificity, the lock and key model, and the Michaelis-Menten kinetics model. This model describes how reaction rates increase with substrate concentration until reaching a maximum rate Vmax as the enzyme becomes saturated.
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Enzyme regulation
The flux of metabolites through metabolic pathways involves
catalysis by numerous enzymes. Active control of homeostasis is achieved by the regulation of only a small number of enzymes.
Enzyme kinetics
Enzyme kinetics can provide information about enzyme activity under different conditions. The Michaelis-Menten approach models enzyme-catalyzed reactions and describes reaction rates with the Michaelis-Menten constant (Km) and maximum reaction rate (Vmax). Enzymes can be inhibited reversibly or irreversibly by inhibitors that reduce reaction rates. Different types of reversible inhibition include competitive, uncompetitive, and mixed inhibition. Temperature, pH, and allosteric effectors can regulate enzymatic activity through various mechanisms.
Allosteric enzymes
Some of the enzyme possess additional sites, known as allosteric sites besides the active site . Such as know as allosteric enzyme. The allosteric sites are unique place on the enzyme molecules allosteric enzyme have one or more allosteric site.
HISTRY
The term allosteric has been introduced by the two Noble Laureates JACOB AND MONOD to denote an enzyme site different from the active site which non competitively bands molecule other than the substrate and may influence the enzyme activity.
Properties of allosteric enzyme
Effector may be positive or negative, this effector regulate the enzyme activity . The enzyme activity is increased when a positive allosteric effector binds at the allosteric site known as activator site. On the other hand negative allosteric effector bind at the allosteric site called inhibitor site and inhibit the enzyme activity
Regulatory and allosteric enzymes and allostrerism
This ppt describes the overview of enzyme regulation and Allosterism. Presented since October 23,2017GC at Addis Ababa University, School of Medicine, Department of medical biochemistry.
Enzyme kinetics and inhibition
This document discusses enzyme kinetics and inhibition. It describes how enzymes exert kinetic control over metabolic pathways and reactions. It aims to determine the maximum velocity, substrate affinity, and inhibitor affinity of enzymes. This can provide information about metabolic pathway flow, substrate utilization, and how to manipulate metabolic events. The document also discusses Michaelis-Menten kinetics, Lineweaver-Burk plots, competitive and non-competitive inhibition, and how inhibitors can be used to study enzyme mechanism and regulation.
Enzyme kinetics
Enzyme kinetics is the study of enzyme-catalyzed reaction rates. The Michaelis-Menten equation relates reaction velocity to substrate concentration and kinetic parameters. It describes the hyperbolic relationship between velocity and substrate concentration. The equation can be linearized into the Lineweaver-Burk plot for easier analysis. Enzyme inhibition studies help understand reaction mechanisms and are important for drug development, as most drugs function by inhibiting specific enzymes.
Proteolytic Activation
Many enzymes exist as inactive forms known as zymogens or Proenzymes • proenzymes are synthesized as inactive precursors that are subsequently activated by cleavage of one or a few specific peptide bonds. • a energy source (ATP) is not needed for cleavage. contrast with reversible regulation by phosphorylation, even proteins located outside cells can be activated by this means. • Proteolytic activation, in contrast with allosteric control and reversible covalent modification, occurs just once in the life of an enzyme molecule i.e. the process is irreversible.
Enzyme kinetics
This presentation deals with basics of enzyme kinetics and introduction to various plots which aid in understanding the mechanism of inhibition of enzymes.
Recommended
Enzyme regulation
The flux of metabolites through metabolic pathways involves
catalysis by numerous enzymes. Active control of homeostasis is achieved by the regulation of only a small number of enzymes.
Enzyme kinetics
Enzyme kinetics can provide information about enzyme activity under different conditions. The Michaelis-Menten approach models enzyme-catalyzed reactions and describes reaction rates with the Michaelis-Menten constant (Km) and maximum reaction rate (Vmax). Enzymes can be inhibited reversibly or irreversibly by inhibitors that reduce reaction rates. Different types of reversible inhibition include competitive, uncompetitive, and mixed inhibition. Temperature, pH, and allosteric effectors can regulate enzymatic activity through various mechanisms.
Allosteric enzymes
Some of the enzyme possess additional sites, known as allosteric sites besides the active site . Such as know as allosteric enzyme. The allosteric sites are unique place on the enzyme molecules allosteric enzyme have one or more allosteric site.
HISTRY
The term allosteric has been introduced by the two Noble Laureates JACOB AND MONOD to denote an enzyme site different from the active site which non competitively bands molecule other than the substrate and may influence the enzyme activity.
Properties of allosteric enzyme
Effector may be positive or negative, this effector regulate the enzyme activity . The enzyme activity is increased when a positive allosteric effector binds at the allosteric site known as activator site. On the other hand negative allosteric effector bind at the allosteric site called inhibitor site and inhibit the enzyme activity
Regulatory and allosteric enzymes and allostrerism
This ppt describes the overview of enzyme regulation and Allosterism. Presented since October 23,2017GC at Addis Ababa University, School of Medicine, Department of medical biochemistry.
Enzyme kinetics and inhibition
This document discusses enzyme kinetics and inhibition. It describes how enzymes exert kinetic control over metabolic pathways and reactions. It aims to determine the maximum velocity, substrate affinity, and inhibitor affinity of enzymes. This can provide information about metabolic pathway flow, substrate utilization, and how to manipulate metabolic events. The document also discusses Michaelis-Menten kinetics, Lineweaver-Burk plots, competitive and non-competitive inhibition, and how inhibitors can be used to study enzyme mechanism and regulation.
Enzyme kinetics
Enzyme kinetics is the study of enzyme-catalyzed reaction rates. The Michaelis-Menten equation relates reaction velocity to substrate concentration and kinetic parameters. It describes the hyperbolic relationship between velocity and substrate concentration. The equation can be linearized into the Lineweaver-Burk plot for easier analysis. Enzyme inhibition studies help understand reaction mechanisms and are important for drug development, as most drugs function by inhibiting specific enzymes.
Proteolytic Activation
Many enzymes exist as inactive forms known as zymogens or Proenzymes • proenzymes are synthesized as inactive precursors that are subsequently activated by cleavage of one or a few specific peptide bonds. • a energy source (ATP) is not needed for cleavage. contrast with reversible regulation by phosphorylation, even proteins located outside cells can be activated by this means. • Proteolytic activation, in contrast with allosteric control and reversible covalent modification, occurs just once in the life of an enzyme molecule i.e. the process is irreversible.
Enzyme kinetics
This presentation deals with basics of enzyme kinetics and introduction to various plots which aid in understanding the mechanism of inhibition of enzymes.
Active site of an enzyme
The active site of an enzyme is the region that binds substrates and contains catalytic groups that directly participate in bond making and breaking. It takes the form of a cleft or pocket formed by amino acid residues far apart in the primary structure. The active sites of multimeric enzymes are located at interfaces between subunits and recruit residues from multiple monomers. Enzymes use an induced-fit or lock-and-key model to bind substrates specifically through weak interactions like hydrogen bonds and van der Waals forces at their active sites.
Enzyme and enzyme inhibition
This document discusses enzymes and enzyme kinetics. It defines enzymes as biomolecules that catalyze chemical reactions and provides examples of enzyme units and the SI unit for enzyme activity, the katal. The document then summarizes Michaelis-Menten enzyme kinetics, including the key assumptions of the MM model. It describes parameters of the MM equation like Km, Vmax, kcat, and kcat/Km. Finally, it discusses enzyme inhibition, categorizing inhibitors as reversible or irreversible and describing different types of reversible and irreversible inhibition.
Enzyme regulation
This document discusses various mechanisms of enzyme regulation in living systems. It begins by explaining that hundreds of enzyme-catalyzed reactions must be precisely controlled for proper cellular functioning. It then describes several key mechanisms by which this regulation can be achieved, including allosteric regulation, isoenzyme expression, zymogen activation, and covalent modification via phosphorylation or glycosylation. Specific examples are provided for each type of regulation, such as feedback inhibition of threonine dehydratase and phosphorylation control of glycogen phosphorylase activity. The document concludes by emphasizing that multiple regulatory strategies acting together ensure survival of the cell and maintenance of homeostasis.
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The document summarizes the mechanisms of enzyme catalysis. It discusses how enzymes lower the activation energy of reactions by releasing binding energy when interacting with substrates. This allows enzymes to accelerate reactions by stabilizing transition states. There are three main types of catalytic mechanisms: acid-base catalysis, covalent catalysis, and metal ion catalysis. Acid-base catalysis involves proton transfers. Covalent catalysis forms temporary covalent bonds between enzymes and substrates. Metal ion catalysis uses metal ions like iron and copper to orient and stabilize reactive molecules in enzyme active sites.
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The document discusses enzyme kinetics models including the Michaelis-Menten model and Lineweaver-Burk double reciprocal plot. The Michaelis-Menten model relates reaction rate to substrate concentration using kinetic constants Km and Vmax. It describes the enzyme-substrate reaction mechanism. The Lineweaver-Burk plot is a graphical representation that transforms the Michaelis-Menten equation into a straight line to determine Km and Vmax. It can distinguish competitive and noncompetitive enzyme inhibition patterns.
Enzyme kinetics
Enzymes are protein molecules that act as catalysts in biological processes, accelerating reactions by lowering their activation energy. Enzyme kinetics is the study of chemical reactions catalyzed by enzymes and how varying conditions affect reaction rates. The Michaelis-Menten model describes reaction rates in terms of the enzyme-substrate binding affinity (Km) and maximum reaction rate (Vmax). Graphical representations like Lineweaver-Burk and Eadie-Hofstee plots can determine these parameters from experimental data.
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Enzymes are protein catalysts that speed up biochemical reactions without being consumed. They achieve specificity and efficiency through their active sites, which bind substrates and use mechanisms like proximity, acid/base catalysis, and covalent bonding to facilitate reactions. Enzyme activity can be measured and is affected by factors like temperature, pH, substrate and enzyme concentration. The Michaelis-Menten model describes the hyperbolic relationship between reaction rate and substrate concentration. Kinetic analysis allows determination of parameters like Km and Vmax. Inhibitors are used clinically and in research to reduce reaction rates by binding in or near the active site.
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Enzymes use several catalytic mechanisms to lower the free energy of transition states and greatly increase reaction rates, including acid-base catalysis, covalent catalysis, metal ion catalysis, and bringing substrates into close proximity and proper orientation. Acid-base catalysis involves proton transfer from catalytic amino acid side chains. Covalent catalysis transiently forms covalent bonds between enzyme and substrate. Metal ion catalysis uses transition metals to orient substrates, mediate redox reactions, or stabilize charges. Proximity and orientation align substrates for reaction, while catalysis by approximation brings two substrates together for reaction.
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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.
Allosteric enzymes
1) Allosteric enzymes have additional sites called allosteric sites that are distinct from the active site. Binding of an effector molecule to these sites can induce a conformational change in the active site, increasing or decreasing the enzyme's activity.
2) There are two main models that describe allosteric regulation - the concerted model where binding causes simultaneous changes in all subunits, and the sequential model where changes occur sequentially.
3) Allosteric enzymes exhibit sigmoidal kinetics curves rather than traditional hyperbolic curves due to their cooperative binding behavior. Positive allosteric effectors increase enzyme activity while negative effectors decrease it.
Enzyme kinetics
This document provides an overview of enzyme kinetics. It defines important terms like rate constant, substrate concentration, enzyme unit, and Michaelis constant. It describes models used to study enzyme kinetics like the Michaelis-Menten equations and Lineweaver-Burk, Hanes-Woolf, and Eadie-Hofstee plots. It discusses factors that affect reaction rates like pH, temperature, and inhibitors. The document also covers cooperative enzyme systems and multireactant reactions.
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This document discusses enzyme kinetics and the Michaelis-Menten model of enzyme kinetics. It provides details on several key aspects:
1) Substrate concentration affects the rate of enzyme-catalyzed reactions, with the initial rate (V0) increasing with substrate concentration ([S]) until reaching a maximum rate (Vmax) at high substrate levels.
2) The Michaelis-Menten model describes this relationship through kinetic parameters like Km (the substrate concentration when V0 is half of Vmax) and Vmax.
3) Various plots like Lineweaver-Burk, Eadie-Hofstee, and Hanes-Woolf plots can be used to
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The document discusses different types of enzyme inhibition. There are three broad categories of enzyme inhibition: reversible, irreversible, and allosteric inhibition. Reversible inhibition includes competitive, non-competitive, and uncompetitive inhibition. Competitive inhibitors bind to the enzyme's active site, preventing substrate binding. Non-competitive inhibitors bind elsewhere, altering the enzyme's shape. Uncompetitive inhibitors only bind to the enzyme-substrate complex. Irreversible inhibitors covalently bind the enzyme, permanently inactivating it. Many drugs work by competitively or non-competitively inhibiting key enzymes.
Regulation of Enzyme activity.pptx
This document discusses various mechanisms by which enzyme activity is regulated in cells. It describes three main mechanisms: allosteric regulation, covalent modification, and proteolytic cleavage. Allosteric regulation involves binding of effector molecules to allosteric sites that increase or decrease catalytic activity. Covalent modification, like phosphorylation, can activate or inactivate enzymes. Proteolytic cleavage activates zymogen enzymes by cleaving them into active forms. Feedback inhibition and cooperativity are also discussed as ways allosteric enzymes can regulate metabolic pathways and adjust activity levels in cells.
Bisubstrate
This document discusses bisubstrate reactions, which involve two substrates and produce two products. Approximately 60% of biochemical reactions are bisubstrate reactions. They can be transferase reactions, where a functional group is transferred between substrates, or oxidation-reduction reactions. Bisubstrate reactions fall into two categories: sequential reactions, where substrates bind sequentially before products are released; and ping pong reactions, where an intermediate enzyme form is produced after the first substrate reaction. Common examples of each type of bisubstrate reaction are provided.
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Presentation given by Dr. Karthikeyan at Department of Biochemistry, Maulana Azad Medical College on 04.04.2013.
Regulation of enzyme activity
1. Enzyme activity can be regulated through several mechanisms including allosteric regulation, feedback inhibition, proenzymes, and protein modification.
2. Allosteric enzymes have effector molecules that bind and induce a conformational change that increases or decreases enzyme activity. Feedback inhibition occurs when a metabolic end product inhibits an earlier enzyme.
3. Proenzymes are inactive precursors that are activated by proteolytic cleavage. Protein modification like phosphorylation can also regulate enzymes by changing their structure.
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enzyme kinetics, mechanism of action of enzymes and line-weaver burk plot
This document discusses key concepts in enzyme kinetics including:
Vmax represents the maximum initial rate of a catalyzed reaction when all enzyme is saturated with substrate. Km is the substrate concentration at which the reaction rate is at half of Vmax, and 50% of enzyme is bound to substrate. A Line-Weaver Burk plot can be used to determine Km and Vmax values from experimental data by taking the inverse of reaction rates and substrate concentrations.
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The active site of an enzyme is the region that binds substrates and contains catalytic groups that directly participate in bond making and breaking. It takes the form of a cleft or pocket formed by amino acid residues far apart in the primary structure. The active sites of multimeric enzymes are located at interfaces between subunits and recruit residues from multiple monomers. Enzymes use an induced-fit or lock-and-key model to bind substrates specifically through weak interactions like hydrogen bonds and van der Waals forces at their active sites.
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This document discusses enzymes and enzyme kinetics. It defines enzymes as biomolecules that catalyze chemical reactions and provides examples of enzyme units and the SI unit for enzyme activity, the katal. The document then summarizes Michaelis-Menten enzyme kinetics, including the key assumptions of the MM model. It describes parameters of the MM equation like Km, Vmax, kcat, and kcat/Km. Finally, it discusses enzyme inhibition, categorizing inhibitors as reversible or irreversible and describing different types of reversible and irreversible inhibition.
Enzyme regulation
This document discusses various mechanisms of enzyme regulation in living systems. It begins by explaining that hundreds of enzyme-catalyzed reactions must be precisely controlled for proper cellular functioning. It then describes several key mechanisms by which this regulation can be achieved, including allosteric regulation, isoenzyme expression, zymogen activation, and covalent modification via phosphorylation or glycosylation. Specific examples are provided for each type of regulation, such as feedback inhibition of threonine dehydratase and phosphorylation control of glycogen phosphorylase activity. The document concludes by emphasizing that multiple regulatory strategies acting together ensure survival of the cell and maintenance of homeostasis.
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This document summarizes a discussion on chemically modifying enzymes to improve their physico-chemical properties. It defines enzymes and describes their physical and chemical properties. Chemical modification involves changing an enzyme's structure or groups to alter its properties. Two main types are group-specific reagents and affinity labels, which target certain amino acid side chains. Chemical modification can provide information on enzyme mechanisms and properties. However, it faces limitations as modifiers may not be absolutely specific and can induce conformational changes.
Enzyme catalysis
The document summarizes the mechanisms of enzyme catalysis. It discusses how enzymes lower the activation energy of reactions by releasing binding energy when interacting with substrates. This allows enzymes to accelerate reactions by stabilizing transition states. There are three main types of catalytic mechanisms: acid-base catalysis, covalent catalysis, and metal ion catalysis. Acid-base catalysis involves proton transfers. Covalent catalysis forms temporary covalent bonds between enzymes and substrates. Metal ion catalysis uses metal ions like iron and copper to orient and stabilize reactive molecules in enzyme active sites.
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The document discusses enzyme kinetics models including the Michaelis-Menten model and Lineweaver-Burk double reciprocal plot. The Michaelis-Menten model relates reaction rate to substrate concentration using kinetic constants Km and Vmax. It describes the enzyme-substrate reaction mechanism. The Lineweaver-Burk plot is a graphical representation that transforms the Michaelis-Menten equation into a straight line to determine Km and Vmax. It can distinguish competitive and noncompetitive enzyme inhibition patterns.
Enzyme kinetics
Enzymes are protein molecules that act as catalysts in biological processes, accelerating reactions by lowering their activation energy. Enzyme kinetics is the study of chemical reactions catalyzed by enzymes and how varying conditions affect reaction rates. The Michaelis-Menten model describes reaction rates in terms of the enzyme-substrate binding affinity (Km) and maximum reaction rate (Vmax). Graphical representations like Lineweaver-Burk and Eadie-Hofstee plots can determine these parameters from experimental data.
Enzymology - an overview
Enzymes are protein catalysts that speed up biochemical reactions without being consumed. They achieve specificity and efficiency through their active sites, which bind substrates and use mechanisms like proximity, acid/base catalysis, and covalent bonding to facilitate reactions. Enzyme activity can be measured and is affected by factors like temperature, pH, substrate and enzyme concentration. The Michaelis-Menten model describes the hyperbolic relationship between reaction rate and substrate concentration. Kinetic analysis allows determination of parameters like Km and Vmax. Inhibitors are used clinically and in research to reduce reaction rates by binding in or near the active site.
Enzyme catalysis mechanisms involved
Enzymes use several catalytic mechanisms to lower the free energy of transition states and greatly increase reaction rates, including acid-base catalysis, covalent catalysis, metal ion catalysis, and bringing substrates into close proximity and proper orientation. Acid-base catalysis involves proton transfer from catalytic amino acid side chains. Covalent catalysis transiently forms covalent bonds between enzyme and substrate. Metal ion catalysis uses transition metals to orient substrates, mediate redox reactions, or stabilize charges. Proximity and orientation align substrates for reaction, while catalysis by approximation brings two substrates together for reaction.
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This presentation provides a comprehensive account on allosteric enzymes and the mechanism of allosteric inhibition.
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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.
Allosteric enzymes
1) Allosteric enzymes have additional sites called allosteric sites that are distinct from the active site. Binding of an effector molecule to these sites can induce a conformational change in the active site, increasing or decreasing the enzyme's activity.
2) There are two main models that describe allosteric regulation - the concerted model where binding causes simultaneous changes in all subunits, and the sequential model where changes occur sequentially.
3) Allosteric enzymes exhibit sigmoidal kinetics curves rather than traditional hyperbolic curves due to their cooperative binding behavior. Positive allosteric effectors increase enzyme activity while negative effectors decrease it.
Enzyme kinetics
This document provides an overview of enzyme kinetics. It defines important terms like rate constant, substrate concentration, enzyme unit, and Michaelis constant. It describes models used to study enzyme kinetics like the Michaelis-Menten equations and Lineweaver-Burk, Hanes-Woolf, and Eadie-Hofstee plots. It discusses factors that affect reaction rates like pH, temperature, and inhibitors. The document also covers cooperative enzyme systems and multireactant reactions.
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This document discusses enzyme kinetics and the Michaelis-Menten model of enzyme kinetics. It provides details on several key aspects:
1) Substrate concentration affects the rate of enzyme-catalyzed reactions, with the initial rate (V0) increasing with substrate concentration ([S]) until reaching a maximum rate (Vmax) at high substrate levels.
2) The Michaelis-Menten model describes this relationship through kinetic parameters like Km (the substrate concentration when V0 is half of Vmax) and Vmax.
3) Various plots like Lineweaver-Burk, Eadie-Hofstee, and Hanes-Woolf plots can be used to
Abzymes
Abzymes, also known as catalytic antibodies, are monoclonal antibodies that exhibit enzymatic activity. They are able to bind to transition states of enzyme-catalyzed reactions with high specificity and affinity, stabilizing the transition state and increasing reaction rates. Abzymes can be artificially produced by immunizing animals with transition state analogs of reactions. They have potential applications in drug development, cancer treatment, and developing therapies for viral infections like HIV. Researchers have engineered an abzyme that can degrade an essential region of the HIV envelope protein, rendering the virus unable to infect cells.
Enzyme inhibition
The document discusses different types of enzyme inhibition. There are three broad categories of enzyme inhibition: reversible, irreversible, and allosteric inhibition. Reversible inhibition includes competitive, non-competitive, and uncompetitive inhibition. Competitive inhibitors bind to the enzyme's active site, preventing substrate binding. Non-competitive inhibitors bind elsewhere, altering the enzyme's shape. Uncompetitive inhibitors only bind to the enzyme-substrate complex. Irreversible inhibitors covalently bind the enzyme, permanently inactivating it. Many drugs work by competitively or non-competitively inhibiting key enzymes.
Regulation of Enzyme activity.pptx
This document discusses various mechanisms by which enzyme activity is regulated in cells. It describes three main mechanisms: allosteric regulation, covalent modification, and proteolytic cleavage. Allosteric regulation involves binding of effector molecules to allosteric sites that increase or decrease catalytic activity. Covalent modification, like phosphorylation, can activate or inactivate enzymes. Proteolytic cleavage activates zymogen enzymes by cleaving them into active forms. Feedback inhibition and cooperativity are also discussed as ways allosteric enzymes can regulate metabolic pathways and adjust activity levels in cells.
Bisubstrate
This document discusses bisubstrate reactions, which involve two substrates and produce two products. Approximately 60% of biochemical reactions are bisubstrate reactions. They can be transferase reactions, where a functional group is transferred between substrates, or oxidation-reduction reactions. Bisubstrate reactions fall into two categories: sequential reactions, where substrates bind sequentially before products are released; and ping pong reactions, where an intermediate enzyme form is produced after the first substrate reaction. Common examples of each type of bisubstrate reaction are provided.
Mechanism of enzyme action
Presentation given by Dr. Karthikeyan at Department of Biochemistry, Maulana Azad Medical College on 04.04.2013.
Regulation of enzyme activity
1. Enzyme activity can be regulated through several mechanisms including allosteric regulation, feedback inhibition, proenzymes, and protein modification.
2. Allosteric enzymes have effector molecules that bind and induce a conformational change that increases or decreases enzyme activity. Feedback inhibition occurs when a metabolic end product inhibits an earlier enzyme.
3. Proenzymes are inactive precursors that are activated by proteolytic cleavage. Protein modification like phosphorylation can also regulate enzymes by changing their structure.
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This document discusses enzyme kinetics and inhibition. It begins by defining enzyme inhibitors as compounds that convert enzymes into inactive forms, slowing reaction rates. There are two main classes of inhibitors - reversible and irreversible. Feedback inhibition is described as when an enzyme catalyzing the first step of a biosynthesis pathway is inhibited by the end product. The document then discusses different types of reversible (competitive, noncompetitive, uncompetitive) and irreversible inhibition in more detail. It also covers concepts such as activation energy, enzyme kinetics models like Michaelis-Menten, and how temperature, pH, substrate and enzyme concentration affect reaction rates.
Powerpoint enzymes models of action
Enzymes are proteins that act as biological catalysts, speeding up chemical reactions without being used up. They work via a "lock and key" mechanism, though the induced fit model suggests enzymes are flexible. Enzyme activity can be measured by looking at reaction rates under different temperatures, pH levels, enzyme and substrate concentrations. Heating an enzyme above its optimal temperature can cause it to denature, changing its shape so the active site no longer fits the substrate. Many enzymes are used industrially in washing powders, food processing, and antibiotic production.
Catalase test
Catalase is an important enzyme that breaks down reactive oxygen species (ROS) such as hydrogen peroxide, protecting cells from oxidative damage. The catalase test detects this enzymatic activity by observing bubble formation when bacterial cultures or colonies are mixed with hydrogen peroxide. A positive result indicates catalase production, allowing distinction between bacterial species - for example, Staphylococcus is catalase-positive while Streptococcus is negative. The procedure involves placing a small amount of bacterial growth on a slide and mixing with hydrogen peroxide, with bubble formation signifying a positive catalase test result.
Enzyme kinetics
Enzyme kinetics is the study of reaction rates catalyzed by enzymes. Michaelis and Menten developed an equation to describe enzyme kinetics based on the assumptions that enzyme-substrate complexes form rapidly and at steady state. The Michaelis-Menten equation relates reaction rate to substrate concentration and can be linearized using double reciprocal plots. Enzyme kinetics are affected by factors like pH, temperature, and substrate concentration, and some enzymes use two substrates in either sequential or double displacement mechanisms.
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enzyme kinetics, mechanism of action of enzymes and line-weaver burk plot
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3 Enzymes.pptx Enzymes, it's types and function
Enzymes are biological molecules that catalyze chemical reactions and increase their rates. They are selective for specific substrates and only catalyze a few reactions. Enzymes work by lowering activation energy and can accelerate reactions by millions of times. They are not consumed in reactions and do not alter equilibrium. Enzyme activity is affected by factors like temperature, pH, inhibitors, and more. The lock and key and induced fit models describe how enzymes and substrates interact specifically in the active site. Cofactors like metal ions and coenzymes are required for some enzyme activity. Enzymes perform critical functions in cell signaling, movement, and metabolism and are targets of drugs and involved in diseases.
Enzymes
Enzymes are protein catalysts that accelerate chemical reactions. They lower the activation energy of reactions allowing metabolic processes to occur faster. Enzymes achieve specificity through their tertiary structure and active site. The induced fit model describes how the active site changes shape upon substrate binding. Enzyme kinetics follow the Michaelis-Menten model where the substrate first binds the enzyme before products are released. Reaction rates depend on factors like substrate/enzyme concentration, temperature, pH, and inhibitors. Enzymes can be immobilized in beads to make them reusable.
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.
enzymatic activities and enzyme pathway
This document summarizes key ways that enzymes are regulated in cells and metabolic pathways. It discusses how enzyme activity is influenced by environmental conditions like temperature and pH. Changes from normal conditions can denature enzymes and disrupt metabolic reactions. The document also describes how metabolic pathways involve series of enzyme-catalyzed reactions that form linear or branching chains. Pacemaker enzymes control pathway rates in response to signals. Finally, it outlines direct controls on enzymes through competitive or noncompetitive inhibition and controls on enzyme synthesis through repression or induction in response to substrates and products.
Enzymes.ppt
Enzymes are protein catalysts that speed up biochemical reactions without being consumed. They work by lowering activation energy and forming enzyme-substrate complexes. Nearly all reactions in living cells require enzyme catalysis. The three main points covered are:
1. Enzymes greatly increase reaction rates, with specificity for substrates. They achieve catalysis via binding sites and lowering energy barriers.
2. Many factors influence enzyme activity rates, such as substrate/enzyme concentration, temperature, pH, and presence of activators/inhibitors.
3. Regulation of enzyme activity is important and occurs through mechanisms like allosteric binding, covalent modification, gene expression control, compartmentalization, and zymogen
Unit 4: Plasma Enzyme tests in diagnosis
This document provides an overview of plasma enzyme tests and their use in diagnosis. It discusses factors that affect enzyme reaction rates, the clinical usefulness of measuring serum enzyme levels, and specific enzymes that are useful in diagnosing various disorders, including cardiac, hepatic, bone, muscle, malignancies and acute pancreatitis. The document also covers enzyme kinetics, the advantages and disadvantages of enzyme assays, how enzyme activity is measured and calculated, and the classification of different enzyme types.
Module 5.pptx
Enzymes are globular proteins that act as biological catalysts, speeding up chemical reactions without being consumed. They are typically named after their substrate with the suffix "-ase". Enzyme activity can be monitored by measuring changes in substrate or product concentration. Mass spectrometry provides an alternative detection method without needing a chromophore. The enzyme binds its substrate at the active site, forming an enzyme-substrate complex. This lowers the activation energy and allows the reaction to proceed, with the unaltered enzyme then dissociating to catalyze more reactions. Kinetic analysis reveals the individual reaction steps and how enzyme activity is controlled.
Enzymes .pptx
1. Enzymes are biological catalysts that lower the activation energy of chemical reactions, speeding up the rate at which reactions occur. They do this by binding to substrate molecules and bringing them close together in an orientation that facilitates the reaction.
2. Enzyme activity can be regulated at the transcriptional, translational, and post-translational levels. Allosteric regulation also allows effector molecules to bind and induce conformational changes that modulate enzyme activity.
3. Enzymes accelerate both the forward and reverse reactions of a chemical equilibrium equally, and thus do not change the position of equilibrium between reactants and products.
Enzyme action
Enzymes are catalysts that accelerate biochemical reactions by lowering the activation energy. They do this by binding to substrates in their active site, which releases energy and activates the substrates. The lock and key model proposes a perfect fit between enzyme and substrate shapes. The induced fit model suggests some flexibility in the active site. Enzymes bind substrates via various bonds like ionic, hydrogen, and Van der Waals. Allosteric enzymes have additional effector binding sites that cause conformational changes altering activity. Isozymes are enzymes that catalyze the same reaction but differ in structure and properties. Ribozymes are catalytically active RNA molecules.
Enzyme kinetics
Enzyme kinetics is the study of the chemical reactions that are catalyzed by enzymes. In enzyme kinetics, the reaction rate is measured and the effects of varying the conditions of the reaction are investigated. Studying an enzyme's kinetics can reveal the catalytic mechanism of this enzyme, its role in metabolism, how its activity is controlled, and how a drug or an agonist might inhibit the enzyme. Creative Enzymes is a renowned service provider, supporting many industrial and academic researchers for kinetic studies. This service helps to determine virtually all kinetic parameters such as Vmax, Kd, KM, kcat, ka, and kb.
Enzyme kinetics
Enzyme kinetics is the study of the chemical reactions that are catalyzed by enzymes. In enzyme kinetics, the reaction rate is measured and the effects of varying the conditions of the reaction are investigated. Studying an enzyme's kinetics can reveal the catalytic mechanism of this enzyme, its role in metabolism, how its activity is controlled, and how a drug or an agonist might inhibit the enzyme. Creative Enzymes is a renowned service provider, supporting many industrial and academic researchers for kinetic studies.
Enzyme kinetics - Creative Enzymes
Enzyme kinetics is the study of the chemical reactions that are catalyzed by enzymes. In enzyme kinetics, the reaction rate is measured and the effects of varying the conditions of the reaction are investigated. Studying an enzyme's kinetics can reveal the catalytic mechanism of this enzyme, its role in metabolism, how its activity is controlled, and how a drug or an agonist might inhibit the enzyme. Creative Enzymes is a renowned service provider, supporting many industrial and academic researchers for kinetic studies. https://www.creative-enzymes.com/service/Enzyme-Kinetics_393.html
plantbiochemlecture5-enzymesb.ppt
The document discusses factors that affect enzyme activity, including environmental conditions like temperature and pH, as well as substrate and enzyme concentration. It then covers enzyme kinetics, explaining how the initial rate of reaction (V0) depends on substrate concentration [S] according to the Michaelis-Menten equation. Finally, it discusses different mechanisms of enzyme regulation, including genetic control of enzyme levels, covalent modification of enzymes, and allosteric regulation where binding of an effector molecule at a separate site influences the active site.
Enzyme kinetics
This document provides an overview of enzyme kinetics concepts including:
1) The relationship between reaction velocity and substrate concentration follows a hyperbolic curve known as Michaelis-Menten kinetics.
2) Enzymes can be inhibited through competitive, mixed, and allosteric inhibition mechanisms which impact the Michaelis-Menten curve.
3) Assays of enzyme activity can be used as diagnostic tools to detect tissue damage or disease based on abnormal levels of enzymes detected in blood serum.
ENZYMES.pptx
Enzymes are biological catalysts that speed up biochemical reactions without being consumed. They do this by lowering the activation energy of reactions. Enzymes are highly specific and only catalyze particular reactions. They work by binding substrates and bringing them into proximity for reactions to occur. Factors like temperature, pH, and inhibitors can impact an enzyme's activity. Enzyme kinetics use the Michaelis-Menten equation to describe the relationship between substrate concentration and reaction rate.
enzymes-160517003157.pptxbiochemistryyyy
This document discusses enzymes and their properties. It begins by explaining that enzymes are biological catalysts that are usually proteins and that speed up biochemical reactions. It describes enzyme structure, including the active site where substrates bind. It discusses cofactors that enzymes require to function properly. The document then explains enzyme kinetics concepts like Michaelis-Menten kinetics and how temperature, pH, and substrate concentration affect reaction rates. Finally, it covers inhibition, where inhibitors bind enzymes and decrease their activity, and activation, where enzymes are converted to more active forms.
D. Pharm BIOCHEMISTRY AND CLINICAL PATHOLOGY Enzyme
Enzymes are biological catalysts that accelerate biochemical reactions. They are characterized by catalytic power, specificity, and regulation. Enzymes are classified based on the type of reaction they catalyze. Factors like substrate and enzyme concentration, temperature, pH, and inhibitors affect enzyme activity. Enzymes act by lowering the activation energy of reactions via two mechanisms - induced fit and lock and key models. Estimation of certain enzymes in blood aids in diagnosis of diseases like acute pancreatitis, liver disease, heart attacks, and cancer.
Enzymes Biochemistry
This document discusses enzymes and provides information on their chemistry, classification, mechanism of action, kinetics, inhibition, activation and specificity. It defines enzymes as biological catalysts that speed up biochemical reactions. Most enzymes are globular proteins that contain an active site for substrate binding. The document outlines different types of enzyme kinetics including effects of temperature, pH, and substrate concentration. It also describes different types of inhibition like competitive, non-competitive and irreversible inhibition. Activation of enzymes by cofactors is also summarized.
Enzymes are proteins used for wide range of reaction.pptx
Enzymes are biological catalysts that speed up chemical reactions in cells. They are proteins that function as catalysts by lowering the activation energy of reactions without being consumed in the process. Enzymes have specific active sites that bind to substrates and catalyze reactions through mechanisms like lock-and-key and induced fit models. Enzyme activity can be regulated by factors like concentration, temperature, pH, and through reversible inhibition by competitive, noncompetitive, or uncompetitive inhibitors binding at the active site.
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D. Pharm BIOCHEMISTRY AND CLINICAL PATHOLOGY Enzyme
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Enzyme kinetics presentation
- 2. ENZYME KINETICS Ahmed Nawaz 13ch153 Waleed Shaikh 13CH03 Talal Ashraf 13CH10 Muzamill Hussain 13CH19 Inayat Morio 13CH136
- 3. Contents: • Enzyme • Enzyme Kinetics • Parametric Analysis of enzyme catalysis • Enzyme specific to substrate • Key And Lock Model • Michaelis Menten Kinetics Model for Enzyme
- 4. Enzymes • Enzymes are usually protein molecules that manipulate other molecules — the enzymes' substrates. • These target molecules bind to an enzyme's active site and are transformed into products through a series of steps known as the enzymatic mechanism. • These mechanisms can be divided into single-substrate and multiple-substrate mechanisms.
- 6. Introduction Enzyme Kinetics • Enzyme kinetics is the study of the chemical reactions that are catalyzed by enzymes. • In enzyme kinetics, the reaction rate is measured and the effects of varying the conditions of the reaction is investigated. • Studying an enzyme's kinetics in this way can reveal the catalytic mechanism of this enzyme, its role in metabolism, how it activity is controlled, and how a drug or an agonist might inhibit the enzyme.
- 8. Parametric Analysis of Enzyme Catalysis • It is often asserted that enzymes are more active, i.e., allow reactions to go faster, than non biological catalysts. • At the ambient temperatures where enzymes are most active they are able to catalyze reactions faster than the majority of artificial catalysts. • When the reaction temperature is increased, solid (synthetic) catalysts may become as active as enzymes. • The enzyme activity does not increase continuously as the temperature is raised. Instead, the enzyme usually loses activity at quite a low temperature, often only slightly above that at which it is typically found.
- 9. How are enzymes specific to substrates? • Enzymes are specific to substrates as they have an active site which only allow certain substrates to bind to the active site.This is due to the shape of the active site and any other substrates cannot bind to the active site. There is a model which is well known in the biology field of the lock and key model.This is because you have to have the correct key to insert it into the lock.This goes the same as an enzymes active site and the substrate.
- 12. Michaelis– Menten kinetics • As enzyme-catalyzed reactions are saturable, their rate of catalysis does not show a linear response to increasing substrate. If the initial rate of the reaction is measured over a range of substrate concentrations (denoted as [S]), the reaction rate (v) increases as [S] increases, as shown on the right. However, as [S] gets higher, the enzyme becomes saturated with substrate and the rate reaches Vmax, the enzyme's maximum rate.
- 13. Mathematical Model For Enzyme Kinetics This equation is called Michaelis–Menten equation. Where, Here, Vmax represents the maximum rate achieved by the system, at maximum (saturating) substrate concentrations. The Michaelis constant Km is the substrate concentration at which the reaction rate is half of Vmax.