chemistry of enzymes, ES complex theories, co factors and coenzymes
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Enzymes are protein catalysts that increase the rate of reactions without being changed. They are typically proteins, heat labile, water soluble, and contain nitrogen. Enzymes consist of an apoenzyme protein component and may also contain non-protein cofactors, coenzymes, prosthetic groups, or metal ions. Enzymes act by lowering the activation energy of reactions, either by properly orienting substrates, or utilizing mechanisms like acid/base catalysis, strain induction, or covalent bonding to substrates. This allows enzymes to greatly accelerate chemical reactions by stabilizing high-energy transition states.
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Mechanism of enzyme catalysis
brief idea of how enzymes function within the body mainly focusing on covalent catalysis and proximity effects
FATTY ACID OXIDATION
Free fatty acids also called unesterified (UFA) or nonesterified (NEFA) fatty acids are fatty acids that are in the unesterified state.
In plasma, longer-chain FFA are combined with albumin, and in the cell they are attached to a fatty acid-binding protein.
Shorter-chain fatty acids are more watersoluble and exist as the un-ionized acid or as a fatty acid anion.
By these means, free fatty acids are made accessible as a fuel in other tissues.
Mechanism of enzyme action
Presentation given by Dr. Karthikeyan at Department of Biochemistry, Maulana Azad Medical College on 04.04.2013.
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.
Chapter 4 enzymes
- Amylase, lipase, proteases added to laundry detergents
- Papain, bromelain added to meat tenderizers
- Lysozyme added to wound dressings
Diagnostic:
- Measuring enzyme levels in blood/urine to detect organ damage
- Measuring enzyme levels in blood to diagnose genetic disorders
Therapeutic:
- Enzyme replacement therapy for genetic disorders
- Enzymes as digestive aids or supplements
Research:
- Enzymes used as reagents in clinical assays and diagnostic kits
So in summary, enzymes play important roles in diagnostics, research, and therapeutics in medicine. Their catalytic properties are exploited for various applications.
Enzyme and coenzyme
briefly describe enzyme and coenzyme and its role in many orders. Consist of enzyme nomenclature, enzyme part: prosthetic group, metalions, cofactors, and secondary substrate. Describe inhibition action.
Basics of Enzyme Catalysis
Enzymes catalyze chemical reactions by reducing the activation energy needed for the reaction to occur. They do this using several mechanisms including acid-base catalysis, covalent bond formation, and metal ion catalysis. Enzymes are also able to increase reaction rates by properly orienting substrates. Enzyme activity can be inhibited through various reversible and irreversible mechanisms such as competitive inhibition where an inhibitor binds to the active site, and suicide inhibition where the inhibitor is converted by the enzyme into a tightly-binding form. The Michaelis-Menten model and Lineweaver-Burk plots are commonly used to study enzyme kinetics and inhibition types.
Enzymes
Enzymes are protein catalysts that accelerate biochemical reactions without being consumed. They are specific, catalytic, reversible, and sensitive to temperature and pH changes. Enzymes lower the activation energy of reactions. The active site of an enzyme binds specifically to substrates. Some enzymes require cofactors like metal ions or coenzymes to function. Enzyme kinetics examines factors that influence reaction rates like substrate concentration. Michaelis-Menten kinetics describes the reversible binding of enzymes and substrates to form enzyme-substrate complexes. Enzyme inhibitors decrease catalytic activity by binding to the active site or elsewhere on the enzyme.
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Mechanism of enzyme catalysis
brief idea of how enzymes function within the body mainly focusing on covalent catalysis and proximity effects
FATTY ACID OXIDATION
Free fatty acids also called unesterified (UFA) or nonesterified (NEFA) fatty acids are fatty acids that are in the unesterified state.
In plasma, longer-chain FFA are combined with albumin, and in the cell they are attached to a fatty acid-binding protein.
Shorter-chain fatty acids are more watersoluble and exist as the un-ionized acid or as a fatty acid anion.
By these means, free fatty acids are made accessible as a fuel in other tissues.
Mechanism of enzyme action
Presentation given by Dr. Karthikeyan at Department of Biochemistry, Maulana Azad Medical College on 04.04.2013.
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.
Chapter 4 enzymes
- Amylase, lipase, proteases added to laundry detergents
- Papain, bromelain added to meat tenderizers
- Lysozyme added to wound dressings
Diagnostic:
- Measuring enzyme levels in blood/urine to detect organ damage
- Measuring enzyme levels in blood to diagnose genetic disorders
Therapeutic:
- Enzyme replacement therapy for genetic disorders
- Enzymes as digestive aids or supplements
Research:
- Enzymes used as reagents in clinical assays and diagnostic kits
So in summary, enzymes play important roles in diagnostics, research, and therapeutics in medicine. Their catalytic properties are exploited for various applications.
Enzyme and coenzyme
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Basics of Enzyme Catalysis
Enzymes catalyze chemical reactions by reducing the activation energy needed for the reaction to occur. They do this using several mechanisms including acid-base catalysis, covalent bond formation, and metal ion catalysis. Enzymes are also able to increase reaction rates by properly orienting substrates. Enzyme activity can be inhibited through various reversible and irreversible mechanisms such as competitive inhibition where an inhibitor binds to the active site, and suicide inhibition where the inhibitor is converted by the enzyme into a tightly-binding form. The Michaelis-Menten model and Lineweaver-Burk plots are commonly used to study enzyme kinetics and inhibition types.
Enzymes
Enzymes are protein catalysts that accelerate biochemical reactions without being consumed. They are specific, catalytic, reversible, and sensitive to temperature and pH changes. Enzymes lower the activation energy of reactions. The active site of an enzyme binds specifically to substrates. Some enzymes require cofactors like metal ions or coenzymes to function. Enzyme kinetics examines factors that influence reaction rates like substrate concentration. Michaelis-Menten kinetics describes the reversible binding of enzymes and substrates to form enzyme-substrate complexes. Enzyme inhibitors decrease catalytic activity by binding to the active site or elsewhere on the enzyme.
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.
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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.
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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.
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Enzymes are protein catalysts that lower the activation energy of biochemical reactions without being consumed. They achieve specificity by fitting substrates into their active sites. Enzyme activity is regulated through various mechanisms including feedback inhibition, cofactors, pH, temperature, and allosteric regulation. Inhibitors bind enzymes to reduce their activity, either reversibly or irreversibly. Enzymes have many applications in medicine including diagnostics, analytical tests, and enzyme replacement therapy.
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Enzyme catalysis mechanisms involved
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Some of the enzyme possess additional sites, known as allosteric sites besides the active site . Such as know as allosteric enzyme. The allosteric sites are unique place on the enzyme molecules allosteric enzyme have one or more allosteric site.
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This document discusses the classification and nomenclature of enzymes. It describes three naming systems: trivial names which provide no functional information; systematic names which indicate the substrate and type of reaction; and EC (Enzyme Commission) numbers which classify enzymes into six main classes based on the type of chemical reaction catalyzed. The six classes are oxidoreductases, transferases, hydrolases, lyases, isomerases, and ligases. EC numbers are a four-digit code that precisely identifies each enzyme and its catalytic activity.
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Vitamins as coenzymes, different forms and deficiency disorders
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Similar to chemistry of enzymes, ES complex theories, co factors and coenzymes
ENZYMES
It covers enzyme kinetics, classification of enzymes, catalysis, types of catalysis, nomenclature of enzymes, apoenzymes, cofactors, isoenzymes, holoenzyme, factors affecting the rate of chemical reaction, clinical importance of enzymes. It is useful for the students of life sciences and biochemistry as well. The slides help even the teachers teaching basics of enzyme kinetics at the UG and PG levels.
enzymes.pptx
This document discusses enzyme kinetics and the mechanisms of enzyme catalysis. It begins with definitions of key terms like enzyme and catalysis. It then describes classification of enzymes and the structure of active sites. The mechanisms of enzyme catalysis include acid-base, covalent, and metal ion catalysis. It also discusses models of enzyme-substrate binding like lock-and-key and induced fit. Kinetics concepts covered include Michaelis-Menten kinetics, Lineweaver-Burk plots, and factors affecting reaction rates like temperature and pH. Finally, it describes reversible and irreversible inhibition and different types of inhibitors.
ENZYMES Quick Study Notes Slides.pptx
Enzymes are usually proteins that act as catalysts for specific biochemical reactions. They facilitate reactions by lowering their activation energy. Most enzymes have globular structures and contain active sites that allow substrates to bind. Enzymes can be made only of proteins or can require cofactors like coenzymes or metal ions. Enzyme activity is affected by factors like temperature, pH, substrate and enzyme concentration. Enzymes demonstrate specificity for their reactions and substrates. They are regulated by inhibition or through feedback control involving allosteric enzymes and zymogens.
CHEMICAL KINETICS AND ENZYMES B23350B,B223081B,B224645B.pptx
This document discusses chemical kinetics and enzyme kinetics. It defines enzymes as biological catalysts that speed up chemical reactions without being used up in the process. The document describes how enzymes lower the activation energy of reactions and explains the mechanisms of enzyme action, including the lock and key and induced fit hypotheses. It also discusses Michaelis-Menten kinetics and how various factors like temperature, pH, cofactors, and inhibitors can affect the rate of enzyme activity. Allosteric enzymes are defined as having additional binding sites for effector molecules.
Enzymes
Enzymes are protein molecules that facilitate chemical reactions in cells. They lower the activation energy of reactions, acting as catalysts. The enzyme binds to the substrate at its active site, forming an enzyme-substrate complex. This allows the reaction to proceed more easily. Enzyme activity is optimized at specific temperatures, pH levels, and substrate concentrations. It can be inhibited by chemicals that bind to the active site or induce structural changes in the enzyme.
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.
Enzymes
Contents:
Enzymes Terminologies
Enzymes Properties
Mechanism Of Enzyme Action
Factors Affecting Enzyme Activity
Inhibition Of Enzyme
Regulation Of Enzyme Activity
Enzymes
Enzymes mechanism of action, their specificity types, active center structure and action, inhibitor types, fisher and Koshlend theory are presented. Enzymes classification, a new class of enzymes discovered recently, detailed explanation of each class reaction types is presented as well
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.
ENZYMES.pptx
This document discusses enzymes and their properties and functions. It begins by defining enzymes as proteins that act as biological catalysts to accelerate metabolic reactions within cells. Enzymes have several key properties, including that they are proteins, increase reaction rates, function at low concentrations, and catalyze reactions under moderate conditions. The mechanisms of enzyme action involve the binding of specific substrates to the active site of the enzyme, forming an activated transition state complex with a high energy that readily breaks down into products. Enzyme activity can be affected by various factors such as temperature, pH, activators, and inhibitors.
Environmental factors affecting enzymatic reactions.pptx
• Enzymes are catalysts or chemical reagents that speed up chemical reactions without being consumed.
• Most enzymes are proteins that function to reduce energy of activation in chemical reactions.
• Because most enzymes are proteins, their activity is affected by factors that disrupt protein structure, as well as by factors that affect catalysts in general.
Enzymes dr.khushbu
This document provides information on enzymes, including their structure, function, classification, and regulation. It defines enzymes as biological catalysts that speed up biochemical reactions without undergoing permanent change. Enzymes are classified according to the type of chemical reaction they catalyze using the Enzyme Commission system with four digit codes. Enzyme activity can be regulated through various mechanisms including allosteric regulation, covalent modification, proteolytic cleavage, and induction/repression of enzyme synthesis.
Kuliah biokimia enzim
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.
Enzymes msc
This document provides an overview of enzymes, including their structure, function, classification, and kinetics. Some key points:
- Enzymes are biological catalysts that speed up biochemical reactions. They are typically globular proteins that contain an active site for substrate binding.
- Enzymes are classified based on the type of reaction they catalyze, with the major classes being oxidoreductases, transferases, hydrolases, lyases, isomerases, and ligases.
- Enzyme kinetics examines how factors like temperature, pH, and substrate concentration influence the rate of enzyme-catalyzed reactions. Enzymes lower the activation energy needed for reactions, speeding them up.
ENZYMES -enzymes biochemistry.slideshare.pptx
Enzymes are protein catalysts that accelerate biochemical reactions without being consumed in the process. They achieve catalysis through four main mechanisms: proximity of substrates, acid-base catalysis, catalysis by strain, and covalent catalysis. Enzymes are highly specific and contain an active site that binds substrates in a way that lowers their activation energy and facilitates the formation of products.
Enzymes
This document provides an overview of enzymes. It discusses that enzymes are protein catalysts that increase the rate of chemical reactions in living cells without changing themselves. The document describes the different components of enzyme molecules, including the protein component called the apoenzyme and various cofactors that can be organic compounds, inorganic ions, or prosthetic groups. It also discusses the active site of enzymes and mechanisms of enzyme action, such as induced fit and lock and key models. Additionally, it covers factors that affect enzyme activity like temperature, pH, substrate concentration, and enzyme concentration. The document summarizes different types of enzyme inhibition including competitive, non-competitive, and uncompetitive inhibition. Finally, it discusses mechanisms of regulating enzyme activity, including controlling enzyme
ENZYME KINETICS
Enzymes accelerate chemical reactions by lowering the activation energy of the reaction. They do this by providing an alternative pathway for the conversion of substrates to products, involving a transition state with lower energy. The Michaelis-Menten model describes the enzyme-catalyzed reaction, where the enzyme reversibly binds to the substrate to form an enzyme-substrate complex, before yielding products and regenerating the free enzyme. The Michaelis-Menten equation relates the initial reaction velocity to the substrate concentration.
Enzymes
Enzymes are biological molecules (proteins) that act as catalysts and help complex reactions occur everywhere in life. Let's say you ate a piece of meat. Proteases would go to work and help break down the peptide bonds between the amino acids.
Enzyme
Catalysts are something that speeds up the chemical reaction. Almost all biochemical reactions require catalysts.
Enzymes are biocatalysts. Biochemical catalysts speed up the biochemical reactions.
In presence of an enzyme, less energy is required for the reaction to take place.
A catalyst may be defined as a substance that increases the velocity or rate of chemical reactions without itself undergoing any change in the overall process.
Enzymes
Enzymes are biological catalysts that speed up biochemical reactions. They are usually globular proteins with an active site that binds substrates. The active site contains residues that position substrates for reactions. Enzymes lower the activation energy of reactions, increasing rates. Rates depend on factors like temperature, pH, and substrate concentration. Enzymes can be inhibited competitively or non-competitively and reversibly or irreversibly. Michaelis-Menten kinetics describe how reaction rates vary with substrate concentration. Enzymes are important for pharmaceuticals as drug targets.
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CHEMICAL KINETICS AND ENZYMES B23350B,B223081B,B224645B.pptx
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BIOLOGY FORM 4 CHAPTER 4 - CHEMICAL COMPOSITION OF THE CELL PART 2
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This document discusses key concepts in enzyme kinetics including:
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chemistry of enzymes, ES complex theories, co factors and coenzymes
- 2. DEFINITION Enzymes are protein catalysts that increase the rate of reaction without being changed in the overall process. CHARACTERISTICS OF ENZYMES 1. Almost all enzymes are PROTEIN 2. Heat labile. 3. Water soluble. 4. Precipitated by protein precipitating reagents. 5. Contain 16% weight as nitrogen.
- 3. CHEMICAL NATURE OF ENZYMES APOENZYME Protein component of enzyme. HOLOENZYME Apoenzyme + non protein component. CO ENZYME Non protein organic/ metallo organic molecules; non covalently/covalently(prosthetic group) attached to the enzyme.
- 4. CHEMICAL NATURE OF ENZYMES CO FACTORS Inorganic / metallic ions forming a loose, easily dissociable complex. PROSTHETIC GROUP Co factors /co enzymes that are tightly bound to the enzyme.
- 5. TERMINOLOGY SUBSTRATE The substance upon which an enzyme acts is called the substrate. TURNOVER RATE The number of substrate molecules acted upon by an enzyme in one second under appropriate conditions. INTERNATIONAL UNIT Amount of enzyme causing Transformation of 1µmol of substrate/minute under optimal conditions.
- 6. ACTIVITY Total units of enzymes in a given solution. SPECIFIC ACTIVITY Number of enzyme units/mg of total protein. KATAL Amount of an enzyme which catalyzes a reaction rate of 1 mole of substrate/second. TERMINOLOGY
- 7. ACTIVE SITE Special pocket or cleft in an enzyme molecule. Has amino acid side chains for substrate binding & catalysis. ALLOSTERIC SITES Enzymes have allosteric sites(other than active site) where effectors (chemical reagents acting as modifiers) bind through non covalent linkage. TERMINOLOGY
- 9. E-S COMPLEX THEORIES FISCHER΄S TEMPLATE THEORY KOSHLAND΄S INDUCED FIT THEORY
- 12. KOSHLAND΄S INDUCED FIT THEORY
- 13. Enzyme catalyzed reactions have three basic steps; Binding of substrate E + S ES Conversion of bound substrate to bound product ES EP Release of product EP E + P
- 15. MECHANISM OF ENZYME ACTION ENERGY CHANGES CHEMICAL CATALYSIS
- 16. ENERGY CHANGES All chemical reactions have an energy barrier separating the reactants & the products; called free energy of activation--- E –act. ENERGY OF ACTIVATION Energy required to convert all molecules of a reacting substance from the ground state to the transition state.
- 17. TRANSITION STATE High energy intermediates state during the conversion of reactants & the products. A T * B Enzymes greatly decrease the E-act & stabilize the transition state. RATE OF REACTION Rate of reaction is ¹/α to the E-act. > The E-act < the reaction rate.
- 23. CHEMICAL CATALYSIS Catalysis by proximity Acid base catalysis Catalysis by strain Covalent catalysis
- 24. CATALYSIS BY PROXIMITY For molecules to react, they must come within bond forming distance of one another. When enzyme binds substrate molecule at its active site, it creates a region of high local substrate concentration. Orients substrate molecules spatially in a position ideal for them to interact, resulting in rate enhancement .
- 25. ACID BASE CATALYSIS Ionizable functional groups of amino acid side chains & of prosthetic groups act as acids or bases.
- 26. CATALYSIS BY STRAIN Enzymes that catalyze lytic reaction ,involve in breaking of a covalent bond , bind their substrate in a conformation that induces strain in the substrate , converting it into transition state.
- 27. COVALENT CATALYSIS Common among enzymes that catalyze group transfer reaction. Formation of covalent bond b/w enzyme & one or more substrate. Covalent catalysis ↓ the E-act & ↑ the reaction rate. Involves ping – pong mechanism.
- 28. PING – PONG MECHANISM