Topic 4 chapter 5 part 1 enzymes - biological catalysts
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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.
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Enzymes.ppt
This document discusses enzymes and their role in biochemistry. It begins with an introduction to enzymes, noting that they are proteins that act as biological catalysts. It then covers the characteristics, classification, functions, examples, properties, structure, and role of enzymes in metabolism. Enzymes are classified based on the reactions they catalyze. They play important roles in biological processes and have many industrial applications, such as in food processing, brewing, and biofuel production. The structure of enzymes allows them to bind specifically to substrates and catalyze reactions without being used up in the process. Enzymes are essential catalysts that allow metabolic reactions to occur efficiently in living organisms.
Enzymes
The document discusses several key points about enzymes:
- Enzymes are biological catalysts that speed up chemical reactions. Almost all enzymes are proteins, but some nucleic acids called ribozymes can also act as enzymes.
- Enzyme catalysts only work efficiently at temperatures below 40°C, while inorganic catalysts can work at higher temperatures and pressures.
- The enzyme carbonic anhydrase accelerates the reaction of H2CO3 to CO2 and H2O by about 10 million times.
- Cofactors like prosthetic groups, coenzymes, and metal ions are required for enzymatic activity. Prosthetic groups are tightly bound organic compounds, while coenzymes associate
Enzymes
Enzymes are proteins that act as biological catalysts, speeding up chemical reactions in cells without being consumed. They are highly specific and can catalyze reactions like metabolism. Enzymes are composed of amino acid chains and sometimes require cofactors to function. They act by binding to substrates at active sites in a lock-and-key or induced fit mechanism. Factors like temperature, pH, concentration of enzymes and substrates affect reaction rates. Enzymes play important roles in the body like digestion, synthesis, degradation of molecules, and protection against pathogens.
Enzymes
Enzymes are protein catalysts that speed up metabolic reactions inside cells. They have specific active sites that allow only certain substrate molecules to bind via lock and key interactions. Enzymes can be intracellular, acting inside cells, or extracellular, acting outside cells. Experiments show that enzyme activity is optimized at certain temperatures and pH levels, and outside those ranges enzymes become denatured and lose function. Biological detergents use enzymes that can function at low temperatures, providing environmental advantages over traditional detergents.
Enzymes
INTRODUCTION
DEFINITIONS
GENERAL PROPERTIES
CLASSIFICATION
MECHANISM OF ACTION
ENZYME ACTIVITY
ENZYME KINETICS
Enzymes as organic catalysts
Enzymes are proteins that act as catalysts to speed up chemical reactions in cells. They work by lowering the activation energy of reactions. Enzymes specifically bind to substrates at their active sites via lock-and-key or induced fit mechanisms. They speed up reactions without being used up. Enzyme activity is optimized at certain temperatures, pH levels, and substrate/enzyme concentrations and can be inhibited. Examples are named after their substrates except for exceptions like pepsin and trypsin.
Enzymes
1) Enzymes are biological catalysts that regulate specific metabolic functions in the body. They are water soluble, colloidal proteins that speed up biochemical reactions without being consumed in the process.
2) Enzymes can be classified based on their chemistry. Pure protein enzymes are called apoenzymes, while conjugated protein enzymes contain both an apoenzyme portion and a non-protein cofactor or prosthetic group to form the active holoenzyme.
3) Enzyme activity is affected by substrate concentration, temperature, pH, and enzyme concentration according to Michaelis-Menten kinetics and induced fit or lock-and-key mechanisms of enzyme-substrate binding.
Enzymes
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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Enzymes.ppt
This document discusses enzymes and their role in biochemistry. It begins with an introduction to enzymes, noting that they are proteins that act as biological catalysts. It then covers the characteristics, classification, functions, examples, properties, structure, and role of enzymes in metabolism. Enzymes are classified based on the reactions they catalyze. They play important roles in biological processes and have many industrial applications, such as in food processing, brewing, and biofuel production. The structure of enzymes allows them to bind specifically to substrates and catalyze reactions without being used up in the process. Enzymes are essential catalysts that allow metabolic reactions to occur efficiently in living organisms.
Enzymes
The document discusses several key points about enzymes:
- Enzymes are biological catalysts that speed up chemical reactions. Almost all enzymes are proteins, but some nucleic acids called ribozymes can also act as enzymes.
- Enzyme catalysts only work efficiently at temperatures below 40°C, while inorganic catalysts can work at higher temperatures and pressures.
- The enzyme carbonic anhydrase accelerates the reaction of H2CO3 to CO2 and H2O by about 10 million times.
- Cofactors like prosthetic groups, coenzymes, and metal ions are required for enzymatic activity. Prosthetic groups are tightly bound organic compounds, while coenzymes associate
Enzymes
Enzymes are proteins that act as biological catalysts, speeding up chemical reactions in cells without being consumed. They are highly specific and can catalyze reactions like metabolism. Enzymes are composed of amino acid chains and sometimes require cofactors to function. They act by binding to substrates at active sites in a lock-and-key or induced fit mechanism. Factors like temperature, pH, concentration of enzymes and substrates affect reaction rates. Enzymes play important roles in the body like digestion, synthesis, degradation of molecules, and protection against pathogens.
Enzymes
Enzymes are protein catalysts that speed up metabolic reactions inside cells. They have specific active sites that allow only certain substrate molecules to bind via lock and key interactions. Enzymes can be intracellular, acting inside cells, or extracellular, acting outside cells. Experiments show that enzyme activity is optimized at certain temperatures and pH levels, and outside those ranges enzymes become denatured and lose function. Biological detergents use enzymes that can function at low temperatures, providing environmental advantages over traditional detergents.
Enzymes
INTRODUCTION
DEFINITIONS
GENERAL PROPERTIES
CLASSIFICATION
MECHANISM OF ACTION
ENZYME ACTIVITY
ENZYME KINETICS
Enzymes as organic catalysts
Enzymes are proteins that act as catalysts to speed up chemical reactions in cells. They work by lowering the activation energy of reactions. Enzymes specifically bind to substrates at their active sites via lock-and-key or induced fit mechanisms. They speed up reactions without being used up. Enzyme activity is optimized at certain temperatures, pH levels, and substrate/enzyme concentrations and can be inhibited. Examples are named after their substrates except for exceptions like pepsin and trypsin.
Enzymes
1) Enzymes are biological catalysts that regulate specific metabolic functions in the body. They are water soluble, colloidal proteins that speed up biochemical reactions without being consumed in the process.
2) Enzymes can be classified based on their chemistry. Pure protein enzymes are called apoenzymes, while conjugated protein enzymes contain both an apoenzyme portion and a non-protein cofactor or prosthetic group to form the active holoenzyme.
3) Enzyme activity is affected by substrate concentration, temperature, pH, and enzyme concentration according to Michaelis-Menten kinetics and induced fit or lock-and-key mechanisms of enzyme-substrate binding.
Enzymes
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.
Enzyme.ppt
Biochemistry & Molecular biology suject, Created by Asad Chowdhury.
University of Dhaka · Department of Pharmaceutical Chemistry.
IB Chem Topic B7: ENZYMES
Enzymes are biological catalysts that are mostly proteins. They are highly specific and only work within a narrow pH and temperature range. Enzymes catalyze reactions by lowering the activation energy through mechanisms like lock-and-key or induced fit. Their activity depends on factors like substrate concentration, inhibitors, temperature, and pH. The Michaelis constant Km and maximum reaction rate Vmax can be determined graphically and provide information about enzyme-substrate binding and activity levels.
Enzymes ,Lecture-1
Here I have tried to cover the following terms--Enzymes, Definition of enzymes, properties of enzymes, substrates, cofactors, coenzymes, functions of cofactors and coenzmes, water soluble vitamins as coenzymes, definition of active site, features of active site, unit of enzyme
Enzymes
This document discusses enzymes and their properties. It begins by defining enzymes as globular proteins that act as biological catalysts to facilitate chemical reactions in living organisms. It then describes general enzyme characteristics such as their catalytic power, specificity, and ability to have their activity regulated. The document discusses how enzymes are named using systematic and common nomenclature systems. It also covers enzyme classification, cofactors/coenzymes, mechanisms of action, factors that influence activity, and kinetic models like Michaelis-Menten. Overall, the document provides a comprehensive overview of the key concepts regarding enzymes.
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.
Enzymes, Structure, Classification and Mechanism Dr.Kamlesh shah, PSSHDA, KADI
This document defines key terms and concepts related to enzymes. It begins by explaining that enzymes are protein complexes that lower the activation energy of biochemical reactions, accelerating their rate. It then provides definitions for important enzyme terminology, such as substrate, active site, cofactor, and zymogen. The document discusses several models that describe how enzymes catalyze reactions, including the lock-and-key and induced fit hypotheses. It also explains how factors like substrate concentration, pH, temperature, and inhibitors can influence enzyme activity. The key roles of enzymes in biological systems and various applications are also briefly outlined.
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.
Enzymes
Enzymes are biological catalysts, mainly proteins, that speed up chemical reactions in organisms. The first enzyme, diastase, was discovered in 1833 by Payen, and in 1897 Buchner found that yeast cells could ferment sugar without being alive. Enzymes work by lowering the activation energy of reactions, bringing substrates together correctly, and forming enzyme-substrate complexes. They are classified based on the type of reaction catalyzed, such as hydrolases which use water or lyases which remove groups non-hydrolytically. Enzymes have many uses including in food processing, detergents, and paper production.
Enzyme
Enzymes are proteins that catalyze chemical reactions by lowering activation energy. They are not consumed in reactions and can catalyze numerous reaction cycles. Nearly all biological reactions require enzyme catalysis. Enzymes contain active sites that bind specific substrates. The binding forms an enzyme-substrate complex that undergoes reaction, producing products. Cofactors like vitamins and ions can bind enzymes and are required for catalytic activity. The active site is a pocket formed by spatially distant amino acids that binds substrates and performs catalysis. Enzymes are measured in units describing their catalytic activity rate.
Enzymes
Enzymes are protein biocatalysts that increase the rate of chemical reactions without being consumed. They achieve specificity via an active site that binds substrates. The International Union of Biochemistry classifies enzymes into six major classes based on the type of chemical reaction catalyzed. Key factors like temperature, pH, and substrate/product concentration affect an enzyme's activity. Michaelis-Menten kinetics describe the reversible binding of enzymes and substrates to form enzyme-substrate complexes, from which products are released and enzymes recycled. Enzymes can be inhibited reversibly or irreversibly by inhibitors binding to the active site.
Enzymes and co enzymes
Enzymes play important roles in digestion, brewing, diagnosis, and therapeutics. They catalyze reactions in the body, lowering activation energy. Enzymes were first discovered in the 18th century during studies of meat digestion, and it was later established that they are protein catalysts. Enzymes are classified into six major classes based on the type of reactions they catalyze.
Enzymes
Enzymes are biological catalysts that are mostly globular proteins and accelerate biochemical reactions. They are high molecular weight compounds composed of amino acid chains linked by peptide bonds, with molecular weights ranging from 10,000 to 200,000. Enzymes enhance the speed of biochemical reactions, are required in minute amounts, are highly specific to their substrates and reactions, and are sensitive to temperature, pH, and substrate concentration. They lower the activation energy of reactions, can reuse substrates to produce products while remaining unchanged, and form complexes with substrates at their active sites containing 3 to 10 amino acids.
Enzymes
This document provides an overview of enzymes, including their chemistry, classification, mechanisms of action, kinetics, inhibition, and activation. It begins with the basic introduction that enzymes are protein catalysts that speed up biochemical reactions. It then covers enzyme structure and components like cofactors. The major sections explain classification of enzymes based on reaction type, mechanisms like induced fit and catalytic types, kinetics concepts like Michaelis-Menten modeling and factors affecting reaction rates, and types of inhibition like competitive and noncompetitive. The document aims to comprehensively summarize the key topics relating to enzymes.
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
Enzymes are biological catalysts that speed up chemical reactions in cells. They are proteins with an active site that binds to a specific substrate molecule. The enzyme-substrate complex undergoes a reaction, producing products. Each enzyme only works on one substrate. Reaction rates are affected by temperature and pH, with an optimum level. Above or below this, the enzyme denatures and loses function. Enzymes help drive many reactions in living things and industrial processes like breaking down stains or lactose.
MIC310 (Microbial Physiology) - Chapter 4 : Enzymes
Regulatory enzymes control metabolic pathways by catalyzing committed steps. There are five forms of enzyme regulation: substrate availability, allosteric regulation, post-translational modification, and interaction with control proteins. Enzymes lower the activation energy of reactions, allowing them to occur at mild temperatures. Enzymes have specific active sites that substrates bind to, forming enzyme-substrate complexes. Enzyme activity is influenced by temperature, pH, substrate concentration, and inhibitors that can competitively or noncompetitively bind the enzyme. Feedback inhibition regulates pathways by inhibiting early enzymes when end products accumulate.
Enzyme ppt
Enzymes are proteins that act as catalysts to accelerate chemical reactions in living organisms. They are highly specific and only catalyze particular reactions. Enzymes work by weakening the bonds of reactants, reducing the amount of energy needed for the reaction to occur. The substance an enzyme acts on is called the substrate, which binds to the enzyme's active site to induce a shape change that facilitates the reaction. Environmental conditions like temperature and pH can impact enzyme activity, as can cofactors, coenzymes, and enzyme inhibitors.
Chap 10 enzyme
Enzymes are protein molecules produced by living organisms that act as biological catalysts, controlling and accelerating biochemical reactions in cells. They do this by lowering the activation energy needed for reactions to occur. Enzymes have an active site that binds to specific substrate molecules. The binding can cause a slight change in the enzyme's shape through an induced fit mechanism to better bind the substrate and catalyze the reaction. An enzyme's activity is affected by factors like temperature, pH, substrate concentration, and enzyme concentration.
Enzymes
Introduction, Nomenclature of enzymes, Classification of enzymes on the basis of site of action, on the reaction of catalysis and Classification depends upon substrates on they which act, Specificity of Enzymes, Active Site of An Enzyme: 1. Lock-key model 2. Induce fit model, Factors Affecting Enzymes Reaction, Enzyme 1.Inhibition Competitive inhibition, 2. Non-Competitive inhibition, Isoenzymes, Allosteric Enzymes, Co-Factors, Turnover Number of An Enzyme, Pharmaceutical Importance Of Enzymes,
Enzymes
The document provides information about enzymes including:
- Enzymes are protein catalysts that speed up biochemical reactions in living cells. They lower the activation energy of reactions and are not consumed in the process.
- Enzymes have specific three-dimensional structures that allow only specific substrates to bind to their active sites. This contributes to their high reaction specificity.
- Factors like temperature, pH, inhibitors, and cofactors can affect an enzyme's activity level.
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Enzyme.ppt
Biochemistry & Molecular biology suject, Created by Asad Chowdhury.
University of Dhaka · Department of Pharmaceutical Chemistry.
IB Chem Topic B7: ENZYMES
Enzymes are biological catalysts that are mostly proteins. They are highly specific and only work within a narrow pH and temperature range. Enzymes catalyze reactions by lowering the activation energy through mechanisms like lock-and-key or induced fit. Their activity depends on factors like substrate concentration, inhibitors, temperature, and pH. The Michaelis constant Km and maximum reaction rate Vmax can be determined graphically and provide information about enzyme-substrate binding and activity levels.
Enzymes ,Lecture-1
Here I have tried to cover the following terms--Enzymes, Definition of enzymes, properties of enzymes, substrates, cofactors, coenzymes, functions of cofactors and coenzmes, water soluble vitamins as coenzymes, definition of active site, features of active site, unit of enzyme
Enzymes
This document discusses enzymes and their properties. It begins by defining enzymes as globular proteins that act as biological catalysts to facilitate chemical reactions in living organisms. It then describes general enzyme characteristics such as their catalytic power, specificity, and ability to have their activity regulated. The document discusses how enzymes are named using systematic and common nomenclature systems. It also covers enzyme classification, cofactors/coenzymes, mechanisms of action, factors that influence activity, and kinetic models like Michaelis-Menten. Overall, the document provides a comprehensive overview of the key concepts regarding enzymes.
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.
Enzymes, Structure, Classification and Mechanism Dr.Kamlesh shah, PSSHDA, KADI
This document defines key terms and concepts related to enzymes. It begins by explaining that enzymes are protein complexes that lower the activation energy of biochemical reactions, accelerating their rate. It then provides definitions for important enzyme terminology, such as substrate, active site, cofactor, and zymogen. The document discusses several models that describe how enzymes catalyze reactions, including the lock-and-key and induced fit hypotheses. It also explains how factors like substrate concentration, pH, temperature, and inhibitors can influence enzyme activity. The key roles of enzymes in biological systems and various applications are also briefly outlined.
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.
Enzymes
Enzymes are biological catalysts, mainly proteins, that speed up chemical reactions in organisms. The first enzyme, diastase, was discovered in 1833 by Payen, and in 1897 Buchner found that yeast cells could ferment sugar without being alive. Enzymes work by lowering the activation energy of reactions, bringing substrates together correctly, and forming enzyme-substrate complexes. They are classified based on the type of reaction catalyzed, such as hydrolases which use water or lyases which remove groups non-hydrolytically. Enzymes have many uses including in food processing, detergents, and paper production.
Enzyme
Enzymes are proteins that catalyze chemical reactions by lowering activation energy. They are not consumed in reactions and can catalyze numerous reaction cycles. Nearly all biological reactions require enzyme catalysis. Enzymes contain active sites that bind specific substrates. The binding forms an enzyme-substrate complex that undergoes reaction, producing products. Cofactors like vitamins and ions can bind enzymes and are required for catalytic activity. The active site is a pocket formed by spatially distant amino acids that binds substrates and performs catalysis. Enzymes are measured in units describing their catalytic activity rate.
Enzymes
Enzymes are protein biocatalysts that increase the rate of chemical reactions without being consumed. They achieve specificity via an active site that binds substrates. The International Union of Biochemistry classifies enzymes into six major classes based on the type of chemical reaction catalyzed. Key factors like temperature, pH, and substrate/product concentration affect an enzyme's activity. Michaelis-Menten kinetics describe the reversible binding of enzymes and substrates to form enzyme-substrate complexes, from which products are released and enzymes recycled. Enzymes can be inhibited reversibly or irreversibly by inhibitors binding to the active site.
Enzymes and co enzymes
Enzymes play important roles in digestion, brewing, diagnosis, and therapeutics. They catalyze reactions in the body, lowering activation energy. Enzymes were first discovered in the 18th century during studies of meat digestion, and it was later established that they are protein catalysts. Enzymes are classified into six major classes based on the type of reactions they catalyze.
Enzymes
Enzymes are biological catalysts that are mostly globular proteins and accelerate biochemical reactions. They are high molecular weight compounds composed of amino acid chains linked by peptide bonds, with molecular weights ranging from 10,000 to 200,000. Enzymes enhance the speed of biochemical reactions, are required in minute amounts, are highly specific to their substrates and reactions, and are sensitive to temperature, pH, and substrate concentration. They lower the activation energy of reactions, can reuse substrates to produce products while remaining unchanged, and form complexes with substrates at their active sites containing 3 to 10 amino acids.
Enzymes
This document provides an overview of enzymes, including their chemistry, classification, mechanisms of action, kinetics, inhibition, and activation. It begins with the basic introduction that enzymes are protein catalysts that speed up biochemical reactions. It then covers enzyme structure and components like cofactors. The major sections explain classification of enzymes based on reaction type, mechanisms like induced fit and catalytic types, kinetics concepts like Michaelis-Menten modeling and factors affecting reaction rates, and types of inhibition like competitive and noncompetitive. The document aims to comprehensively summarize the key topics relating to enzymes.
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
Enzymes are biological catalysts that speed up chemical reactions in cells. They are proteins with an active site that binds to a specific substrate molecule. The enzyme-substrate complex undergoes a reaction, producing products. Each enzyme only works on one substrate. Reaction rates are affected by temperature and pH, with an optimum level. Above or below this, the enzyme denatures and loses function. Enzymes help drive many reactions in living things and industrial processes like breaking down stains or lactose.
MIC310 (Microbial Physiology) - Chapter 4 : Enzymes
Regulatory enzymes control metabolic pathways by catalyzing committed steps. There are five forms of enzyme regulation: substrate availability, allosteric regulation, post-translational modification, and interaction with control proteins. Enzymes lower the activation energy of reactions, allowing them to occur at mild temperatures. Enzymes have specific active sites that substrates bind to, forming enzyme-substrate complexes. Enzyme activity is influenced by temperature, pH, substrate concentration, and inhibitors that can competitively or noncompetitively bind the enzyme. Feedback inhibition regulates pathways by inhibiting early enzymes when end products accumulate.
Enzyme ppt
Enzymes are proteins that act as catalysts to accelerate chemical reactions in living organisms. They are highly specific and only catalyze particular reactions. Enzymes work by weakening the bonds of reactants, reducing the amount of energy needed for the reaction to occur. The substance an enzyme acts on is called the substrate, which binds to the enzyme's active site to induce a shape change that facilitates the reaction. Environmental conditions like temperature and pH can impact enzyme activity, as can cofactors, coenzymes, and enzyme inhibitors.
Chap 10 enzyme
Enzymes are protein molecules produced by living organisms that act as biological catalysts, controlling and accelerating biochemical reactions in cells. They do this by lowering the activation energy needed for reactions to occur. Enzymes have an active site that binds to specific substrate molecules. The binding can cause a slight change in the enzyme's shape through an induced fit mechanism to better bind the substrate and catalyze the reaction. An enzyme's activity is affected by factors like temperature, pH, substrate concentration, and enzyme concentration.
Enzymes
Introduction, Nomenclature of enzymes, Classification of enzymes on the basis of site of action, on the reaction of catalysis and Classification depends upon substrates on they which act, Specificity of Enzymes, Active Site of An Enzyme: 1. Lock-key model 2. Induce fit model, Factors Affecting Enzymes Reaction, Enzyme 1.Inhibition Competitive inhibition, 2. Non-Competitive inhibition, Isoenzymes, Allosteric Enzymes, Co-Factors, Turnover Number of An Enzyme, Pharmaceutical Importance Of Enzymes,
Enzymes
The document provides information about enzymes including:
- Enzymes are protein catalysts that speed up biochemical reactions in living cells. They lower the activation energy of reactions and are not consumed in the process.
- Enzymes have specific three-dimensional structures that allow only specific substrates to bind to their active sites. This contributes to their high reaction specificity.
- Factors like temperature, pH, inhibitors, and cofactors can affect an enzyme's activity level.
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Enzymes, Structure, Classification and Mechanism Dr.Kamlesh shah, PSSHDA, KADI
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IB Biology 1.2 Slides: Ultrastructure of Cells
Electron microscopes have much higher resolution than light microscopes due to the shorter wavelengths of electron beams. Prokaryotes like E. coli have a simple cell structure without compartments, containing a cell wall, plasma membrane, ribosomes, nucleoid, cytoplasm and other structures. They divide via binary fission. Eukaryotes have a compartmentalized cell structure containing organelles like the nucleus, mitochondria, endoplasmic reticulum, Golgi apparatus, lysosomes, and vacuoles. Organelles in specialized cells like pancreatic and leaf cells are adapted for their functions like enzyme secretion and photosynthesis.
IGCSE Biology - Chemical Coordination in Plants
This PowerPoint answers the following questions:
Do you understand that plants respond to stimuli?
Can you give an example of positive phototropism?
How do plant roots and stems respond to gravity?
It covers section 3.3 of the IGCSE Edexcel Biology Course.
Kingdom Protista, Protist Biology Lesson PowerPoint
This PowerPoint is one small part of the Taxonomy and Classification unit from www.sciencepowerpoint.com. A 3800+ slide Five Part PowerPoint presentation becomes the roadmap for an amazing and interactive science experience full of built-in lab activities, built-in quizzes, video links, class notes(red slides),review games, projects, unit notes, answer keys, and much more. Also included is a student version of the unit that is much like the teachers but missing the answer keys, quizzes, PowerPoint review games, hidden box challenges, owl, and surprises meant for the classroom. This is a great resource to distribute to your students and support professionals. The Classification and Taxonomy Unit covers topics associated with Taxonomy and Classification. The unit examines all of the Kingdoms of Life in detail. Areas of Focus within The Taxonomy and Classification Unit: -Taxonomy, Classification, Need for Taxonomy vs. Common Names, What is a Species?, Dichotomous Keys, What does Classification Use?, The Domains of Life, Kingdoms of Life,The 8 Taxonomic Ranks, Humans Taxonomic Classification, Kingdom Monera, Prokaryotic Cells, Types of Eubacteria, Bacteria Classification, Gram Staining,Bacterial Food Borne Illnesses, Penicillin and Antiseptic, Oral Hygiene and Plaque, Bacterial Reproduction (Binary Fission), Asexual Reproduction, Positives and Negatives of Bacteria, Protista, Plant-like Protists, Animal-like Protists, Fungi-like Protists, Animalia, Characteristics of Animalia, Animal Symmetry, Phylums of Animalia (Extensive), Classes of Chordata, Mammals, Subclasses of Mammals, Characteristics of Mammals, Fungi, Positives and Negatives of Fungi, Divisions of Fungi (Extensive), Parts of a Mushroom, 3 Roles of Fungi, Fungi Reproduction, Mold Prevention, Plant Divisions, Kingdom Plantae. If you have any questions please feel free to contact me. Thanks again and best wishes. Sincerely, Ryan Murphy www.sciencepowerpoint@gmail.com
Kingdom Plantae
The document describes the three divisions of bryophytes - liverworts, mosses, and hornworts. It outlines their key characteristics such as lacking true roots, stems and vascular tissue. Liverworts have a flattened thallus structure or leafy appearance. Mosses have a leafy body and reproduce asexually through budding. Hornworts are distinguished by their horn-like sporophytes. All bryophytes reproduce both sexually and asexually and play an important role as some of the earliest land plants.
Adhesion molecules
This document summarizes several major families of cell adhesion molecules (CAMs) and adhesion receptors. It discusses cadherins, which form homophilic bonds between adjacent cells and link to the cytoskeleton. Integrins are heterodimeric receptors that bind extracellular matrix proteins and require calcium or magnesium. Selectins contain lectin domains that recognize sugar structures on neighboring cells. Neural cell adhesion molecules are single-pass transmembrane proteins important for neural tissue formation.
Kingdom protista[1]
Protists are a diverse kingdom of eukaryotic organisms that are not classified as plants, animals, or fungi. They include both single-celled and multicellular organisms, many of which are aquatic. Protists can be categorized as animal-like, plant-like, or fungus-like depending on their characteristics and behaviors. Animal-like protists include those that use pseudopods, cilia, or flagella to move and feed, as well as non-motile sporozoans that are often parasitic. Plant-like protists include unicellular algae that perform photosynthesis and release oxygen into the environment, providing an important food source. Fungus-like protists absorb nutrients
Presentasi animalia
Kingdom Animalia terdiri dari invertebrata dan vertebrata. Invertebrata terdiri dari 8 filum yaitu Porifera, Coelenterata, Platyhelminthes, Nemathelminthes, Annelida, Mollusca, Arthropoda dan Echinodermata. Vertebrata hanya satu filum yaitu Chordata yang terdiri dari ikan, amfibi, reptil, burung dan mamalia.
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Kingdom Protista, Protist Biology Lesson PowerPoint
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5.2 heterotrophic nutrition UEC Senior 1 Biology
The document discusses mammalian nutrition and digestion. It begins by defining heterotrophic and mammalian nutrition. It then describes the multi-step digestion process, including ingestion, physical and chemical digestion in the mouth, stomach, small intestine, liver and pancreas. Key enzymes and sites of action are identified. Absorption of digested end products like glucose, amino acids and fatty acids occurs in the small intestine. These are then distributed and utilized by cells for energy production or protein/fat synthesis.
Cellular metabolism
The document discusses the control and processes of the digestive system. It explains that digestion is controlled by reflexes triggered by the parasympathetic nervous system and chemical and mechanical receptors. The major organs of digestion - the stomach, small intestine, and pancreas - are described in terms of their roles in breaking down nutrients and absorbing them. The document also provides an overview of cellular metabolism, explaining the catabolic and anabolic processes that break down and build up biomolecules to produce energy and maintain life.
Bioenergetics.pdf
Bioenergetics is the quantitative study of energy conversions that occur in living cells, including sunlight used in photosynthesis, electrical nerve impulses, muscle contractions, and heat from chemical reactions. The major source of biological energy is chemical reactions inside cells. Cellular respiration includes glycolysis, the citric acid cycle, and the electron transport chain, which produce carbon dioxide, water, ATP, and heat. ATP is an important energy carrier that is regenerated through oxidative phosphorylation. Other important energy carriers include NAD+/NADH, FAD/FADH2, and coenzyme A.
LIPIDS- Metabolism of Lipids.pptx
Lipid metabolism entails the oxidation of fatty acids to either generate energy or synthesize new lipids from smaller constituent molecules. Lipid metabolism is associated with carbohydrate metabolism,
E 01 Classification and Properties of enzymes
This document provides information about enzymes, including their properties, classification, and roles in biochemical processes and medicine. Some key points:
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- There are six major classes of enzymes based on the type of reaction catalyzed: oxidoreductases, transferases, hydrolases, lyases, isomerases, and ligases.
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Module 1 Metabolism.pptx
Metabolism describes chemical reactions that maintain living cells and organisms. There are two main types of metabolic reactions: catabolism breaks down molecules, releasing energy, while anabolism uses this energy to build complex molecules. Enzymes catalyze metabolic reactions and allow organisms to couple spontaneous reactions that release energy to drive other reactions. The main biomolecules that make up living things - amino acids, lipids, carbohydrates, and nucleotides - are broken down and synthesized through metabolic pathways.
Biotransfortamion dr. kirran 12th february..2021
This document discusses biotransformation and drug metabolism. It covers topics such as the phases of metabolism, sites of drug metabolism, factors affecting metabolism, and consequences of metabolism such as activation, inactivation, and production of active metabolites. It also discusses concepts like first pass metabolism, enzyme induction, and enzyme inhibition which can impact drug metabolism. Microsomal enzymes like cytochrome P450 play a key role in phase I reactions like oxidation, while phase II involves conjugation reactions adding groups like glucuronic acid to make compounds more water soluble and able to be excreted.
Energy metabolism.pptx
This document discusses the effect of various food processing methods on vitamins and other nutrients. It notes that water-soluble vitamins like vitamin C are more unstable during processing compared to fat-soluble vitamins. High-pressure processing, freezing, pasteurization, dehydration, and microwave drying can all reduce vitamin C levels in foods. Irradiation at low doses has a negligible effect on most vitamins but higher doses can cause losses. The document also discusses changes to proteins, carbohydrates, and lipids during storage and processing, as well as the digestion and absorption of macronutrients.
Drug Metabolism 2023 2nd year mbbs medical students.pptx
Drug metabolism involves the conversion of drugs into other forms through biotransformation in the body. This involves two phases: phase I reactions like oxidation and reduction via cytochrome P450 enzymes in the liver; and phase II conjugation reactions adding subgroups like glucuronide. Biotransformation makes drugs more polar and excretable. The liver is a major site of metabolism via first pass effect. Enzyme inducers increase and inhibitors decrease metabolism, affecting drug concentrations.
Digestive enzymes
This document discusses enzyme digestion in the human digestive system. It explains that chemical digestion uses enzymes to break down food into smaller molecules that can be absorbed. The major organs involved include the liver, gallbladder, and pancreas. The pancreas produces enzymes that digest fats, carbohydrates, and proteins in the small intestine. Hydrolysis is the process by which enzymes break bonds between larger nutrient molecules, converting carbohydrates, lipids, and proteins into simpler forms like sugars, fatty acids, glycerol, and amino acids that can be absorbed. Different enzymes are involved in digesting each macronutrient type at various locations along the digestive tract.
Living state and enzyme introduction
The document discusses the concept of metabolism and the dynamic state of body constituents. It defines metabolism as the set of chemical reactions in living organisms that break down biomolecules to release energy and build up new complex structures. Biomolecules are constantly being broken down and resynthesized through metabolic pathways, which are series of enzyme-catalyzed reactions. This dynamic state allows organisms to maintain concentrations of biomolecules and exist in a non-equilibrium steady state, which is necessary for life. Metabolism provides a mechanism for energy production to power biological work through ATP.
biochemistry2-160609131435, I vjvuv, udita g,,ucucigig,xycuvivhufugigohof। ज...
Proteins are polymers of amino acids that play essential roles in living organisms. They have complex structures ranging from primary to quaternary levels defined by amino acid sequences and folding patterns. Major classes of proteins include simple proteins like albumins and globulins, conjugated proteins with attached groups like glycoproteins, and derived proteins from digestion. Proteins are critical for structures, chemical processes, oxygen transport, and heredity through roles as enzymes, hemoglobin, nucleoproteins, and more. They are thus vital molecules for life.
Chapter 1 the chemical nature of cells
This document provides an overview of the key biomolecules found within cells, including their structure and functions. It discusses the roles of water, carbohydrates like glucose and glycogen, lipids, proteins, and nucleic acids such as DNA and RNA. These biomolecules are involved in essential cellular processes like metabolism, protein synthesis, and storage of genetic information. The document also examines how biomolecules interact and are organized within cells and cellular structures.
PCI - BPH4 - METABOLISM chapter pdf simple
Metabolism involves enzyme-catalyzed reactions that convert substances in the body. Drug metabolism occurs mainly in the liver and involves two phases: phase I reactions like oxidation, reduction, and hydrolysis that functionalize drugs; and phase II conjugation reactions that make drugs more polar for excretion. Cytochrome P450 enzymes are an important family of mixed function oxidases in the liver endoplasmic reticulum that catalyze many phase I oxidative reactions using oxygen, NADPH, and electrons.
final_starvation-16.pptx
During starvation, the body goes through four stages of metabolic adaptation to utilize its stored fuels. In the first stage, glycogen stores are broken down. In the second, gluconeogenesis increases to maintain blood glucose levels. In the third stage, lipolysis and fatty acid oxidation increase to provide energy. Finally, in the fourth stage, ketone bodies are produced from fatty acids to serve as an alternative fuel for tissues like the brain. Hormonal changes like decreased insulin and increased glucagon, epinephrine help stimulate these metabolic pathways and allow the body to survive on its endogenous reserves during periods of starvation.
Proteins and peptides
1. The document discusses various topics related to proteins and peptides, including what proteins are, their properties, classification, metabolism, and some protein-related disorders.
2. Key points include that proteins are composed of amino acids and are essential for human life, occurring in all cells. They can be classified based on their structure as globular, fibrous or membrane proteins.
3. Protein metabolism involves breaking down proteins through catabolism and building new proteins through anabolism. The urea cycle is involved in detoxifying ammonia produced from amino acid catabolism.
4. Some protein-related disorders discussed are maple syrup urine disease, Gaucher disease, kwashiorkor, and
Core 6.1 and Option D1-D3
The document summarizes key aspects of human digestion and nutrition. It describes the main stages of digestion that occur in the oral cavity, stomach, small intestine and large intestine. Key points include:
- Digestion involves both physical and chemical breakdown of food facilitated by enzymes and accessory organs like the liver and pancreas.
- The small intestine is the primary site of nutrient absorption into the bloodstream through processes like diffusion, facilitated diffusion and active transport.
- The liver plays an important role in regulating blood composition and nutrient storage/processing through functions like detoxification, bile production, and albumin synthesis.
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Enterohepatic circulation.ppt
The liver has several important functions:
1. It stores, metabolizes, and releases nutrients and vitamins while also detoxifying and eliminating toxins, drugs, and metabolites.
2. The liver synthesizes important proteins like albumin, clotting factors, and apolipoproteins. It also synthesizes and secretes bile which aids in lipid digestion and absorption.
3. The liver plays a role in immune function and clears intestinally absorbed bacteria.
Bmm480 Enzymology lecture-1
This document outlines the syllabus for a course on enzymology taught at TOBB University of Economics and Technology. The course covers topics such as how enzymes work, enzyme kinetics, inhibition and clinical applications over 12 weeks. Students will present on various metabolic pathways and enzyme-related subjects. The course aims to explain why enzymes are important and their roles in various industries like food engineering. Evaluation will be based on midterm and final exams, as well as a presentation homework assignment.
Digestion and Nutrition 2016 (Core and Option D)
The document summarizes key aspects of human digestion and nutrition. It describes the five stages of food processing: ingestion, digestion, absorption, assimilation, and egestion. It details the organs and structures involved in digestion, including the oral cavity, esophagus, stomach, small intestine, large intestine, liver, and pancreas. It explains the roles of enzymes and hormones in breaking down food and regulating digestion. The document also covers nutrient absorption in the small intestine and discusses nutrition, including energy sources, vitamins, minerals, and essential nutrients required in the diet.
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Drug Metabolism 2023 2nd year mbbs medical students.pptx
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Molecular genetics 2 win q
This document discusses genetic engineering techniques such as transferring genes between organisms using vectors like plasmids, creating transgenic organisms like bacteria that express human genes to produce proteins like insulin, and potential benefits and disadvantages of genetic engineering including more affordable medicines, crop improvements, but also environmental, economic, health, and social/ethical risks.
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.
Topic 11 Excretion
The document provides instructions for comparing urine samples from two subjects and identifying which sample belongs to each subject. It discusses observing the color, volume, smell, temperature, and texture/taste of solutions A and B. Subject X's urine was collected one hour after drinking water, while subject Y's urine was not collected for 5 hours without drinking water. The document also contains information about the structure and functions of the urinary system.
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 3 enzymes - limiting factors
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.
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 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 3 enzymes - limiting factors
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Topic 4 chapter 5 part 1 enzymes - biological catalysts
- 1. Topic 4: Chapter 5 EnzymesEnzymes –– Part 1Part 1 Biological Biological Catalysts Catalysts
- 2. What are Catalysts? • Substances which can alter or speed up a chemical reaction, • without itself being chemically changed at the end of the reaction. • Substances which can alter or speed up a chemical reaction, • without itself being chemically changed at the end of the reaction.
- 3. CatalystsCatalysts (A) Inorganic • Iron – Haber process • Vanadium (v) Oxide – production of sulphuric acid • Manganese (IV) Oxide (A) Inorganic • Iron – Haber process • Vanadium (v) Oxide – production of sulphuric acid • Manganese (IV) Oxide (B) Organic • Digestive enzymes • Metabolic enzymes (B) Organic • Digestive enzymes • Metabolic enzymes
- 4. • Enzymes are biological catalysts • which are mainly proteins that are produced by living cells. • Enzymes can be DENATURED by heating or by changes in the pH of the solution • E.g. Digestive enzymes, Metabolic enzymes (B) Organic Catalysts(B) Organic Catalysts
- 5. The function of enzymes • How is energy released from sugar (glucose)? • But how can our cells provide such high temperatures during cellular respiration to release energy from glucose?? Glucose + Oxygen Carbon dioxide + Water + Energy Strong Heat
- 6. The function of enzymes Lower Activation EnergyLower Activation Energy • Activation Energy: Energy required to start a chemical reaction. Activation Energy with enzyme Activation Energy without enzyme Reactants (Substrate): (Glucose + Oxygen) Products: (Carbon dioxide + water) Energy Time
- 7. Enzyme-Catalyzed ReactionsEnzyme-Catalyzed Reactions (A) Synthesis of complex substances Anabolic Reactions • Protein synthesis • Photosynthesis • Conversion of glucose to glycogen • etc… (A) Synthesis of complex substances Anabolic Reactions • Protein synthesis • Photosynthesis • Conversion of glucose to glycogen • etc… (B) Breaking down of complex substances Catabolic Reactions • Digestion • Cellular Respiration • Detoxification in the liver and blood by catalase • etc… (B) Breaking down of complex substances Catabolic Reactions • Digestion • Cellular Respiration • Detoxification in the liver and blood by catalase • etc…
- 8. Enzyme-Catalyzed Anabolic ReactionsEnzyme-Catalyzed Anabolic Reactions Protein SynthesisProtein Synthesis • Synthesis of proteins from amino acids in the cytoplasm PhotosynthesisPhotosynthesis • Synthesis of sugar from carbon dioxide and water Glycogen formationGlycogen formation • Conversion of glucose to glycogen for storage.
- 9. Enzyme-Catalyzed Catabolic ReactionsEnzyme-Catalyzed Catabolic Reactions DigestionDigestion • Breakdown of complex food substances to smaller, simpler, more soluble and diffusible substances. • So that food can pass through the cell membrane and be absorbed into the bloodstream. • Enzymes involved – Hydrolases (e.g Carbohydrases, Proteases and Lipases)
- 10. Enzyme-Catalyzed Catabolic ReactionsEnzyme-Catalyzed Catabolic Reactions Cellular RespirationCellular Respiration • Oxidation of glucose by cells to release energy. • Many enzymes involved
- 11. Enzyme-Catalyzed Catabolic ReactionsEnzyme-Catalyzed Catabolic Reactions Detoxification in the liver and bloodDetoxification in the liver and blood • Conversion of toxic to non-toxic substances • Example: Conversion of toxic Hydrogen peroxide, H2O2 (a by-product of cellular respiration) to non- toxic water and oxygen by enzyme CATALASE
- 12. Classification of enzymes HydrolasesHydrolases • Enzymes that catalyzes hydrolytic reactions which involves the addition of water molecules to breakdown a complex molecule • Examples of hydrolytic reactions: Digestion of carbohydrates, proteins & fats
- 13. Classification of enzymes HydrolasesHydrolases Types of Hydrolases Example(s) Substrate Carbohydrases Salivary and pancreatic amylase Starch Cellulase produced by some bacteria Cellulose Proteases Pepsin produced in the stomach Proteins Trypsin produced as an inactive form (trypsinogen) by the pancreas Proteins Erepsin produced by intestinal glands Polypeptides Lipases Pancreatic and Intestinal lipases Fats
- 14. Classification of enzymes Oxidation-Reduction EnzymesOxidation-Reduction Enzymes • Enzymes that are involved in cellular respiration. • Breaks down glucose to release energy, carbon dioxide and water
- 15. 15 Test yourself With questions in Textbook Page 75
- 16. 16 Test yourself – pg 75 - answers 1 An enzyme is a biological catalyst made of protein. It alters the rate of a chemical reaction without itself being chemically changed at the end of the reaction.
- 17. 17 Test yourself – pg 75 - answers 2 Yes, the statement is valid. Large, insoluble molecules such as carbohydrates, fats and proteins cannot diffuse through the cell surface membrane. They must first be converted into simpler, smaller substances, which are soluble and diffusible.
- 18. 18 Test yourself – pg 75 - answers 3 Meat contains mostly proteins, hence we can infer that this enzyme acts on proteins. The enzyme could soften meat by breaking down the proteins into peptides or amino acids.
- 19. 19 Test yourself – pg 75 - answers 4 A very rapid, violent chemical reaction would take place, with a thick layer of foam produced. Water and oxygen are produced when catalase in the red blood cells breaks down hydrogen peroxide.