This document provides information about enzymes including their definition, classification, nomenclature, characteristics, and factors that affect their activity. Some key points:
- Enzymes are proteins that act as catalysts for biochemical reactions in living cells and are highly specific. There are six major classes of enzymes based on the type of reaction they catalyze.
- Classification systems such as IUBMB provide unambiguous names for enzymes based on the reaction they catalyze.
- Enzymes have an active site where substrates bind and catalytic residues that participate in reactions. Cofactors such as metals and organic molecules are required for some enzymes to function.
- Factors like concentration of enzyme and substrate, temperature, pH
What are Enzymes; Properties of enzymes; Classification of Enzyme; Mechanism of action of enzyme; Enzyme-Substrate Interactions; Enzyme Activation; Enzyme Inhibition; What are Coenzymes; Salient features of coenzyme; Some Co-Enzymes & its function.
History
Introduction
Functions
Classification – Monosaccharides
Disaccharides
Oligosaccharides
Polysaccharides
Digestion of carbohydrates
Absorption of carbohydrates
Dietary guidelines
Carbohydrates and oral health
Nutritional health programs in India
Public health significance
The tricarboxylic acid (TCA) cycle is a series of enzyme-catalyzed reactions that forms a key part of aerobic respiration in cells. It was discovered by Hans Krebs in 1937 and is also known as the Krebs cycle or citric acid cycle. The cycle occupies a central position in metabolism, using acetate to generate carbon dioxide, reducing agents like NADH, and ATP through oxidative phosphorylation. It provides precursors for amino acid and nucleotide biosynthesis. The cycle is critical for generating the majority of a cell's energy needs through the complete oxidation of carbohydrates, fatty acids, and amino acids.
The document discusses the immune system and its response to foreign substances called antigens. It describes innate immunity, which is present from birth, and acquired immunity, which develops through exposure to antigens. Passive immunity provides temporary protection through antibodies transferred from mother to infant or through immunization. The document also details the structure and classification of immunoglobulins, which are antibody proteins produced by B cells in response to antigens.
This document discusses proteins, including their structure, function, digestion, and importance. It notes that proteins are made up of amino acids and are essential for building muscle mass. During digestion, proteins are broken down into amino acids in the stomach and small intestine through chemical and mechanical processes aided by enzymes. The amino acids are then absorbed and transported to cells to build new proteins. Maintaining a variety of protein sources in the diet is important for health.
Composition and metabolism of carbohydrates by Dr. Pallavi PathaniaDR .PALLAVI PATHANIA
This document discusses carbohydrate metabolism, including glycolysis, gluconeogenesis, glycogenolysis, the pentose phosphate pathway, and blood sugar regulation. It explains that glycolysis breaks down glucose into pyruvate, producing a small amount of ATP. Gluconeogenesis converts non-carbohydrates into glucose when glycogen stores are depleted. The Cori cycle involves the liver converting lactate from muscles back into glucose. The TCA cycle further breaks down pyruvate from glycolysis to generate more ATP. Glycogenolysis breaks down glycogen into glucose as needed. The pentose phosphate pathway generates NADPH and pentoses from glucose-6-phosphate. Hormones like insulin regulate blood sugar levels.
Proteins are composed of amino acids that link together via peptide bonds. There are 20 naturally occurring amino acids that vary in properties like polarity, charge, and ability to form secondary structures. The sequence and interactions of amino acids give proteins their unique 3D structures and functions. Denaturation disrupts non-covalent bonds within proteins, altering their shapes and eliminating biological activity.
What are Enzymes; Properties of enzymes; Classification of Enzyme; Mechanism of action of enzyme; Enzyme-Substrate Interactions; Enzyme Activation; Enzyme Inhibition; What are Coenzymes; Salient features of coenzyme; Some Co-Enzymes & its function.
History
Introduction
Functions
Classification – Monosaccharides
Disaccharides
Oligosaccharides
Polysaccharides
Digestion of carbohydrates
Absorption of carbohydrates
Dietary guidelines
Carbohydrates and oral health
Nutritional health programs in India
Public health significance
The tricarboxylic acid (TCA) cycle is a series of enzyme-catalyzed reactions that forms a key part of aerobic respiration in cells. It was discovered by Hans Krebs in 1937 and is also known as the Krebs cycle or citric acid cycle. The cycle occupies a central position in metabolism, using acetate to generate carbon dioxide, reducing agents like NADH, and ATP through oxidative phosphorylation. It provides precursors for amino acid and nucleotide biosynthesis. The cycle is critical for generating the majority of a cell's energy needs through the complete oxidation of carbohydrates, fatty acids, and amino acids.
The document discusses the immune system and its response to foreign substances called antigens. It describes innate immunity, which is present from birth, and acquired immunity, which develops through exposure to antigens. Passive immunity provides temporary protection through antibodies transferred from mother to infant or through immunization. The document also details the structure and classification of immunoglobulins, which are antibody proteins produced by B cells in response to antigens.
This document discusses proteins, including their structure, function, digestion, and importance. It notes that proteins are made up of amino acids and are essential for building muscle mass. During digestion, proteins are broken down into amino acids in the stomach and small intestine through chemical and mechanical processes aided by enzymes. The amino acids are then absorbed and transported to cells to build new proteins. Maintaining a variety of protein sources in the diet is important for health.
Composition and metabolism of carbohydrates by Dr. Pallavi PathaniaDR .PALLAVI PATHANIA
This document discusses carbohydrate metabolism, including glycolysis, gluconeogenesis, glycogenolysis, the pentose phosphate pathway, and blood sugar regulation. It explains that glycolysis breaks down glucose into pyruvate, producing a small amount of ATP. Gluconeogenesis converts non-carbohydrates into glucose when glycogen stores are depleted. The Cori cycle involves the liver converting lactate from muscles back into glucose. The TCA cycle further breaks down pyruvate from glycolysis to generate more ATP. Glycogenolysis breaks down glycogen into glucose as needed. The pentose phosphate pathway generates NADPH and pentoses from glucose-6-phosphate. Hormones like insulin regulate blood sugar levels.
Proteins are composed of amino acids that link together via peptide bonds. There are 20 naturally occurring amino acids that vary in properties like polarity, charge, and ability to form secondary structures. The sequence and interactions of amino acids give proteins their unique 3D structures and functions. Denaturation disrupts non-covalent bonds within proteins, altering their shapes and eliminating biological activity.
Carbohydrates are an important source of energy. They include sugars, starches, and fiber. Sugars are small, simple carbohydrates like glucose, fructose, and galactose. Starches are complex carbohydrates made of linked glucose units. Fiber is a type of carbohydrate that the body cannot digest. The body breaks down carbohydrates into glucose for energy or stores them as glycogen in the liver and muscles. A balanced diet should obtain about 40-60% of calories from carbohydrates to fuel the body and brain. Too little or too much carbohydrate intake can impair health.
CARBOHYDRATES AND THEIR METABOLISM for nurses - P.B.Sc.pptxNamita Batra
This document provides information on carbohydrates including their classification, structure, and roles. It discusses monosaccharides, disaccharides, oligosaccharides, and polysaccharides. Key points include: monosaccharides cannot be further hydrolyzed; examples include glucose, fructose, and galactose. Disaccharides are double sugars formed from two monosaccharides joined by a glycosidic bond. Examples include sucrose, lactose, and maltose. Polysaccharides serve as energy stores and structural components in plants and animals. Glycogen and starch are examples of storage polysaccharides.
Digestion and absorption of lipids ppt
what is lipid ppt
digestion of lipid ppt
phase of digestion and absorption ppt
phases of lipids ppt
digestion in mouth and stomach ppt
digestion in small intestine ppt
secretion of lipids ppt
enzyme involved in lipid digestion ppt
transportation phases of lipids ppt
principles of lipid digestion ppt
The TCA cycle, also known as the Krebs cycle or citric acid cycle, is the central metabolic pathway that catalyzes the oxidation of acetyl-CoA derived from carbohydrates, fats, and proteins to produce carbon dioxide, water, and energy in the form of ATP, NADH, and FADH2. The TCA cycle occurs in the mitochondrial matrix and is the final common pathway for the oxidation of these three macronutrient types. Through a series of chemical reactions, acetyl-CoA is oxidized, producing carbon dioxide and hydrogen ions that will be used in the electron transport chain to generate ATP through oxidative phosphorylation.
Proteins are naturally occurring polymers made up of amino acids and linked together by peptide bonds.
Proteins are the most abundant organic molecules in the living system.
The term "protein" is derived from the Greek word proteios, meaning holding the first place.
These are nitrogenous organic compounds that have large molecules weight of one or more long chains of amino acids.
Proteins are made from 20 ɑ-amino acids. (chains of amino acids)
A single unit of amino acid is known as a monomer. When many monomers combine together, they form polymers.
Anomers are carbohydrate structures that differ only in the configuration of the hydroxyl group on the anomeric carbon. The anomeric carbon is the carbon atom involved in the cyclic formation of carbohydrates. Examples of anomers are alpha-glucose and beta-glucose which have different hydroxyl group positions on the first carbon. Epimers differ at only one other chiral carbon, not the anomeric carbon, while mutarotation is the process where glucose anomers interconvert between ring forms in solution.
The document discusses cholesterol, including its structure, functions, synthesis, regulation, and levels in the body. Some key points:
- Cholesterol is the major sterol in animal tissues and is present as free cholesterol or combined with fatty acids.
- It performs essential functions like being a membrane component, precursor for bile acids and steroid hormones, and is required for nerve transmission.
- Cholesterol is derived from diet, de novo synthesis in the body, and hydrolysis of cholesteryl esters.
- The rate-limiting enzyme for its synthesis is HMG-CoA reductase, which is regulated by feedback inhibition and hormones like insulin and glucagon.
Lipids are a heterogeneous group of compounds that are insoluble in water but soluble in organic solvents. They are classified into simple lipids, compound lipids, and derived lipids. Simple lipids include fats and oils (esters of fatty acids and glycerol) and waxes (esters of fatty acids and higher alcohols). Compound lipids contain additional groups like phosphate, carbohydrates, or sulfur. Phospholipids and glycolipids are examples. Derived lipids are produced from simple and compound lipids and include fatty acids, cholesterol, and hormones. Fatty acids are the building blocks of lipids and are classified as saturated or unsaturated based on double bond presence. Lipids serve important roles in energy storage
The TCA cycle (also known as the Krebs cycle or citric acid cycle) is a series of chemical reactions in the mitochondria that breaks down acetyl-CoA molecules derived from carbohydrates, fats, and proteins into carbon dioxide. It is a cyclic process where oxaloacetate is regenerated at the end of each cycle. The cycle produces reduced electron carriers NADH and FADH2 that feed into the electron transport chain to generate ATP through oxidative phosphorylation. It is a central metabolic hub that connects several biochemical pathways and provides precursors for biosynthesis.
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.
The document discusses the tricarboxylic acid (TCA) cycle, also known as the Krebs cycle or citric acid cycle. It provides three key points:
1. The TCA cycle involves the oxidation of acetyl-CoA to carbon dioxide and water and is the final common pathway for carbohydrates, fats, and amino acids.
2. The cycle generates energy in the form of ATP, NADH, and FADH2 and provides precursors for biosynthesis.
3. The cycle occurs in the mitochondrial matrix and is tightly regulated by enzymes and cellular energy levels to integrate major metabolic pathways.
This document discusses enzymes, coenzymes, and cofactors. It covers the classification, structure, and function of enzymes. Key points include:
1. Enzymes are proteins that act as catalysts and increase the rate of biochemical reactions without being consumed.
2. Coenzymes and cofactors are non-protein molecules required for enzymatic activity. Coenzymes include NAD+, FAD, and ATP.
3. Enzymes can be classified based on their catalytic action, such as oxidoreductases, transferases, hydrolases, lyases, isomerases, and ligases.
1) Fatty acids are oxidized through beta-oxidation in the mitochondria to generate acetyl-CoA units and energy in the form of ATP.
2) Beta-oxidation involves four steps - dehydrogenation, hydration, dehydrogenation, and thiolysis - that occur in a recurring cycle to shorten the fatty acid by two carbons each time.
3) Fatty acid oxidation provides the major source of energy during periods of fasting or low carbohydrate availability and yields substantial ATP through the electron transport chain.
This document discusses various applications of enzymes in diagnostics, therapeutics, and analytical testing. It provides examples of enzymes used as diagnostic markers for conditions like myocardial infarction. It also outlines some therapeutic uses of enzymes like streptokinase to break up blood clots and asparaginase in cancer treatment. Finally, it notes analytical applications of enzymes in techniques like ELISA and uses in industries like food production and DNA analysis.
Carbohydrates are biomolecules composed of carbon, hydrogen, and oxygen. They are classified as monosaccharides, oligosaccharides, or polysaccharides depending on the number of monomer units present. Monosaccharides include simple sugars like glucose and fructose. Disaccharides are formed from two monosaccharides joined by a glycosidic bond, examples being sucrose and lactose. Polysaccharides are polymers of monosaccharides and include starch, glycogen, and cellulose. Carbohydrates serve important functions as energy sources, structural components of cells and organisms, and precursors for other biomolecules.
The document summarizes protein metabolism and the urea cycle. It discusses that 1-2% of body proteins are degraded and renewed daily. Ammonia produced is highly toxic, so the liver converts it to urea. Glutamine synthase fixes ammonia as non-toxic glutamine and glutaminase releases it for urea synthesis. The urea cycle uses ammonia, CO2, and aspartate to synthesize urea using 5 enzymes in the liver. Rare metabolic disorders can cause urea synthesis blockage, increasing blood ammonia and risking intoxication and brain damage. Treatments include low-protein diets and frequent small meals to avoid sudden ammonia increases.
Citric acid cycle (TCA cycle) by Dr. Anurag YadavDr Anurag Yadav
The citric acid cycle, also known as the Krebs cycle or TCA cycle, is the final common pathway for the oxidation of acetyl CoA derived from carbohydrates, fats, and proteins. The cycle consists of 8 steps that oxidize acetyl CoA completely to carbon dioxide, producing reduced coenzymes NADH and FADH2 that fuel the electron transport chain. The cycle takes place in the mitochondrial matrix and generates ATP through substrate-level phosphorylation. It also provides precursors for biosynthesis and integrates various metabolic pathways. Defects in enzymes of the citric acid cycle can cause various metabolic disorders.
The document provides an overview of enzymology and enzyme catalysis. It discusses:
1. The teaching objectives which are to introduce enzymes as catalysts, classify enzyme types and mechanisms, illustrate enzyme kinetics, highlight mechanisms of enzyme regulation and clinical importance.
2. Key characteristics of enzyme-catalyzed reactions including high specificity and regulation in response to changes.
3. Mechanisms by which enzymes catalyze reactions including proximity and orientation effects, transition state stabilization, and acid/base catalysis.
This document provides an overview of enzymes, including their chemistry, nomenclature, classification, mechanisms of action, and factors that affect enzyme activity. It discusses how enzymes are proteins that act as biological catalysts, lowering the activation energy of biochemical reactions. Enzymes are classified according to the type of chemical reactions they catalyze into six main classes: oxidoreductases, transferases, hydrolases, lyases, isomerases, and ligases. The document also covers enzyme kinetics, regulation, diagnostic and therapeutic uses of enzymes.
Carbohydrates are an important source of energy. They include sugars, starches, and fiber. Sugars are small, simple carbohydrates like glucose, fructose, and galactose. Starches are complex carbohydrates made of linked glucose units. Fiber is a type of carbohydrate that the body cannot digest. The body breaks down carbohydrates into glucose for energy or stores them as glycogen in the liver and muscles. A balanced diet should obtain about 40-60% of calories from carbohydrates to fuel the body and brain. Too little or too much carbohydrate intake can impair health.
CARBOHYDRATES AND THEIR METABOLISM for nurses - P.B.Sc.pptxNamita Batra
This document provides information on carbohydrates including their classification, structure, and roles. It discusses monosaccharides, disaccharides, oligosaccharides, and polysaccharides. Key points include: monosaccharides cannot be further hydrolyzed; examples include glucose, fructose, and galactose. Disaccharides are double sugars formed from two monosaccharides joined by a glycosidic bond. Examples include sucrose, lactose, and maltose. Polysaccharides serve as energy stores and structural components in plants and animals. Glycogen and starch are examples of storage polysaccharides.
Digestion and absorption of lipids ppt
what is lipid ppt
digestion of lipid ppt
phase of digestion and absorption ppt
phases of lipids ppt
digestion in mouth and stomach ppt
digestion in small intestine ppt
secretion of lipids ppt
enzyme involved in lipid digestion ppt
transportation phases of lipids ppt
principles of lipid digestion ppt
The TCA cycle, also known as the Krebs cycle or citric acid cycle, is the central metabolic pathway that catalyzes the oxidation of acetyl-CoA derived from carbohydrates, fats, and proteins to produce carbon dioxide, water, and energy in the form of ATP, NADH, and FADH2. The TCA cycle occurs in the mitochondrial matrix and is the final common pathway for the oxidation of these three macronutrient types. Through a series of chemical reactions, acetyl-CoA is oxidized, producing carbon dioxide and hydrogen ions that will be used in the electron transport chain to generate ATP through oxidative phosphorylation.
Proteins are naturally occurring polymers made up of amino acids and linked together by peptide bonds.
Proteins are the most abundant organic molecules in the living system.
The term "protein" is derived from the Greek word proteios, meaning holding the first place.
These are nitrogenous organic compounds that have large molecules weight of one or more long chains of amino acids.
Proteins are made from 20 ɑ-amino acids. (chains of amino acids)
A single unit of amino acid is known as a monomer. When many monomers combine together, they form polymers.
Anomers are carbohydrate structures that differ only in the configuration of the hydroxyl group on the anomeric carbon. The anomeric carbon is the carbon atom involved in the cyclic formation of carbohydrates. Examples of anomers are alpha-glucose and beta-glucose which have different hydroxyl group positions on the first carbon. Epimers differ at only one other chiral carbon, not the anomeric carbon, while mutarotation is the process where glucose anomers interconvert between ring forms in solution.
The document discusses cholesterol, including its structure, functions, synthesis, regulation, and levels in the body. Some key points:
- Cholesterol is the major sterol in animal tissues and is present as free cholesterol or combined with fatty acids.
- It performs essential functions like being a membrane component, precursor for bile acids and steroid hormones, and is required for nerve transmission.
- Cholesterol is derived from diet, de novo synthesis in the body, and hydrolysis of cholesteryl esters.
- The rate-limiting enzyme for its synthesis is HMG-CoA reductase, which is regulated by feedback inhibition and hormones like insulin and glucagon.
Lipids are a heterogeneous group of compounds that are insoluble in water but soluble in organic solvents. They are classified into simple lipids, compound lipids, and derived lipids. Simple lipids include fats and oils (esters of fatty acids and glycerol) and waxes (esters of fatty acids and higher alcohols). Compound lipids contain additional groups like phosphate, carbohydrates, or sulfur. Phospholipids and glycolipids are examples. Derived lipids are produced from simple and compound lipids and include fatty acids, cholesterol, and hormones. Fatty acids are the building blocks of lipids and are classified as saturated or unsaturated based on double bond presence. Lipids serve important roles in energy storage
The TCA cycle (also known as the Krebs cycle or citric acid cycle) is a series of chemical reactions in the mitochondria that breaks down acetyl-CoA molecules derived from carbohydrates, fats, and proteins into carbon dioxide. It is a cyclic process where oxaloacetate is regenerated at the end of each cycle. The cycle produces reduced electron carriers NADH and FADH2 that feed into the electron transport chain to generate ATP through oxidative phosphorylation. It is a central metabolic hub that connects several biochemical pathways and provides precursors for biosynthesis.
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.
The document discusses the tricarboxylic acid (TCA) cycle, also known as the Krebs cycle or citric acid cycle. It provides three key points:
1. The TCA cycle involves the oxidation of acetyl-CoA to carbon dioxide and water and is the final common pathway for carbohydrates, fats, and amino acids.
2. The cycle generates energy in the form of ATP, NADH, and FADH2 and provides precursors for biosynthesis.
3. The cycle occurs in the mitochondrial matrix and is tightly regulated by enzymes and cellular energy levels to integrate major metabolic pathways.
This document discusses enzymes, coenzymes, and cofactors. It covers the classification, structure, and function of enzymes. Key points include:
1. Enzymes are proteins that act as catalysts and increase the rate of biochemical reactions without being consumed.
2. Coenzymes and cofactors are non-protein molecules required for enzymatic activity. Coenzymes include NAD+, FAD, and ATP.
3. Enzymes can be classified based on their catalytic action, such as oxidoreductases, transferases, hydrolases, lyases, isomerases, and ligases.
1) Fatty acids are oxidized through beta-oxidation in the mitochondria to generate acetyl-CoA units and energy in the form of ATP.
2) Beta-oxidation involves four steps - dehydrogenation, hydration, dehydrogenation, and thiolysis - that occur in a recurring cycle to shorten the fatty acid by two carbons each time.
3) Fatty acid oxidation provides the major source of energy during periods of fasting or low carbohydrate availability and yields substantial ATP through the electron transport chain.
This document discusses various applications of enzymes in diagnostics, therapeutics, and analytical testing. It provides examples of enzymes used as diagnostic markers for conditions like myocardial infarction. It also outlines some therapeutic uses of enzymes like streptokinase to break up blood clots and asparaginase in cancer treatment. Finally, it notes analytical applications of enzymes in techniques like ELISA and uses in industries like food production and DNA analysis.
Carbohydrates are biomolecules composed of carbon, hydrogen, and oxygen. They are classified as monosaccharides, oligosaccharides, or polysaccharides depending on the number of monomer units present. Monosaccharides include simple sugars like glucose and fructose. Disaccharides are formed from two monosaccharides joined by a glycosidic bond, examples being sucrose and lactose. Polysaccharides are polymers of monosaccharides and include starch, glycogen, and cellulose. Carbohydrates serve important functions as energy sources, structural components of cells and organisms, and precursors for other biomolecules.
The document summarizes protein metabolism and the urea cycle. It discusses that 1-2% of body proteins are degraded and renewed daily. Ammonia produced is highly toxic, so the liver converts it to urea. Glutamine synthase fixes ammonia as non-toxic glutamine and glutaminase releases it for urea synthesis. The urea cycle uses ammonia, CO2, and aspartate to synthesize urea using 5 enzymes in the liver. Rare metabolic disorders can cause urea synthesis blockage, increasing blood ammonia and risking intoxication and brain damage. Treatments include low-protein diets and frequent small meals to avoid sudden ammonia increases.
Citric acid cycle (TCA cycle) by Dr. Anurag YadavDr Anurag Yadav
The citric acid cycle, also known as the Krebs cycle or TCA cycle, is the final common pathway for the oxidation of acetyl CoA derived from carbohydrates, fats, and proteins. The cycle consists of 8 steps that oxidize acetyl CoA completely to carbon dioxide, producing reduced coenzymes NADH and FADH2 that fuel the electron transport chain. The cycle takes place in the mitochondrial matrix and generates ATP through substrate-level phosphorylation. It also provides precursors for biosynthesis and integrates various metabolic pathways. Defects in enzymes of the citric acid cycle can cause various metabolic disorders.
The document provides an overview of enzymology and enzyme catalysis. It discusses:
1. The teaching objectives which are to introduce enzymes as catalysts, classify enzyme types and mechanisms, illustrate enzyme kinetics, highlight mechanisms of enzyme regulation and clinical importance.
2. Key characteristics of enzyme-catalyzed reactions including high specificity and regulation in response to changes.
3. Mechanisms by which enzymes catalyze reactions including proximity and orientation effects, transition state stabilization, and acid/base catalysis.
This document provides an overview of enzymes, including their chemistry, nomenclature, classification, mechanisms of action, and factors that affect enzyme activity. It discusses how enzymes are proteins that act as biological catalysts, lowering the activation energy of biochemical reactions. Enzymes are classified according to the type of chemical reactions they catalyze into six main classes: oxidoreductases, transferases, hydrolases, lyases, isomerases, and ligases. The document also covers enzyme kinetics, regulation, diagnostic and therapeutic uses of enzymes.
This document provides information on enzymes including their structure, function, classification, nomenclature and properties. Some key points:
- Enzymes are protein catalysts that increase the rate of reactions without being consumed in the process. They contain an active site that binds substrates.
- Enzymes are classified based on their catalytic activity into six major classes including oxidoreductases, transferases, hydrolases, lyases, isomerases and ligases.
- Enzyme activity can be regulated and influenced by factors like concentration, temperature, pH and inhibitors. Competitive and noncompetitive inhibition are described.
- Measurement of plasma enzyme levels is useful for clinical diagnosis as increased levels can indicate
The document discusses the classification of enzymes by the International Union of Biochemistry and Molecular Biology (IUBMB). Enzymes are grouped into six main classes based on their catalytic activity: oxidoreductases, transferases, hydrolases, lyases, isomerases, and ligases. Each class is further divided into subclasses based on the type of reaction catalyzed. Key features of enzyme active sites and factors that influence enzyme activity such as cofactors, pH, temperature, and substrate binding are also summarized.
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.
This document provides information on enzymes. It begins by defining enzymes as soluble, colloidal organic catalysts formed by living cells that are specific, protein in nature, and inactive at 0°C. It notes that all enzymes are proteins and that activity is lost through denaturation or dissociation. The document discusses enzymes as proteins that often require cofactors. It provides details on different types of enzymes based on their structure, location, and method of secretion. The rest of the document covers enzyme nomenclature, classification, specificity, and mechanisms of action. It discusses factors that affect enzyme activity such as temperature, pH, product concentration, and more.
This document provides information about enzymes, including their chemistry, structure, cofactors, mechanism of action, kinetics, and classification. It discusses that enzymes are proteins that act as biological catalysts, speeding up biochemical reactions. They have an active site that binds to substrates. Cofactors such as metal ions and organic molecules are required for some enzyme activities. The mechanism of action involves lowering the activation energy of reactions. Enzyme kinetics examines how factors like temperature, pH, and substrate concentration influence reaction rates. Enzymes are classified based on the type of reaction they catalyze.
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.
Enzymes are complex protein molecules called biocatalysts that accelerate chemical reactions without being consumed. They do this by lowering the activation energy of reactions. Each enzyme is highly specific and will only catalyze one type of reaction or convert one particular substrate. Enzymes work by binding to substrates in their active site and using mechanisms like lock-and-key or induced fit to facilitate the reaction. They are classified based on the type of reaction they catalyze and many require cofactors like vitamins and metals to function properly. External factors such as temperature, pH, substrate and inhibitor concentrations can impact an enzyme's activity level.
V.JAGAN MOHAN RAO is an Assistant Professor at NIPER-KOLKATA and MIPER-KURNOOL who provides information on enzyme chemistry. The document discusses enzyme structure, including active sites and cofactors. It also covers enzyme classification, mechanisms of action such as covalent catalysis and acid-base catalysis, kinetics including factors affecting reaction rates like temperature and pH, and inhibition and activation of enzymes.
D. Pharm BIOCHEMISTRY AND CLINICAL PATHOLOGY EnzymeArun Kumar
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.
Dr. Naresh Panigrahi discusses enzymes and biochemistry. Some key points:
- Enzymes are proteins that act as catalysts to speed up chemical reactions in cells without being used up in the process. They have high specificity for their substrate.
- Enzyme structure includes an apoenzyme protein portion and often a cofactor like a coenzyme, prosthetic group, or metal ion that is required for catalytic activity.
- Factors like pH, temperature, and inhibitors can impact enzyme activity by altering its structure-function relationship.
- Enzymes are classified based on the type of reaction they catalyze and have unique names and EC numbers in enzyme nomenclature systems
Enzymes are biological catalysts that accelerate chemical reactions without being consumed. They achieve this by lowering the activation energy of reactions. The document discusses the definition, mechanism of action, classification, and properties of enzymes. It also examines factors that affect enzyme activity such as temperature, pH, and inhibitors. Important clinical enzymes are mentioned for diagnosing conditions like heart attacks and liver disease. Key applications of enzymes include disease diagnosis, therapeutics, and use in laboratory reactions.
This document discusses enzymes and provides definitions, explanations of their mechanisms of action, and classifications. It describes how enzymes lower the activation energy of reactions, form enzyme-substrate complexes, and use induced fit and cofactors/coenzymes. Enzymes are classified based on the type of reaction they catalyze. Key properties include specificity, inhibition, and factors like temperature, pH, and inhibitors that influence enzyme activity. Important clinical enzymes are discussed.
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 are proteins that act as catalysts and speed up chemical reactions without being consumed. They are highly specific and function most effectively within a certain pH range and temperature. The active site of the enzyme binds to the substrate and the transition state requires lower activation energy than without the enzyme. The turnover number refers to the number of substrate molecules an enzyme can convert to products per unit time. Enzyme activity is affected by factors like substrate and inhibitor concentration, pH, temperature, and cofactors. Different types of inhibitors like competitive, non-competitive, and allosteric inhibitors can bind to enzymes and decrease their activity.
The document discusses microbial metabolism and various metabolic pathways and processes. It describes catabolic reactions that break down nutrients and anabolic reactions that synthesize cellular components. Central to metabolism are enzymes, which lower activation energy for reactions. Metabolic pathways generate ATP through oxidative phosphorylation or substrate-level phosphorylation. The main energy-generating pathways include glycolysis, the Krebs cycle, and the electron transport chain.
This document provides information about enzymes including their structure, function, and kinetics. It discusses that enzymes are proteins that act as biological catalysts by lowering the activation energy of biochemical reactions. The active site of an enzyme binds substrates and contains residues that facilitate the reaction. Cofactors like metals and organic molecules are also required for some enzyme reactions. The rate of enzyme-catalyzed reactions depends on factors like temperature, pH, and substrate concentration as described by the Michaelis-Menten kinetic model. The document also outlines different types of inhibition like competitive, non-competitive, and irreversible inhibition.
This document provides an overview of thyroid function and thyroid testing. It discusses the anatomy and physiology of the thyroid gland, including hormone biosynthesis and mechanisms of action. It also covers thyroid disorders such as hypothyroidism and hyperthyroidism. Finally, it reviews different thyroid tests including measurements of thyroid hormones, binding proteins, antibodies, and other related proteins. The goal is to understand the basic functions of the thyroid as well as how to interpret thyroid test results.
This document discusses the metabolism of xenobiotics, or foreign chemicals, in the body. It notes that xenobiotics are mostly lipophilic and cannot be easily cleared from the body. Their metabolism involves two phases - in the first phase enzymes like cytochrome P450 modify xenobiotics through reactions like hydroxylation and oxidation, while the second phase involves conjugating the substances to make them more water soluble and able to be excreted, through processes like glucuronidation and sulfation. Factors like genetic variability and drug interactions can impact an individual's ability to metabolize different xenobiotics. The document provides many examples of common xenobiotics and discusses how their metabolism can sometimes produce toxic effects.
The document discusses cancer and cancer care. The theme for World Cancer Day 2022 is "Close the care gap" which aims to raise awareness about differences in access to cancer prevention and treatment. Cancer rates have been increasing exponentially. While India's cancer burden is lower than other countries, it is estimated that 1 in 9 Indians will develop cancer in their lifetime. Common cancers in India vary by sex, with breast cancer being most common among women and lung cancer among men. Treatment options discussed include surgery, chemotherapy, radiotherapy, and genomic therapy.
This presentation is targeted for MBBS, MD and BDS students that describes briefly about aetiopathogenesis, tumour markers, anti cancer agents, apoptosis
RNA comes in several types that serve different functions. Messenger RNA (mRNA) acts as a template for protein synthesis by carrying genetic code from DNA to the ribosomes. Transfer RNA (tRNA) transfers amino acids to the ribosome during protein synthesis. Ribosomal RNA (rRNA) is a core component of ribosomes and catalyzes peptide bond formation. Other non-coding RNAs include microRNAs (miRNAs) that regulate gene expression at the post-transcriptional level, and small nuclear RNAs (snRNAs) that are involved in splicing mRNA transcripts. RNAs play essential roles in coding, decoding, regulating, and expressing genes.
RNA metabolism and transcription are complex processes involving multiple steps. There are three major types of RNA - mRNA, rRNA and tRNA. Transcription involves initiation, elongation and termination. It requires a DNA template, RNA polymerase enzyme, and nucleotide substrates. Prokaryotes have a single RNA polymerase while eukaryotes have three specialized RNA polymerases. Transcription results in primary transcripts that undergo extensive processing before becoming functional RNAs. Alternative splicing allows generation of multiple mRNAs from a single gene. Transcription and its regulation play an important role in gene expression.
This document discusses the organization and structure of DNA. It notes that DNA is highly compressed through winding around histone proteins to form nucleosomes. Histone chaperones assist in nucleosome formation. Nucleosomes are arranged differently in transcriptionally active versus inactive regions of DNA. Euchromatin, which is actively transcribed, replicates earlier than heterochromatin, which is transcriptionally silent. The document also discusses repetitive sequences in DNA, including transposable elements, microsatellites, and trinucleotide repeats linked to genetic diseases. Pseudogenes and gene rearrangements are mentioned as well.
The document summarizes key facts about DNA and its structure. It notes that it takes 8 hours for a cell to copy its DNA, which contains about 30 billion nucleotide base pairs on each strand. If total human DNA was laid end to end, it would stretch to the sun and back over 600 times. Our genes are highly similar to other organisms, with over 90% similarity to mice. DNA is made up of nucleotides containing phosphate groups, deoxyribose sugars, and nitrogenous bases of A, T, C, or G. The double helix structure of DNA involves base pairing and hydrogen bonding between strands in an antiparallel fashion.
Glycine is an aliphatic amino acid which gives rise to many vital derivatives. This is a non-essential amino acid. This presentation is targeted for MBBS, MD, BDS and general Biochemistry students.
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Cell Therapy Expansion and Challenges in Autoimmune DiseaseHealth Advances
There is increasing confidence that cell therapies will soon play a role in the treatment of autoimmune disorders, but the extent of this impact remains to be seen. Early readouts on autologous CAR-Ts in lupus are encouraging, but manufacturing and cost limitations are likely to restrict access to highly refractory patients. Allogeneic CAR-Ts have the potential to broaden access to earlier lines of treatment due to their inherent cost benefits, however they will need to demonstrate comparable or improved efficacy to established modalities.
In addition to infrastructure and capacity constraints, CAR-Ts face a very different risk-benefit dynamic in autoimmune compared to oncology, highlighting the need for tolerable therapies with low adverse event risk. CAR-NK and Treg-based therapies are also being developed in certain autoimmune disorders and may demonstrate favorable safety profiles. Several novel non-cell therapies such as bispecific antibodies, nanobodies, and RNAi drugs, may also offer future alternative competitive solutions with variable value propositions.
Widespread adoption of cell therapies will not only require strong efficacy and safety data, but also adapted pricing and access strategies. At oncology-based price points, CAR-Ts are unlikely to achieve broad market access in autoimmune disorders, with eligible patient populations that are potentially orders of magnitude greater than the number of currently addressable cancer patients. Developers have made strides towards reducing cell therapy COGS while improving manufacturing efficiency, but payors will inevitably restrict access until more sustainable pricing is achieved.
Despite these headwinds, industry leaders and investors remain confident that cell therapies are poised to address significant unmet need in patients suffering from autoimmune disorders. However, the extent of this impact on the treatment landscape remains to be seen, as the industry rapidly approaches an inflection point.
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Mercurius is named after the roman god mercurius, the god of trade and science. The planet mercurius is named after the same god. Mercurius is sometimes called hydrargyrum, means ‘watery silver’. Its shine and colour are very similar to silver, but mercury is a fluid at room temperatures. The name quick silver is a translation of hydrargyrum, where the word quick describes its tendency to scatter away in all directions.
The droplets have a tendency to conglomerate to one big mass, but on being shaken they fall apart into countless little droplets again. It is used to ignite explosives, like mercury fulminate, the explosive character is one of its general themes.
5-hydroxytryptamine or 5-HT or Serotonin is a neurotransmitter that serves a range of roles in the human body. It is sometimes referred to as the happy chemical since it promotes overall well-being and happiness.
It is mostly found in the brain, intestines, and blood platelets.
5-HT is utilised to transport messages between nerve cells, is known to be involved in smooth muscle contraction, and adds to overall well-being and pleasure, among other benefits. 5-HT regulates the body's sleep-wake cycles and internal clock by acting as a precursor to melatonin.
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2. What shall we learn?
Why should we learn about enzymes?
Why nursing staff should know about them?
Who thought about them first?- History
How do we define them?
How do we name them?- The classification
3.
4. Definition
Enzymes are “Biocatalysts”, synthesized by living
cells and highly specific in their action.
They are:
Mostly proteins (Exception- Ribozymes)
Heat labile
Soluble in water
Colloidal
Precipitated by precipitation reaction
Contain 16% weight as nitrogen
5. Classification & Nomenclature
A. Recommended name
B. Systematic name
IUBMB
Unambiguous & Informative
But Cumbersome
6 major classes
Class.Subclass.sub-subclass.substrate
6.
7. OTHLIL
Oxidoreductases→ Transfer of H, O or e-
Transferases → Transfer of gr other than H
Hydrolases → Cleave bond & add H2O
Lyases → Cleave bond without adding H2O
Isomerases → Intramolecular transfers
Ligases → ATP dependent condensation of 2 molecules
8. 1. Oxidoreductases
AH2 + B →A + BH2
Alcohol+ NAD+ ADH Aldehyde + NADH +H+
• Dehydrogenases (hydride transfer)- ADH
• Oxidases (electron transfer to molecular oxygen)- L-
and D- AA oxidase
• Oxygenases (oxygen transfer from molecular
oxygen)- oxygenase, mono- & di-oxygenases,
Cytochrome oxidase
• Peroxidases (electron transfer to peroxide)-
Glutathione peroxidase
9. 2. Transferases
A-R + B → A + B-R
• transfer of an atom or group of atoms
(e.g. acyl-, alkyl- and glycosyl- ), between
two molecules, but excluding such
transfers as are classified in the other
groups (e.g. Oxidoreductases and
Hydrolases).
• Ex- Aminotransferases, all kinases,
transmethylases
• Hexose + ATP Hexokinase Hexose-6-P +
ADP
10. 3. Hydrolases
Cleavage of ester, ether, peptide or
glycosidic bond by addition of H2O
Ach + H2O acetylcholine esterase Choline +
Acetate
Ex: All digestive enzymes, lipase, pepsin,
Trypsin, ALP, Urease
11. 4. Lyases
Cleave bond without addition of H2O
Fructose-1,6-BP Aldolase Glyceraldehyde-3-
P
+ Dihydroxyacetone P
Ex: Fumarase, Histidase, HMG CoA lyase
12. 5. Isomerases
Can produce optical, geometrical or
positional isomers of substrates
Gly-3-P Triose P isomerase DHAP
Ex: Racemase, Epimerase
13. 6. Ligases (synthetases)
ATP dependent condensation of two
molecules
Acetyl CoA + CO2 + ATP Acetyl CoA Carboxylase
Malonyl CoA + ADP + Pi
Synthases and synthetases are different
!!!
Synthatase- need ATP; Synthase- no ATP
Ex: Glycogen synthase, ALA synthase
14.
15.
16. Some Terminologies
Active Site
Region where substrate binds
Occupies a very small portion of the enzyme
Situated in a crevice or a cleft
During binding specific groups realign themselves to fit
exactly
Substrate binds by non-covalent bonds
AA or grs. That directly participate in binding are
known as catalytic residues
Sometimes catalytic site and substrate binding site may
be different
Coenzymes and cofactors are a part of the catalytic site
Serine- frequently present
21. Characteristics of coenzymes
I. When cofactor is some organic substance
II. Group is transferred from or accepted by the
coenzyme
III. Heat stable
IV. Low MW
V. Combine loosely with enzyme
VI. Separated by dialysis
VII. Reaction complete→ Coenzyme released →
Goes to other reaction site
22. Prosthetic group
• When cofactor (collectively includes coenzymes
and metal ions) is strongly bound to the
apoenzyme by covalent or non-covalent forces
• Ex: PLP, FMN, FAD, TPP, Biotin;
metal ions of Co, Cu, Mg, Mn, Se, and Zn
• Metals are most common
• 1/3rd enzymes contain metals- Metallozymes
/Metallo-enzymes
• Metals as cofactors- Metal activated enzymes
23. Metallo -enzymes
Metal Metal containing enzyme
Zn Carbonic anhydrase, Carboxypeptidase, ADH
Mg Hexokinase, PFK, Enolase, Glu-6-Phosphatase
Mn Phospho gluco mutase, Hexokinase, Enolase,
Glycosyl transferase
Cu Tyrosinase, cytochrome oxidase, SOD, Lysyl
oxidase
Fe cytochrome oxidase, catalase, peroxidase,
Xanthine oxidase
Ca Lecithinase, lipase
Se Glutathione peroxidase, Deiodinase
Mo Xanthine oxidase
25. How enzymes work???
Enzymes provide an alternate,
energetically favorable pathway different
from uncatalyzed reaction
The active site chemically facilitates
catalysis
26. A. Energy changes occurring during reaction
A ↔ T* ↔ B
Energy barrier separates reactants and products.
Energy barrier- Free energy of activation
↓
Energy difference between reactants and high energy
intermediate T*
27. a) Free energy of activation
Uncatalyzed reactions- high EA
Rate of reactions thus slow
32. Enzymes can be isolated and
properties can be studied in vitro
Factors affecting enzymes are:
1. Concentration of enzyme
2. Concentration of substrate
3. Concentration of product
4. Temperature
5. pH
6. Activators
7. Time
8. Light & radiation
9. Inhibitors
33. 1. Enzyme concentration
affecting enzyme activity
When substrate is sufficient,
Rate of reaction is proportional to
Enzyme concentration
Unit of enzyme activity- IU, Katal
(Kat), U, KAU
34.
35. 2. Substrate concentration
affecting enzyme activity
E + S ↔ ES ↔ E + P
A
B
C
3 Phases
A. At low substrate
conc.– V α [S]
B. [S] not directly
proportional to V
C. Reaction
independent of [S]
36. Most of the enzymes follow
Michelis-Menten kinetics
37. MICHELIS-MENTEN EQUATION
Enzyme combines reversibly with
substrate to form ES.
Breakdown of ES to product is
irreversible.
E= Enzyme
S= Substrate
P= Product
Es= Enz- substrate complex
K1, K-1, K2= Rate constants
39. Km/ Michelis constant
It’s the substrate concentration (expressed in
moles/lit) at half-maximal velocity.
50% of enzyme molecules are bound with
substrate molecules at that particular substrate
concentration
Km is independent of enzyme concentration
Expressed in moles/lit
Km is a constant for an enzyme. It’s the
characteristic feature of a particular enzyme for a
specific substrate- Signature of the enzyme
40. Km is the representative of measuring
the strength of the ES complex
Low Km – strong affinity between enzyme
and substrate
Ex: Glucokinase– Km= 10 mmol /lit
Hexokinase– Km= 0.05 mmol/lit
So what’s the inference??
41. 50% molecules of Hexokinase are
saturated even at a lower conc. Of
glucose.
When [S] << Km → reaction is first-
order
When [S] >> Km → reaction is zero-
order
44. 5. Effect of pH
pH change alters:
Ionization states of the amino acid residues
present in the active site
Ionization state of substrate
May dissociate apoenzyme from cofactor
Drastic change denatures the enzyme protein
Optimum pH is different for different enzymes
Mostly 6-8
Exception: Pepsin– 1-2
ALP– 9-10
Acid phosphatase – 4-5
52. Many different kinds of molecules inhibit
enzymes and act in a variety of ways
Enzyme inhibition
Competitive
Non-competitive
Reversible Irreversible
Uncompetitive
Suicide
Allosteric
Feedback
53. Competitive inhibition
• Inhibitor competes with the substrate for the active
site
• Inhibitor is substrate analogue
• Usually reversible
• ↑ [S] abolishes inhibition
• ↓ velocity of reaction
• ↑ Km
• Vmax unchanged
56. Non-competitive inhibition
• No competition between substrate and
inhibitor
• Different binding sites
• No structural similarities
• ↑ [S] doesn’t resolve the inhibition
• Usually irreversible
• May be reversible when inhibitor is
removed
• Km value unchanged
• Vmax reduces
57.
58. Clinical significance
• Cyanide inhibits cytochrome oxidase
• F inhibits enolase- removes Mn & Mg
• Heavy metals react with –SH gr. Of BAL-
hence BAL is used in heavy metal
poisoning
Toxicological importance
• Most of the poisons- Irreversible NC
inhibitors- iodoacetate, heavy metal
poisons
59. Competitive Vs Non-competitive inhibition
Competitive
inhibition
Non-competitive
inhibition
Act on Active site May/may not be
Str of inhibitor Substrate
analogue
Not an analogue
Reversibility Reversible Mostly irreversible
↑ Substrate Inhibition relieved No effect
Km ↑ No change
Vmax Unchanged ↓
Significance Drug action Toxicological
60.
61. How Isozymes help in Medicine??
Diagnosis
Prognosis
Treatment
Biochemical assays
62. LDH iso -enzymes
No. of
isozyme
Subunit
Make
up
Tissue of origin % in
human
serum
LDH-1 H4 Heart muscle 30
LDH-2 H3M1 RBC 35
LDH-3 H2M2 Brain 20
LDH-4 H1M3 Liver, Skeletal muscle 10
LDH-5 M4 Liver, Skeletal muscle 5
63. Clinical application of LDH
Myocardial infarction-LDH-1> LDH-2;
flipped pattern see in MI (usually LDH-2 >
LDH-1)
↑LDH-1, LDH-2- peaks at 72hrs and
stays till 1 week
Muscular dystrophies- ↑LDH-5
Hepatocellular damage- ↑LDH-5
Megaloblastic anemia, renal infarction-
↑LDH-1, LDH-2
Cancers- ↑↑↑
64. Creatine kinase
Normal serum level- 15-100 U/L for males;
10-80 U/L for females
Dimer, 2 units M &B
3 isoenzymes
MM (CK3)- Skeletal Mm.
MB (CK2)- Heart Mm.
BB (CK1)- Brain
65. Clinical application of
CK
Myocardial infarction
Muscular dystrophies
CK-MB peaks after AMI at 10-24 hrs, returns
to normal within 2-3 days