enzymes-
-definition,types and classification of enzymes.
-coenzymes,specificity of enzymes ,isoenzymes,enzyme kinetics including factors affecting velocity of enzymes catalysed reaction.enzyme inhibition
"Bacterial metabolism: Fueling life's processes in tiny powerhouses."
Use of bacterial metabolism in biotechnology, biofuels, and other industries
Examples of how bacterial metabolism is harnessed for beneficial purposes
"Metabolism: the sum of chemical reactions in an organism, supporting growth, energy production, and vital functions."
"Bacterial Metabolism and Life: Pervading every aspect of life, shaping ecosystems, and influencing our world."
Bacterial metabolism refers to the collective chemical reactions and processes that occur within bacterial cells, enabling them to maintain life, grow, and reproduce. These metabolic activities involve a complex network of biochemical pathways that facilitate the conversion of nutrients into energy, biomolecules, and essential compounds necessary for bacterial survival.
Metabolic processes in bacteria include catabolic pathways that break down complex molecules (such as sugars) to release energy and anabolic pathways that build complex molecules (such as proteins, nucleic acids) using energy. Bacteria utilize various metabolic strategies based on their energy and carbon sources, including aerobic and anaerobic respiration, fermentation, and photosynthesis in photosynthetic bacteria.
The primary goals of bacterial metabolism are to obtain energy, synthesize necessary cellular components, regulate chemical processes, and adapt to changing environmental conditions. The understanding of bacterial metabolism is crucial for various fields, including medicine, agriculture, biotechnology, and environmental science, as it allows us to develop strategies to combat harmful bacteria, harness their metabolic capabilities for beneficial applications, and study their role in ecological systems.
Enzymes are biological catalysts that are essential for life. They catalyze biochemical reactions efficiently and selectively. Enzymes lower the activation energy of reactions, increasing their rate. Most enzymes are proteins that use their tertiary structure and amino acid residues within their active site to catalyze reactions. The active site facilitates reactions by bringing substrates close together, stabilizing transition states, and using mechanisms like acid-base catalysis. This allows reactions to proceed rapidly under mild biological conditions. Without enzymes, reactions in living organisms would not occur at a useful pace to sustain life.
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.
The document discusses enzymes and how they catalyze biochemical reactions in living cells. It provides information on what enzymes are made of, how they work, and factors that affect their activity. Enzymes are proteins that function as biological catalysts and have an active site where reactions occur. They speed up reactions by lowering activation energy. The rate of enzyme-catalyzed reactions depends on factors like substrate concentration, temperature, pH, and surface area, with each enzyme having an optimum level. The shape and bonds of an enzyme determine its specific function. Enzymes are important for processes like digestion, respiration, photosynthesis, and more. They are also used in industries like food and detergents. Experiments can investigate how temperature,
The document discusses various aspects of metabolism, including the two main types of metabolic processes (catabolism and anabolism), how organisms obtain energy through the breakdown of nutrients like carbohydrates and proteins, and factors that can increase metabolic rate such as caffeine, fiber, and organic foods. It also covers topics like microbial metabolism, nitrogen fixation by microbes, aerobic and anaerobic respiration, and the role of metabolism in sustaining life.
This document provides an overview of enzymes and their properties. It discusses:
- The history of enzyme discovery and early debates about fermentation
- That enzymes are proteins that catalyze metabolic reactions in cells
- Key properties of enzymes including that they are catalysts, require small amounts, and are not consumed in reactions
- The importance of enzymes in cellular processes and their medical applications such as diagnosing disease
- How enzymes accelerate reactions by reducing activation energy without changing reaction thermodynamics or products
- General properties of enzymes like substrate specificity, effect of temperature and pH on activity, and being proteinaceous
This document discusses enzymes and their properties. It begins by explaining that enzymes are biological catalysts that are usually proteins and that speed up biochemical reactions. It describes enzyme structure, including the active site where substrates bind. It discusses cofactors that enzymes require to function properly. The document then explains enzyme kinetics concepts like Michaelis-Menten kinetics and how temperature, pH, and substrate concentration affect reaction rates. Finally, it covers inhibition, where inhibitors bind enzymes and decrease their activity, and activation, where enzymes are converted to more active forms.
1. Living organisms are composed of biomolecules like nucleic acids, proteins, carbohydrates and lipids made from carbon, hydrogen, oxygen and nitrogen.
2. Within cells, these biomolecules and inorganic elements confer the property of life and allow the cell to obtain materials, produce enzymes, and undergo chemical reactions to sustain itself.
3. Biochemistry studies the biomolecules, elements, and chemical reactions within living things to understand functions at the molecular level, from single-celled to multicellular organisms.
"Bacterial metabolism: Fueling life's processes in tiny powerhouses."
Use of bacterial metabolism in biotechnology, biofuels, and other industries
Examples of how bacterial metabolism is harnessed for beneficial purposes
"Metabolism: the sum of chemical reactions in an organism, supporting growth, energy production, and vital functions."
"Bacterial Metabolism and Life: Pervading every aspect of life, shaping ecosystems, and influencing our world."
Bacterial metabolism refers to the collective chemical reactions and processes that occur within bacterial cells, enabling them to maintain life, grow, and reproduce. These metabolic activities involve a complex network of biochemical pathways that facilitate the conversion of nutrients into energy, biomolecules, and essential compounds necessary for bacterial survival.
Metabolic processes in bacteria include catabolic pathways that break down complex molecules (such as sugars) to release energy and anabolic pathways that build complex molecules (such as proteins, nucleic acids) using energy. Bacteria utilize various metabolic strategies based on their energy and carbon sources, including aerobic and anaerobic respiration, fermentation, and photosynthesis in photosynthetic bacteria.
The primary goals of bacterial metabolism are to obtain energy, synthesize necessary cellular components, regulate chemical processes, and adapt to changing environmental conditions. The understanding of bacterial metabolism is crucial for various fields, including medicine, agriculture, biotechnology, and environmental science, as it allows us to develop strategies to combat harmful bacteria, harness their metabolic capabilities for beneficial applications, and study their role in ecological systems.
Enzymes are biological catalysts that are essential for life. They catalyze biochemical reactions efficiently and selectively. Enzymes lower the activation energy of reactions, increasing their rate. Most enzymes are proteins that use their tertiary structure and amino acid residues within their active site to catalyze reactions. The active site facilitates reactions by bringing substrates close together, stabilizing transition states, and using mechanisms like acid-base catalysis. This allows reactions to proceed rapidly under mild biological conditions. Without enzymes, reactions in living organisms would not occur at a useful pace to sustain life.
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.
The document discusses enzymes and how they catalyze biochemical reactions in living cells. It provides information on what enzymes are made of, how they work, and factors that affect their activity. Enzymes are proteins that function as biological catalysts and have an active site where reactions occur. They speed up reactions by lowering activation energy. The rate of enzyme-catalyzed reactions depends on factors like substrate concentration, temperature, pH, and surface area, with each enzyme having an optimum level. The shape and bonds of an enzyme determine its specific function. Enzymes are important for processes like digestion, respiration, photosynthesis, and more. They are also used in industries like food and detergents. Experiments can investigate how temperature,
The document discusses various aspects of metabolism, including the two main types of metabolic processes (catabolism and anabolism), how organisms obtain energy through the breakdown of nutrients like carbohydrates and proteins, and factors that can increase metabolic rate such as caffeine, fiber, and organic foods. It also covers topics like microbial metabolism, nitrogen fixation by microbes, aerobic and anaerobic respiration, and the role of metabolism in sustaining life.
This document provides an overview of enzymes and their properties. It discusses:
- The history of enzyme discovery and early debates about fermentation
- That enzymes are proteins that catalyze metabolic reactions in cells
- Key properties of enzymes including that they are catalysts, require small amounts, and are not consumed in reactions
- The importance of enzymes in cellular processes and their medical applications such as diagnosing disease
- How enzymes accelerate reactions by reducing activation energy without changing reaction thermodynamics or products
- General properties of enzymes like substrate specificity, effect of temperature and pH on activity, and being proteinaceous
This document discusses enzymes and their properties. It begins by explaining that enzymes are biological catalysts that are usually proteins and that speed up biochemical reactions. It describes enzyme structure, including the active site where substrates bind. It discusses cofactors that enzymes require to function properly. The document then explains enzyme kinetics concepts like Michaelis-Menten kinetics and how temperature, pH, and substrate concentration affect reaction rates. Finally, it covers inhibition, where inhibitors bind enzymes and decrease their activity, and activation, where enzymes are converted to more active forms.
1. Living organisms are composed of biomolecules like nucleic acids, proteins, carbohydrates and lipids made from carbon, hydrogen, oxygen and nitrogen.
2. Within cells, these biomolecules and inorganic elements confer the property of life and allow the cell to obtain materials, produce enzymes, and undergo chemical reactions to sustain itself.
3. Biochemistry studies the biomolecules, elements, and chemical reactions within living things to understand functions at the molecular level, from single-celled to multicellular organisms.
This document provides an overview of enzymology for biochemistry students. It discusses the key components and characteristics of enzymes, including their chemical nature, cofactors, and metal ions. Various classes of enzymes are described based on their general functions. Important concepts like enzyme specificity, turnover number, and the roles of coenzymes and cofactors are summarized. The document also covers enzyme nomenclature, classification, and some of the advantages and drawbacks of using enzymes as catalysts. Overall, the document serves as an introductory lesson on the fundamentals of enzymology.
Enzyme structure and Mechanism of Action Swati Raysing
This document discusses enzyme structure and mechanism of action. It defines enzymes as specialized proteins that catalyze biochemical reactions by lowering activation energy. Enzymes play important roles in metabolism, diagnosis, and therapeutics. The active site of an enzyme is where substrate binds. Enzymes use cofactors like coenzymes and prosthetic groups to function. Reaction rates depend on factors like substrate/enzyme concentration, temperature, pH, and presence of activators. Enzymes work via lock-and-key or induced fit models to form enzyme-substrate complexes and reduce activation energy of reactions.
Biochemical engineering uses microorganisms and biological materials to develop products and processes for industries like biotechnology, biofuels, pharmaceuticals, water purification, and food. Biochemical engineers use their knowledge of engineering, biology, and chemistry to create new products and manufacturing processes from biological materials. They work with other professionals to test interactions between materials in a lab and then develop large-scale manufacturing processes. Microorganisms are tiny organisms that can only be seen with a microscope. They are used industrially to produce foods, beverages, biofuels, chemicals, enzymes, antibiotics, and vitamins. Different fermentation methods like batch, fed-batch, and continuous fermentation are used to produce products using microorganisms on
This document provides an overview of biochemistry and metabolism presented by Dr. Kirpa Ram. It begins with defining biochemistry as the study of life at the cellular and molecular levels and explores the major disciplines related to biochemistry such as molecular genetics, pharmacology, and molecular biology. Several sections discuss the importance of biochemistry in fields like medicine, nursing, agriculture, nutrition, pharmacy, and plants. Key concepts in biochemistry like atomic structure, molecules, and different classes of organic compounds like carbohydrates and lipids are also introduced.
Enzymes are proteins that act as biological catalysts, regulating the rate of chemical reactions in living organisms. They accelerate reactions by lowering the activation energy without being consumed in the process. Enzymes are highly specific and each enzyme catalyzes only one type of reaction. They are affected by factors like temperature, pH, and substrate concentration. The active site of the enzyme binds specifically to substrates and catalyzes the conversion of substrates to products. Enzymes play essential roles in processes like digestion, cellular metabolism, and protection against pathogens.
.Enzymes are proteins that catalyze or speed up chemical reactions. They also help digest the foods we eat food and heal our wounds. They play major roles in respiration, making proteins, and DNA replication..
This document discusses enzymes and enzyme kinetics. It defines enzymes as biological catalysts that accelerate biochemical reactions. Enzymes have three main properties - catalytic power, specificity, and regulation. The document describes enzyme classification systems, cofactors, factors that affect enzyme activity like temperature and pH, enzyme inhibition, and models of enzyme action including lock-and-key and induced fit. It also discusses enzyme kinetics concepts such as Michaelis-Menten kinetics, activation energy, and Gibbs free energy.
This document discusses enzymes and provides information on their chemistry, classification, mechanism of action, kinetics, inhibition, activation and specificity. It defines enzymes as biological catalysts that speed up biochemical reactions. Most enzymes are globular proteins that contain an active site for substrate binding. The document outlines different types of enzyme kinetics including effects of temperature, pH, and substrate concentration. It also describes different types of inhibition like competitive, non-competitive and irreversible inhibition. Activation of enzymes by cofactors is also summarized.
Enzymes are biological catalysts that accelerate biochemical reactions in living organisms. They are typically proteins that catalyze specific reactions without being consumed in the process. This document provides an overview of enzymes, including their structure, classification, examples, mechanism of action, interactions with substrates, and functions in the body. Key points are that enzymes are proteins that help regulate metabolic processes and reactions through binding with substrate molecules at active sites to lower activation energy. They are classified based on the type of reaction catalyzed and include oxidoreductases, transferases, hydrolases, lyases, isomerases, and ligases. Enzymes play critical roles in cellular processes and metabolism.
This document discusses biocatalysts and enzymes. It begins by listing five properties of useful industrial microbes, such as producing spores or being amenable to genetic manipulation. It then defines biocatalysts as enzymes or microbes that accelerate chemical reactions. Enzymes function as biocatalysts by lowering the activation energy of reactions. The document outlines the structure and function of enzymes, including their active sites, and compares enzymes to non-biological catalysts. It also discusses producing biocatalysts through fermentation and engineering enzymes to modify their properties.
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.
The document defines key terms related to enzymes including substrate, active site, and cofactors. It describes the lock and key and induced fit models of how enzymes bind to substrates. Environmental factors like temperature, pH, and substrate concentration can affect the rate of enzymatic reactions. Cofactors and coenzymes are required for some enzymatic reactions. Competitive and noncompetitive inhibitors can regulate enzyme activity. Examples are given of enzymatic uses in industry, detergents, food, and diagnosing/treating diseases.
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.
INTRODUCTORY BIOCHEMISTRY NOTES
Simplified biochemistry for easy understanding. Meant all Biochemistry students. A special dedication to all FST 2019/2020
Enzymes are protein catalysts that speed up biochemical reactions without being consumed. They are produced by living organisms and work by lowering the activation energy of reactions. Enzymes are used as biocatalysts in industries like food processing and are essential for human digestion and DNA replication. Environmental factors like temperature and pH can impact enzyme activity, as can cofactors and inhibitors. Biocatalysts offer advantages over chemical catalysts like milder reaction conditions and higher product quality. They have many applications including food processing, diagnostics, and molecular biology.
Enzymes /certified fixed orthodontic courses by Indian dental academy Indian dental academy
The Indian Dental Academy is the Leader in continuing dental education , training dentists in all aspects of dentistry and offering a wide range of dental certified courses in different formats.
Indian dental academy provides dental crown & Bridge,rotary endodontics,fixed orthodontics,
Dental implants courses.for details pls visit www.indiandentalacademy.com ,or call
0091-9248678078
The document provides an overview of key topics in microbial physiology and genetics covered in Chapter 7, including:
- Microbial metabolism, including catabolic and anabolic reactions, and how ATP is used to store and transport energy.
- Aerobic respiration and fermentation pathways for breaking down glucose.
- Mutations and how bacteria can acquire new genetic material through transduction, transformation, conjugation and lysogenic conversion.
- Genetic engineering and how bacteria are used to produce compounds like insulin.
This chapter introduces the key concepts of biochemistry including: 1) the defining features of living organisms as highly organized systems that intake and transform energy, 2) the structure and organelles of cells including differences between prokaryotic and eukaryotic cells, and 3) the roles of biomolecules, pathways, and catalysis in metabolic reactions and energy transformations that are regulated and allow organisms to evolve over time.
This chapter introduces the key concepts of biochemistry by discussing (1) the defining features of living organisms, including their complexity, use of energy, and ability to self-replicate, (2) the structure and function of cells and their components, and (3) how the three-dimensional structure of biomolecules allows them to perform specific functions and drive metabolic pathways and evolution.
Enzymes are biological catalysts that speed up biochemical reactions without being consumed. They achieve high catalytic efficiency by lowering the activation energy of reactions. Enzymes are usually highly specific and function by binding substrates and facilitating the formation of enzyme-substrate complexes. Many enzymes require non-protein cofactors like metal ions, coenzymes, or prosthetic groups to function. Reaction rates carried out by enzymes can be affected by factors like substrate concentration, temperature, pH, and inhibitors. Enzymes play essential roles in cellular metabolism and are regulated through various mechanisms to control metabolic pathways.
More Related Content
Similar to unit-4 enzymes by poonam9 Pgdiploma.pptx
This document provides an overview of enzymology for biochemistry students. It discusses the key components and characteristics of enzymes, including their chemical nature, cofactors, and metal ions. Various classes of enzymes are described based on their general functions. Important concepts like enzyme specificity, turnover number, and the roles of coenzymes and cofactors are summarized. The document also covers enzyme nomenclature, classification, and some of the advantages and drawbacks of using enzymes as catalysts. Overall, the document serves as an introductory lesson on the fundamentals of enzymology.
Enzyme structure and Mechanism of Action Swati Raysing
This document discusses enzyme structure and mechanism of action. It defines enzymes as specialized proteins that catalyze biochemical reactions by lowering activation energy. Enzymes play important roles in metabolism, diagnosis, and therapeutics. The active site of an enzyme is where substrate binds. Enzymes use cofactors like coenzymes and prosthetic groups to function. Reaction rates depend on factors like substrate/enzyme concentration, temperature, pH, and presence of activators. Enzymes work via lock-and-key or induced fit models to form enzyme-substrate complexes and reduce activation energy of reactions.
Biochemical engineering uses microorganisms and biological materials to develop products and processes for industries like biotechnology, biofuels, pharmaceuticals, water purification, and food. Biochemical engineers use their knowledge of engineering, biology, and chemistry to create new products and manufacturing processes from biological materials. They work with other professionals to test interactions between materials in a lab and then develop large-scale manufacturing processes. Microorganisms are tiny organisms that can only be seen with a microscope. They are used industrially to produce foods, beverages, biofuels, chemicals, enzymes, antibiotics, and vitamins. Different fermentation methods like batch, fed-batch, and continuous fermentation are used to produce products using microorganisms on
This document provides an overview of biochemistry and metabolism presented by Dr. Kirpa Ram. It begins with defining biochemistry as the study of life at the cellular and molecular levels and explores the major disciplines related to biochemistry such as molecular genetics, pharmacology, and molecular biology. Several sections discuss the importance of biochemistry in fields like medicine, nursing, agriculture, nutrition, pharmacy, and plants. Key concepts in biochemistry like atomic structure, molecules, and different classes of organic compounds like carbohydrates and lipids are also introduced.
Enzymes are proteins that act as biological catalysts, regulating the rate of chemical reactions in living organisms. They accelerate reactions by lowering the activation energy without being consumed in the process. Enzymes are highly specific and each enzyme catalyzes only one type of reaction. They are affected by factors like temperature, pH, and substrate concentration. The active site of the enzyme binds specifically to substrates and catalyzes the conversion of substrates to products. Enzymes play essential roles in processes like digestion, cellular metabolism, and protection against pathogens.
.Enzymes are proteins that catalyze or speed up chemical reactions. They also help digest the foods we eat food and heal our wounds. They play major roles in respiration, making proteins, and DNA replication..
This document discusses enzymes and enzyme kinetics. It defines enzymes as biological catalysts that accelerate biochemical reactions. Enzymes have three main properties - catalytic power, specificity, and regulation. The document describes enzyme classification systems, cofactors, factors that affect enzyme activity like temperature and pH, enzyme inhibition, and models of enzyme action including lock-and-key and induced fit. It also discusses enzyme kinetics concepts such as Michaelis-Menten kinetics, activation energy, and Gibbs free energy.
This document discusses enzymes and provides information on their chemistry, classification, mechanism of action, kinetics, inhibition, activation and specificity. It defines enzymes as biological catalysts that speed up biochemical reactions. Most enzymes are globular proteins that contain an active site for substrate binding. The document outlines different types of enzyme kinetics including effects of temperature, pH, and substrate concentration. It also describes different types of inhibition like competitive, non-competitive and irreversible inhibition. Activation of enzymes by cofactors is also summarized.
Enzymes are biological catalysts that accelerate biochemical reactions in living organisms. They are typically proteins that catalyze specific reactions without being consumed in the process. This document provides an overview of enzymes, including their structure, classification, examples, mechanism of action, interactions with substrates, and functions in the body. Key points are that enzymes are proteins that help regulate metabolic processes and reactions through binding with substrate molecules at active sites to lower activation energy. They are classified based on the type of reaction catalyzed and include oxidoreductases, transferases, hydrolases, lyases, isomerases, and ligases. Enzymes play critical roles in cellular processes and metabolism.
This document discusses biocatalysts and enzymes. It begins by listing five properties of useful industrial microbes, such as producing spores or being amenable to genetic manipulation. It then defines biocatalysts as enzymes or microbes that accelerate chemical reactions. Enzymes function as biocatalysts by lowering the activation energy of reactions. The document outlines the structure and function of enzymes, including their active sites, and compares enzymes to non-biological catalysts. It also discusses producing biocatalysts through fermentation and engineering enzymes to modify their properties.
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.
The document defines key terms related to enzymes including substrate, active site, and cofactors. It describes the lock and key and induced fit models of how enzymes bind to substrates. Environmental factors like temperature, pH, and substrate concentration can affect the rate of enzymatic reactions. Cofactors and coenzymes are required for some enzymatic reactions. Competitive and noncompetitive inhibitors can regulate enzyme activity. Examples are given of enzymatic uses in industry, detergents, food, and diagnosing/treating diseases.
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.
INTRODUCTORY BIOCHEMISTRY NOTES
Simplified biochemistry for easy understanding. Meant all Biochemistry students. A special dedication to all FST 2019/2020
Enzymes are protein catalysts that speed up biochemical reactions without being consumed. They are produced by living organisms and work by lowering the activation energy of reactions. Enzymes are used as biocatalysts in industries like food processing and are essential for human digestion and DNA replication. Environmental factors like temperature and pH can impact enzyme activity, as can cofactors and inhibitors. Biocatalysts offer advantages over chemical catalysts like milder reaction conditions and higher product quality. They have many applications including food processing, diagnostics, and molecular biology.
Enzymes /certified fixed orthodontic courses by Indian dental academy Indian dental academy
The Indian Dental Academy is the Leader in continuing dental education , training dentists in all aspects of dentistry and offering a wide range of dental certified courses in different formats.
Indian dental academy provides dental crown & Bridge,rotary endodontics,fixed orthodontics,
Dental implants courses.for details pls visit www.indiandentalacademy.com ,or call
0091-9248678078
The document provides an overview of key topics in microbial physiology and genetics covered in Chapter 7, including:
- Microbial metabolism, including catabolic and anabolic reactions, and how ATP is used to store and transport energy.
- Aerobic respiration and fermentation pathways for breaking down glucose.
- Mutations and how bacteria can acquire new genetic material through transduction, transformation, conjugation and lysogenic conversion.
- Genetic engineering and how bacteria are used to produce compounds like insulin.
This chapter introduces the key concepts of biochemistry including: 1) the defining features of living organisms as highly organized systems that intake and transform energy, 2) the structure and organelles of cells including differences between prokaryotic and eukaryotic cells, and 3) the roles of biomolecules, pathways, and catalysis in metabolic reactions and energy transformations that are regulated and allow organisms to evolve over time.
This chapter introduces the key concepts of biochemistry by discussing (1) the defining features of living organisms, including their complexity, use of energy, and ability to self-replicate, (2) the structure and function of cells and their components, and (3) how the three-dimensional structure of biomolecules allows them to perform specific functions and drive metabolic pathways and evolution.
Enzymes are biological catalysts that speed up biochemical reactions without being consumed. They achieve high catalytic efficiency by lowering the activation energy of reactions. Enzymes are usually highly specific and function by binding substrates and facilitating the formation of enzyme-substrate complexes. Many enzymes require non-protein cofactors like metal ions, coenzymes, or prosthetic groups to function. Reaction rates carried out by enzymes can be affected by factors like substrate concentration, temperature, pH, and inhibitors. Enzymes play essential roles in cellular metabolism and are regulated through various mechanisms to control metabolic pathways.
Similar to unit-4 enzymes by poonam9 Pgdiploma.pptx (20)
2. TOPICS TO BE
DISCUSSED
What is biochemistry?
Objectives,scope and importance of biochemistry and
its relation to
nutrition
ENZYMES-
Definition,types and classification
Coenzymes,specificity of enzymes,isoenzymes,enzyme
kinetics including factors affecting velocity of enzymes
catalysed reaction.Enzyme inhibition
NUCLEIC ACIDS-
Classification,composition and function of nucleic acids
Structure and properties of nucleosides,nucleotides
Genetic code.
3. BIOCHEMISTRY
“Biochemistry has become the foundation for
understanding all biological processes. It has
provided explanations for the causes of many
diseases in humans, animals and plants.”
“Biochemistry is a study of the chemical
substances & processes that occur in plants,
animals & microorganisms & of the changes
they undergo during development & life.”
4. Biochemistry is both life science and a chemical science
- it explores the chemistry of living organisms and the
molecular basis for the changes occurring in living cells.
It uses the methods of chemistry, physics, molecular
biology, and immunology to study the structure and
behavior of the complex molecules found in biological
material and the ways these molecules interact to form
cells, tissues, and whole organisms
5. OBJECTIVES OF
BIOCHEMISTRY
Study the structures and functions of biomolecules like
carbohydrate, lipids, proteins minerals and DNA.
Focuses on techniques used to control diseases, abnormal
deficiency and treatment of deficiencies.
Understand the dynamic changes of cellular systems and
corresponding need of nutrients.
They act as catalyst agent.
Metabolic abnormalities can be studied by knowledge of
biochemistry.
Study of the energy transformations in living cells,
organisms is another objective of study of biochemistry.
6. IMPORTANCE OF
BIOCHEMISTRY
Biochemistry is thriving right now. In recent years it has
become the most critical area of science.
It combines the core of biology and chemistry, which
opens a new door for research from the very ground up.
Biochemistry helps us understand the medical
conditions such as diabetes, jaundice, rickets, etc. with
its research, and scientists are now able to find a
medication that can cure them or put them in control.
Biochemistry can help us find a way to decompose our
waste without harming nature successfully.
This field can also do wonders in the coming years and
make us live on other planets as we study the chemical
changes that happen on other planets such as mars.
7. SCOPES OF BIOCHEMISTRY
Biochemistry play an important role in various
fields such as; in clinical medicine,
pharmacology, biotechnology, agriculture,
horticulture, forestry, nursing, pathology, in
physiology, and also in microbiology.
BIOCHEMISTRY IN MEDICINE
• Physiology
• Pathology
• Nursing and diagnosis
9. SCOPE OF
BIOCHEMISTRY
BIOCHEMISTRY IN NUTRITION
• Food chemistry gives an idea of what we eat. The
nutrients value of food material can also be determined
by biochemical tests.
• Nutritional biochemical therapy saves lives, reduces
morbidity, improves health outcomes, and reduces
healthcare costs and patients.
11. OTHER SCOPES
• Biotechnologist
• Research Scientist
• Clinical Scientist
• Research Associates
• Chemist Microbiologist
• Biomedical Scientist
• Pharmacologist Laboratory Technician
• Lecturer in an Educational institution
12. RELATIONSHIP WITH
NUTRITION
Nutrition is the study of nutrients in food, how the body uses
them, and the relationship between diet, health, and disease.
Nutritional biochemistry deals with various studies in
nutrients, food constituents and their function regarding
humans and other mammals, nutritional biochemistry
specifically focuses on nutrient chemical components, and
how they function biochemically, physiologically,
metabolically, as well as their impact on disease.
13.
14. Definition
“Enzymes can be defined as biological polymers that
catalyze biochemical reactions.”
• Enzymes are nitrogenous organic molecules
produced by living organisms such as plants and
animals. A long chain of one or more amino acids
is connected together using amide or peptide
bonds to make them.
• Enzymes have a specific method of action (Lock-
and-Key mechanism and Enzyme Fit Hypothesis).
15. STRUCTURE OF ENZYMES
• Enzymes are proteins that are made up of
several polypeptide chains, also known as
amino acids, that have been folded and coiled
numerous times.
• They have linear chains of amino acids in
three-dimensional structures.
• The enzyme’s catalytic activity is determined
by the amino acid sequence. Only a small
portion of an enzyme’s structure participates in
catalysis and is located around the binding
sites.
• They have separate sites; the active site of an
enzyme is made up of the catalytic and binding
sites.
17. 1. Oxidoreductases
Catalyze oxidation/reduction reactions
Oxidation is the loss of electronsor an
increase in the oxidation state of an atom,
an ion, or of certain atoms in a molecule.
Reduction is the gain of electrons or a
decrease in the oxidation state of an atom,
an ion, or of certain atoms in a molecule.
Eg. Alcohol dehydrogenase
Cytochrome oxidase
Amino acid oxidases
18. 2. Transferases
• Involved in transfer of functional groups between molecules
Eg. :-
➢Hexokinase
➢Transaminases
➢Phosphorylase
3. Hydrolases
• Break bonds by adding H2O
Eg:-
Lipase (triacylglycerol acyl hydrolase)
Choline esterase
Acid and alkaline phosphatase
Pepsin
Urease
20. 6. Ligases
• Join molecules with new bonds Eg:-
Glutamine synthetase
Succinate thiokinase
Acetyl CoA carboxylase
21. Examples of Enzymes
Beverages
• Alcoholic beverages generated by fermentation vary a lot
based on many factors. Based on the type of the plant’s
product, which is to be used and the type of enzyme
applied, the fermented product varies.
• For example, grapes, honey, hops, wheat, cassava roots,
and potatoes depending upon the materials available.
Beer, wines and other drinks are produced from plant
fermentation.
Food Products
• Bread can be considered as the finest example of
fermentation in our everyday life.
• A small proportion of yeast and sugar is mixed with the
batter for making bread. Then one can observe that the
bread gets puffed up as a result of fermentation of the
sugar by the enzyme action in yeast, which leads to the
formation of carbon dioxide gas. This process gives the
texture to the bread, which would be missing in the
absence of the fermentation process.
22. Drug Action
Enzyme action can be inhibited or promoted by
the use of drugs which tend to work around the
active sites of enzymes.
Mechanism of Enzyme Reaction
Enzymes are said to possess an active site. The
active site is a part of the molecule that has a
definite shape and the functional group for the
binding of reactant molecules. The molecule that
binds to the enzyme is referred to as the substrate
group. The substrate and the enzyme form an
intermediate reaction with low activation energy
without any catalysts.
24. Action and Nature of Enzymes
• The enzyme action basically happens in two
steps:
• Step1: Combining of enzyme and the
reactant/substrate.
• E+S → [ES]
• Step 2: Disintegration of the complex
molecule to give the product.
• [ES]→E+P
• Thus, the whole catalyst action of enzymes
is summarized as:
• E + S → [ES] → [EP] → E + P
26. Factors Affecting Enzyme Activity
• The conditions of the reaction have a great impact
on the activity of the enzymes. Enzymes are
particular about the optimum conditions provided
for the reactions such as temperature, pH,
alteration in substrate concentration, etc.
27. Active site
Enzymatic catalysis depends upon the activity of
amino acid side chains assembled in the active
centre. Enzymes bind the substrate into a region of
the active site in an intermediate conformation.
Temperature and pH
Enzymes require an optimum temperature and pH
for their action. The temperature or pH at which a
compound shows its maximum activity is called
optimum temperature or optimum pH,
respectively. As mentioned earlier, enzymes
are protein compounds. A temperature or pH more
than optimum may alter the molecular structure
of the enzymes. Generally, an optimum pH for
enzymes is considered to be ranging between 5
and 7.
28. • Optimum T°
• The greatest number of molecular collisions
• human enzymes = 35°- 40°C
• body temp = 37°C
• Heat: increase beyond optimum T°
• The increased energy level of molecule disrupts bonds in
enzyme & between enzyme & substrate H, ionic = weak
bonds
• Denaturation = lose 3D shape (3° structure)
• Cold: decrease T°
• Molecules move slower decrease collisions between
enzyme & substrate
30. ENZYME INHIBITION
Enzyme inhibitor is defined as a substance which
binds with the enzyme and brings about a
decrease in catalyrtc activity of that enzyme. The
inhibitor may be organic or inorganic in nature.
There are three broad categories of enzyme
inhibition
• 1 . Reversible inhibition.
• 2. Irreversible inhibition.
• 3. Allosteric inhibition.
31. 1. Reversible inhibition
The inhibiior binds non-covalently with enzyme and
the enzyme inhibition can be reversed if the
inhibitor is removed. The reversible inhibition is
further sub-divided into
l. Competitive inhibition
ll. Non-competitive inhibition
34. 2. lrreversible inhibition
Inhibitor binds covalently(strong)with the enzyme
irreversibly
Soit can’t dissociate from the enzyme
Inhibitor cause conformation change at active site
of the E –destroying their capacity to function as
catalysts
Enzyme activity is not regained on dialysis/by
increasing the conc.of S
A variety of poisons,such as iodoacetate,OP
poisoning and oxidizing agents act as irreversible
inhibition
35. In terms of kinetics –irreversible is similor to non
competitive inhibition Vmax– Decreased
Km– No change
36. Suicide Inhibition
Specialized form of irreversible inhibition
Also known as mechanism based inactivation
I makes use of all enzyme’s own reaction
mechanism to inactivate it
Inhibitor(structural analog) is converted to a more
effective inhibitor with the help of the E to be
inhibited
E literally commits suicide-they utilize normal E
mechanism to inactivate the E.
37. 3. Allosteric inhibition
Some E possess additional site other than the
active siete called as Allosteric sites,E –AllostericE.
They are unique site on protein molecule
Allosteric effectors–substances bind of Allosteric
site & regulate E activity
Positive Allosteric effectors-E activity is increased
Negative Allostric effectors-E activity is decreased
Allostric enzyme-sigmoidal curve
38. ENZYME SPECIFICITY
Enzymes are highly specific in their action when
compared with the chemical catalysts. The
occurrence of thousands of enzymes in the
biological system might be due to the specific
nature of enzymes.
39. COENZYME
The non-protein, organic, Iow molecular weight
and dialysable substance associated with enzyme
function is known as coenzyme.
The functional enzyme is referred to as
holoenzyme which is made up of a protein part
(apoenzyme) and a non-protein part (coenzyme).
Coenzymes are often regarded as the second
substrates or co-substrafes, since thev have
affinity with the enzyme comparable with that of
the substrate.
the coenzymes are the derivatives of water
soluble B-complex vitamins. In fact, the
biochemical functions of B-complex vitamins are
exerted through their respective coenzyme.
40. LOCK- AND- KEY MODEL
• In the lock and key model of enzyme action:
-the active site has a rigid shap.
-only substrate with the matching shape can fit.
-the substrate is a key that fits the lock of the active
site.
-the amino acid R group of enzymes hepl to mediat
interaction of active site and substrate.
• This is an older model,however and does not work
for all enzymes.
Limitations
• Generally applicable for enzymes that
work on single type of substrate.
• It indicates the active site as a rigid
shape but it is actually flexible.
• Rigid shape is insensitive to enviroment
modification for substrate binding.
41. INDUCED FIT MODEL
• In the induced fit model of enzyme action:
-the active site is flexible,not rigid.
-the shape of the enzyme,active site and substrate
adjust to maximize the fit,which improves catalysis.
-there is greater range of substrate specificity
• This model is more consistant with a wider range
of enzymes.
Advantages:
Support enzymes which can act on different
Substrate of different conformations.
Enhance fidelity of molecular recognition
In presence of competitor via conformational
Proof reading.
Much accepted as enzymes are not rigid and
Different conditions promote differential interactions.
If it was rigid all the actions were same att always.
43. HOW ARE THEY FORMED?
• formed due to homologous or recombination of
genepair.
• i.e.during gene duplication the duplicate code is
retained which leads to formation of isoenzymes.
44. Isoenzymes existence’s explanation
1.lsoenzymes synthesized from different
genes e.g. malate dehydrogenase of cytosol
is different from that found in mitochondria.
2. Oligomeric enzymes consisting of more
than one type of subunits e.g. lactate
dehydrogenase and creatine
phosphokinase.
3. Isoenzyme may be active as monomer or
oligomer e.g. glutamate dehydrogenase.
4. Differences in carbohydrate content may
be responsible for isoenzymes e.g. alkaline
phosphatase.
45. Isoenzymes of Lactate Dehydrogenase
• Tetramer with foursubunits
• Subunits may be either H or M polypeptide
chain
• Due to different combination of H & M
5 isoforms are there
Isoform subunits Location
LDH1 H4 Heart
LDH2 H3M1 RBC
LDH3 H2M2 Brain
LDH4 H1M3 Liver
LDH5 M4 Muscle
Function:-convert locatate to pyruvate.
46. Isoenzymes of creatine phosphokinase
• Dimer
• Contain M and B subunits
• Has 3 isoforms
Isoform subunits Location
CPK1 MM Muscle
CPK2 MB Heart
CPK3 BB Brain
Function:-converts creatine phosphatase to creation.
47. Alkaline phosphatase
• Has 6 isoenzymes
• Monomer
• Isoenzymes are due to different in
carbohydrate content.
1. Alpha1 ALP -epithelial cells of biliary
canaliculi
2. Alpha2 ht labile -hepatic cells
3. Alpha2 ht stable -placenta
4. Pre beta ALP -bone
5. Gamma ALP -intestinal cells
6. Leukocyte ALP
48. ENZYME PATTERN IN
DISEASES
• Enzymes in myocardial infarction
Creatine phosphokinase
Asparate transaminase
Lactate dehydrogenase
Cardiac troponins
49. • Enzymes in liver diseases
• Enzymes in muscle diseases
• Enzymes in cancers
50. ENYME KINEETICS-FACTORS
• The catalytic properties of enzymes,and
consequently their activity,are influenced by
numerous factors.
• These factors include
Physical quantities(temperature,pressure)
The chemical properties of the solution (pH
vatue,ionic strength)
The concentrations of the relevent
subntrates,cofactors and inhibitors.
51. pH dependency of enzyme activity
• Eeffect of enzymes is strongly dependent on the Ph
• A ctivity is plotted against pH,a bell-shapped curve is
usually obtained
• Bell shape of the activity-pH profile results from the fact
that amino acid residues with ionizable groups in the side
chain are essential for catalysis.
pH dependency of enzyme
activity
• A basic group B(pKa=8)which has to be protonated in order
to become active.
• A second acidic amino acid AH(pKa=6),which is only active
in a dissociated state.
• At the optimum pH of 7,around 90%of both groups are
present in the active form.
• At higher and lower values,one or the other of the groups
52. Temperature dependency of enzyme
activity
• The pemperature dependency of enzymatic activity is
usually asymmetric.
• With increasing temperature,the increased thermal
movement of the molecules initially leads to a rate
acceleration.
• At a certain temperature the enzyme then becomes
unstable and its activity is lost within a narrow
temperature difference as a result of denaturation.
53.
54. HISTORIC RESUME FRIEDRICH
MIESCHER IN 1869
• Isolated what he called nuclein from the nuclei
of pus cells.
• Nuclein was shown to have acidic
properties,hemce it became called nucleic
acid.
NUCLEIC ACID
• Nucleicc asid aree polymers that consist of nucleotide
residues.
• Located in nuclei of cell.
• Hereditary determinants of living organisms
• Elemental composition-
carbon,hydrogen,oxygen,nitrogen and phosphorus.
56. The Distribution of nucleic acids in the
eukaryotic cell
• DNA is found in the nucleus
with small amounts in mitochondria and chloroplasts
• RNA is found throughtout the cell
NUCLEIC ACID
STRUCTURE
• Nucleic acids are polynucleotides
• Their building blocks are nucleotides
57. NUCLEOTIDES
• Energy rich compounds that drive meta bolic process in
cell
• Serve as chemical signals,key links in cellilar systems that
respond to hormones and other extracellular stimuli
• Structural component of an of enzyme cofactor and
metabollic intermediate
• Each nucleotide is formed by 3 units-
PHOSPHATE,SUGAR,NITROGENUOS BASE
58. NUCLEOSIDES
When ribose or 2-deoxyribose is
combinedwith purine and pyramidine base
Nucleoside is formed.
59. Properties of Nucleotides
Properties of purine bases
• Sparingly soluble in water
• Absorb light in UV region at 260 nm. (detection &
quantitation of nucleotides)
• Capable of forming hydrogen bond
• Aromatic base atoms numbered 1 to 9
• Purine ring is formed by fusion of pyrimidine ring
with imidazole ring.
• Numbering is anticlockwise.
Adenine : Chemically it is 6-aminopurine
Guanine : Chemically it is 2-amino,6-oxy purine
Can be present as lactam & lactim form
60. Properties of pyrimidine bases
• Sparingly soluble in water
• Absorb light in UV region at 260 nm. (detection &
quantitation of nucleotides)
• Capable of forming hydrogen bond
• Aromatic base atoms numbered 1 to 9
• Purine ring is formed by fusion of pyrimidine ring
with imidazole ring.
• Numbering is anticlockwise.
• Adenine : Chemically it is 6-aminopurine
• Guanine : Chemically it is 2-amino,6-oxy purine
Can be present as lactam & lactim form
61. Properties of pyrimidine bases
• Soluble at body pH
• Also absorb UV light at 260 nm
• Capable of forming hydrogen bond
• Aromatic base atoms are numbered 1 to 6 for
pyrimidine.
• Atoms or group attached to base atoms have same
number as the ring atom to which they are bonded.
• Cytosine: Chemically is 2-oxy ,4-amino pyrimidine
Exist both lactam or lactim form
• Thymine: Chemically is 2,4 dioxy ,5-methyl pyrimidine
• Occurs only in DNA
• Uracil: Chemically is 2,4 dioxy pyrimidine
Found only in RNA
62. Properties of Pentose Sugars
• A pentose is a monosaccharide with five carbon atoms.
• Ribose is the most common pentose with one oxygen
atom attached to each carbon atom.
• Deoxyribose sugar is derived from the sugar ribose by loss
of an oxygen atom.
• The aldehyde functional group in the carbohydrates react
with neighbouring hydroxyl functional groups to
form intramolecular hemiacetals.
• The resulting ring structure is related to furan, and is
termed a furanose.
• The ring spontaneously opens and closes, allowing rotation
to occur about the bond between the carbonyl group and
the neighboring carbon atom yielding two distinct
configurations (α and β). This process is
termed mutarotation.
64. Classification of Nucleosides
1. Adenosine nucleotides: ATP, ADP, AMP, Cyclic
AMP
2. Guanosine nucleotides: GTP, GDP, GMP, Cyclic
GMP
3. Cytidine nucleotides: CTP, CDP, CMP and
certain deoxy CDP derivatives of glucose,
choline and ethanolamine
4. Uridine nucleotides: UDP
5. Miscellaneous : PAPS (active sulphate), SAM
(active methionine), certain coenzymes like
NAD+, FAD, FMN, Cobamide coenzyme, CoA
65. GENETIC CODE
The genetic code can be defined as the set
of certain rules using which the living cells
translate the information encoded within
genetic material (DNA or mRNA sequences).
The ribosomes are responsible to
accomplish the process of translation. They
link the amino acids in an mRNA-specified
(messenger RNA) order using tRNA (transfer
RNA ) molecules to carry amino acids and
to read the mRNA three nucleotides at a
time.
67. A key point of the genetic code is its universal
nature. This indicates that virtually all species with
minor exceptions use the genetic code for protein
synthesis.
In other words, genetic code is defined as the
nucleotide sequence of the base on DNA which is
translated into a sequence of amino acids of the
protein to be synthesized.
Properties of Genetic Code
• Triplet code
• Non-ambiguous and Universal
• Degenerate code
• Nonoverlapping code
• Commaless
• Start and Stop Codons
• Polarity
68. Triplet code
The four bases of nucleotide i.e, (A, G, C, and U) are used
to produce three-base codons. The 64 codons involve
sense codons (that specify amino acids). Hence, there are
64 codons for 20 amino acids since every codon for one
amino acid means that there exist more than code for the
same amino acid.
Commaless code
No room for punctuation in between which indicates that
every codon is adjacent to the previous one without any
nucleotides between them.
Nonoverlapping code
The code is read sequentially in a group of three and a
nucleotide which becomes a part of triplet never becomes
part of the next triplet.
• For example
• 5’-UCU-3’ codes for Serine
• 5’-AUG-3’ codes for methionine
69. Polarity
Each triplet is read from 5’ → 3’ direction and the
beginning base is 5’ followed by the base in the middle
then the last base which is 3’. This implies that the codons
have a fixed polarity and if the codon is read in the reverse
direction, the base sequence of the codon would reverse
and would specify two different proteins.
Degenerate code
• Every amino acid except tryptophan (UGG) and methionine
(AUG) is coded by various codons, i.e, a few codons are
synonyms and this aspect is known as the degeneracy of
genetic code. For instance, UGA codes for tryptophan in
yeast mitochondria.
• Start and Stop Codons
• Generally, AUG codon is the initiating or start codon. The
polypeptide chain starts either with eukaryotes
(methionine) or prokaryotes (N- formylmethionine).
• On the other hand, UAG, UAA and UGA are called as
termination codons or stop codons. These are not read by
any tRNA molecules and they never code for any amino
acids.
70. Non-ambiguous and Universal
The genetic code is non-ambiguous which means a
specificcodon will only code for a particular amino acid. Also,
the same genetic code is seen valid for all the organisms i.e.
they are universal.