Enzymes are protein catalysts that lower the activation energy of biochemical reactions without being consumed. They achieve specificity by fitting substrates into their active sites. Enzyme activity is regulated through various mechanisms including feedback inhibition, cofactors, pH, temperature, and allosteric regulation. Inhibitors bind enzymes to reduce their activity, either reversibly or irreversibly. Enzymes have many applications in medicine including diagnostics, analytical tests, and enzyme replacement therapy.
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.
Enzymes are protein catalysts that accelerate biochemical reactions without being consumed. They are specific, catalytic, reversible, and sensitive to temperature and pH changes. Enzymes lower the activation energy of reactions. The active site of an enzyme binds specifically to substrates. Some enzymes require cofactors like metal ions or coenzymes to function. Enzyme kinetics examines factors that influence reaction rates like substrate concentration. Michaelis-Menten kinetics describes the reversible binding of enzymes and substrates to form enzyme-substrate complexes. Enzyme inhibitors decrease catalytic activity by binding to the active site or elsewhere on the enzyme.
The document discusses enzymes and their properties. It begins by defining enzymes as biological catalysts and describes their characteristics, including that they are not used up in chemical reactions. It then covers enzyme structure and function, classification, regulation, and clinical significance. Key points include: enzymes have an active site that facilitates reactions; there are multiple levels of enzyme classification based on the type of reaction catalyzed; factors like temperature, pH, and inhibitors can impact enzyme activity; isozymes and zymogens are discussed. Measurement of plasma enzyme levels is also described as being diagnostically useful.
This document defines enzymes and describes their key characteristics. It states that enzymes are biological catalysts that speed up chemical reactions without being used up in the process. The document outlines several models of enzyme action, including the lock-and-key and induced fit models. It also discusses factors that can affect an enzyme's activity, such as substrate concentration, temperature, and pH. Finally, it describes how enzymes are classified and their high specificity for particular reactions and substrates.
Enzymes are biological catalysts that are usually proteins and speed up biochemical reactions. They work by lowering the activation energy of reactions. Enzymes are very specific and only catalyze one type of reaction. The active site of an enzyme binds to specific substrates. Enzyme activity is affected by factors like pH, temperature, and substrate/product concentration. There are two main models for enzyme activity - the lock and key model suggests a rigid enzyme structure that substrates fit into, while the induced fit model suggests substrates cause enzyme structures to change shape for binding. Enzymes can be inhibited competitively by substrates that resemble their real substrates or non-competitively by other molecules.
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.
This document discusses enzymes and their properties. It defines enzymes as biocatalysts that are proteins synthesized by living cells. Enzymes lower the activation energy of chemical reactions and catalyze the formation of products. Enzymes can exist as single peptides or complexes of multiple subunits. They are classified based on the type of reaction catalyzed and have specific active sites that bind substrates. Many factors influence enzyme activity such as temperature, pH, substrate and inhibitor concentrations. The mechanisms of enzyme action and inhibition are also described.
Enzymes are protein catalysts that lower the activation energy of biochemical reactions without being consumed. They achieve specificity by fitting substrates into their active sites. Enzyme activity is regulated through various mechanisms including feedback inhibition, cofactors, pH, temperature, and allosteric regulation. Inhibitors bind enzymes to reduce their activity, either reversibly or irreversibly. Enzymes have many applications in medicine including diagnostics, analytical tests, and enzyme replacement therapy.
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.
Enzymes are protein catalysts that accelerate biochemical reactions without being consumed. They are specific, catalytic, reversible, and sensitive to temperature and pH changes. Enzymes lower the activation energy of reactions. The active site of an enzyme binds specifically to substrates. Some enzymes require cofactors like metal ions or coenzymes to function. Enzyme kinetics examines factors that influence reaction rates like substrate concentration. Michaelis-Menten kinetics describes the reversible binding of enzymes and substrates to form enzyme-substrate complexes. Enzyme inhibitors decrease catalytic activity by binding to the active site or elsewhere on the enzyme.
The document discusses enzymes and their properties. It begins by defining enzymes as biological catalysts and describes their characteristics, including that they are not used up in chemical reactions. It then covers enzyme structure and function, classification, regulation, and clinical significance. Key points include: enzymes have an active site that facilitates reactions; there are multiple levels of enzyme classification based on the type of reaction catalyzed; factors like temperature, pH, and inhibitors can impact enzyme activity; isozymes and zymogens are discussed. Measurement of plasma enzyme levels is also described as being diagnostically useful.
This document defines enzymes and describes their key characteristics. It states that enzymes are biological catalysts that speed up chemical reactions without being used up in the process. The document outlines several models of enzyme action, including the lock-and-key and induced fit models. It also discusses factors that can affect an enzyme's activity, such as substrate concentration, temperature, and pH. Finally, it describes how enzymes are classified and their high specificity for particular reactions and substrates.
Enzymes are biological catalysts that are usually proteins and speed up biochemical reactions. They work by lowering the activation energy of reactions. Enzymes are very specific and only catalyze one type of reaction. The active site of an enzyme binds to specific substrates. Enzyme activity is affected by factors like pH, temperature, and substrate/product concentration. There are two main models for enzyme activity - the lock and key model suggests a rigid enzyme structure that substrates fit into, while the induced fit model suggests substrates cause enzyme structures to change shape for binding. Enzymes can be inhibited competitively by substrates that resemble their real substrates or non-competitively by other molecules.
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.
This document discusses enzymes and their properties. It defines enzymes as biocatalysts that are proteins synthesized by living cells. Enzymes lower the activation energy of chemical reactions and catalyze the formation of products. Enzymes can exist as single peptides or complexes of multiple subunits. They are classified based on the type of reaction catalyzed and have specific active sites that bind substrates. Many factors influence enzyme activity such as temperature, pH, substrate and inhibitor concentrations. The mechanisms of enzyme action and inhibition are also described.
Enzymes are protein catalysts that accelerate chemical reactions in living organisms. They facilitate reactions by lowering the activation energy needed. Enzymes achieve specificity through their active sites, which are complementary in shape and chemical properties to their substrates. Factors like temperature, pH, and inhibitors can impact an enzyme's activity. There are several mechanisms of enzyme action and regulation, including competitive and non-competitive inhibition, as well as allosteric regulation through effectors binding at distinct sites. Precise control of enzymes is crucial for metabolic processes in cells and organisms.
Enzymes are biological molecules (typically proteins) that significantly speed up the rate of virtually all of the chemical reactions that take place within cells. They are vital for life and serve a wide range of important functions in the body, such as aiding in digestion and metabolism
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 and metabolism. It defines enzymes as proteins that catalyze chemical reactions and discusses the lock-and-key and induced-fit models of enzyme action. It also explains factors that influence enzyme activity such as pH and temperature, and describes the roles of coenzymes and enzyme inhibitors.
Enzymes are proteins that catalyze biochemical reactions in cells. They increase the rate of reactions by lowering activation energy. Most enzymes are named based on their substrate or the reaction they catalyze. Studying enzyme kinetics and regulation provides insight into metabolic pathways and cellular functions.
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 biomolecules that catalyze chemical reactions by lowering their activation energy. They speed up reactions without being used up. Enzymes have an active site where substrates bind and reactions occur. The Michaelis-Menten equation describes enzyme kinetics and defines terms like Km and Vmax. Enzyme activity is affected by factors like temperature, pH, substrate concentration, and inhibitors. Regulation occurs through competitive and allosteric inhibition or covalent modification like phosphorylation.
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 an overview of enzymes. It discusses that enzymes are protein catalysts that increase the rate of chemical reactions in living cells without changing themselves. The document describes the different components of enzyme molecules, including the protein component called the apoenzyme and various cofactors that can be organic compounds, inorganic ions, or prosthetic groups. It also discusses the active site of enzymes and mechanisms of enzyme action, such as induced fit and lock and key models. Additionally, it covers factors that affect enzyme activity like temperature, pH, substrate concentration, and enzyme concentration. The document summarizes different types of enzyme inhibition including competitive, non-competitive, and uncompetitive inhibition. Finally, it discusses mechanisms of regulating enzyme activity, including controlling enzyme
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.
Enzymes mechanism of action, their specificity types, active center structure and action, inhibitor types, fisher and Koshlend theory are presented. Enzymes classification, a new class of enzymes discovered recently, detailed explanation of each class reaction types is presented as well
Enzymes are protein catalysts that speed up biochemical reactions without being consumed. They have specific active sites that substrates bind to in order to be converted into products. Most enzymes require cofactors like metal ions, vitamins, or prosthetic groups to function properly. There are two main models of enzyme action - the lock and key model where the active site rigidly binds substrates, and the induced fit model where the active site changes shape upon substrate binding. Enzymes lower the activation energy of reactions, allowing them to proceed more quickly within cells without damaging heat. Some molecules can inhibit enzymes by blocking their active sites and preventing catalysis.
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 protein catalysts that speed up biochemical reactions without being consumed. They achieve this by lowering the activation energy of reactions. Enzymes are very specific and only catalyze one or a few reactions. The active site of an enzyme is where substrates bind and reactions occur. Many factors can influence an enzyme's activity, such as temperature, pH, substrate/product concentration, and inhibitors. Enzymes work by reducing the energy needed for reactions to occur and stabilizing the transition state.
This document summarizes various molecular interactions and mechanisms of regulation in cell events. It discusses how enzymes catalyze biochemical reactions through metabolic pathways, and how their activity is regulated through different mechanisms including allosteric effectors, covalent modification like phosphorylation, proteolytic cleavage, and end-product inhibition which provides negative feedback control of pathways.
Enzymes are protein catalysts found in cells and tissues. They are responsible for chemical reactions in the body and can be detected in serum to diagnose diseases. Increased enzyme levels in serum may indicate tissue damage or certain disease states. Common enzymes measured include alkaline phosphatase, acid phosphatase, amylase, lipase, SGPT and SGOT which can help diagnose diseases of the bones, prostate, pancreas and liver. Enzymes function as biological catalysts by lowering the activation energy of reactions and increasing their rates without being consumed in the process. They are highly specific and their activity can be affected by factors like pH, temperature, substrate and inhibitor concentrations.
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 their properties and functions. It begins by defining enzymes as proteins that act as biological catalysts to accelerate metabolic reactions within cells. Enzymes have several key properties, including that they are proteins, increase reaction rates, function at low concentrations, and catalyze reactions under moderate conditions. The mechanisms of enzyme action involve the binding of specific substrates to the active site of the enzyme, forming an activated transition state complex with a high energy that readily breaks down into products. Enzyme activity can be affected by various factors such as temperature, pH, activators, and inhibitors.
1. The document discusses the structure, properties, and mechanisms of enzyme action.
2. It describes how enzymes are classified and named based on their reactions.
3. Key factors that affect enzyme activity like pH, temperature, inhibitors, and cofactors are explained.
BREEDING METHODS FOR DISEASE RESISTANCE.pptxRASHMI M G
Plant breeding for disease resistance is a strategy to reduce crop losses caused by disease. Plants have an innate immune system that allows them to recognize pathogens and provide resistance. However, breeding for long-lasting resistance often involves combining multiple resistance genes
ANAMOLOUS SECONDARY GROWTH IN DICOT ROOTS.pptxRASHMI M G
Abnormal or anomalous secondary growth in plants. It defines secondary growth as an increase in plant girth due to vascular cambium or cork cambium. Anomalous secondary growth does not follow the normal pattern of a single vascular cambium producing xylem internally and phloem externally.
Enzymes are protein catalysts that accelerate chemical reactions in living organisms. They facilitate reactions by lowering the activation energy needed. Enzymes achieve specificity through their active sites, which are complementary in shape and chemical properties to their substrates. Factors like temperature, pH, and inhibitors can impact an enzyme's activity. There are several mechanisms of enzyme action and regulation, including competitive and non-competitive inhibition, as well as allosteric regulation through effectors binding at distinct sites. Precise control of enzymes is crucial for metabolic processes in cells and organisms.
Enzymes are biological molecules (typically proteins) that significantly speed up the rate of virtually all of the chemical reactions that take place within cells. They are vital for life and serve a wide range of important functions in the body, such as aiding in digestion and metabolism
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 and metabolism. It defines enzymes as proteins that catalyze chemical reactions and discusses the lock-and-key and induced-fit models of enzyme action. It also explains factors that influence enzyme activity such as pH and temperature, and describes the roles of coenzymes and enzyme inhibitors.
Enzymes are proteins that catalyze biochemical reactions in cells. They increase the rate of reactions by lowering activation energy. Most enzymes are named based on their substrate or the reaction they catalyze. Studying enzyme kinetics and regulation provides insight into metabolic pathways and cellular functions.
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 biomolecules that catalyze chemical reactions by lowering their activation energy. They speed up reactions without being used up. Enzymes have an active site where substrates bind and reactions occur. The Michaelis-Menten equation describes enzyme kinetics and defines terms like Km and Vmax. Enzyme activity is affected by factors like temperature, pH, substrate concentration, and inhibitors. Regulation occurs through competitive and allosteric inhibition or covalent modification like phosphorylation.
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 an overview of enzymes. It discusses that enzymes are protein catalysts that increase the rate of chemical reactions in living cells without changing themselves. The document describes the different components of enzyme molecules, including the protein component called the apoenzyme and various cofactors that can be organic compounds, inorganic ions, or prosthetic groups. It also discusses the active site of enzymes and mechanisms of enzyme action, such as induced fit and lock and key models. Additionally, it covers factors that affect enzyme activity like temperature, pH, substrate concentration, and enzyme concentration. The document summarizes different types of enzyme inhibition including competitive, non-competitive, and uncompetitive inhibition. Finally, it discusses mechanisms of regulating enzyme activity, including controlling enzyme
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.
Enzymes mechanism of action, their specificity types, active center structure and action, inhibitor types, fisher and Koshlend theory are presented. Enzymes classification, a new class of enzymes discovered recently, detailed explanation of each class reaction types is presented as well
Enzymes are protein catalysts that speed up biochemical reactions without being consumed. They have specific active sites that substrates bind to in order to be converted into products. Most enzymes require cofactors like metal ions, vitamins, or prosthetic groups to function properly. There are two main models of enzyme action - the lock and key model where the active site rigidly binds substrates, and the induced fit model where the active site changes shape upon substrate binding. Enzymes lower the activation energy of reactions, allowing them to proceed more quickly within cells without damaging heat. Some molecules can inhibit enzymes by blocking their active sites and preventing catalysis.
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 protein catalysts that speed up biochemical reactions without being consumed. They achieve this by lowering the activation energy of reactions. Enzymes are very specific and only catalyze one or a few reactions. The active site of an enzyme is where substrates bind and reactions occur. Many factors can influence an enzyme's activity, such as temperature, pH, substrate/product concentration, and inhibitors. Enzymes work by reducing the energy needed for reactions to occur and stabilizing the transition state.
This document summarizes various molecular interactions and mechanisms of regulation in cell events. It discusses how enzymes catalyze biochemical reactions through metabolic pathways, and how their activity is regulated through different mechanisms including allosteric effectors, covalent modification like phosphorylation, proteolytic cleavage, and end-product inhibition which provides negative feedback control of pathways.
Enzymes are protein catalysts found in cells and tissues. They are responsible for chemical reactions in the body and can be detected in serum to diagnose diseases. Increased enzyme levels in serum may indicate tissue damage or certain disease states. Common enzymes measured include alkaline phosphatase, acid phosphatase, amylase, lipase, SGPT and SGOT which can help diagnose diseases of the bones, prostate, pancreas and liver. Enzymes function as biological catalysts by lowering the activation energy of reactions and increasing their rates without being consumed in the process. They are highly specific and their activity can be affected by factors like pH, temperature, substrate and inhibitor concentrations.
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 their properties and functions. It begins by defining enzymes as proteins that act as biological catalysts to accelerate metabolic reactions within cells. Enzymes have several key properties, including that they are proteins, increase reaction rates, function at low concentrations, and catalyze reactions under moderate conditions. The mechanisms of enzyme action involve the binding of specific substrates to the active site of the enzyme, forming an activated transition state complex with a high energy that readily breaks down into products. Enzyme activity can be affected by various factors such as temperature, pH, activators, and inhibitors.
1. The document discusses the structure, properties, and mechanisms of enzyme action.
2. It describes how enzymes are classified and named based on their reactions.
3. Key factors that affect enzyme activity like pH, temperature, inhibitors, and cofactors are explained.
BREEDING METHODS FOR DISEASE RESISTANCE.pptxRASHMI M G
Plant breeding for disease resistance is a strategy to reduce crop losses caused by disease. Plants have an innate immune system that allows them to recognize pathogens and provide resistance. However, breeding for long-lasting resistance often involves combining multiple resistance genes
ANAMOLOUS SECONDARY GROWTH IN DICOT ROOTS.pptxRASHMI M G
Abnormal or anomalous secondary growth in plants. It defines secondary growth as an increase in plant girth due to vascular cambium or cork cambium. Anomalous secondary growth does not follow the normal pattern of a single vascular cambium producing xylem internally and phloem externally.
EMERGENCE OF THE FIRST LIVING CELL [Autosaved].pptxRASHMI M G
The origin of life on Earth is a mystery of science, with no widely accepted theory but many hypotheses supported by evidence. The earliest known fossils are 3.5 billion years old, but there is evidence that bacteria-like organisms lived on Earth 3.5 billion years ago, and may have existed even earlier, when the first solid crust formed, almost 4 billion years ago. Scientists think that early life may have formed from lighting strikes or arisen in deep sea vents.
ANATOMY OF DICOT AND MONOCOT LEAVES.pptxRASHMI M G
A leaf is a principal appendage of the stem of a vascular plant, usually borne laterally aboveground and specialized for photosynthesis. Leaves are collectively called foliage, as in "autumn foliage", while the leaves, stem, flower, and fruit collectively form the shoot system
A leaf is made up of three main parts: the blade (lamina), the petiole (leaf stalk), and the stipules. The blade is the flat, green surface of the leaf, and is made up of veins and veinlets. The petiole is a long, thin stalk that connects the blade to the stem. The stipules are two small leaf-like structures located on either side of the petiole base.
INTRODUCTION TO THE PROCESSING OF TOBACCO LEAVES.pptxRASHMI M G
Tobacco is the common name of several plants in the genus Nicotiana of the family Solanaceae, and the general term for any product prepared from the cured leaves of these plants. More than 70 species of tobacco are known, but the chief commercial crop is N. tabacum.
STRUCTURE AND FUNCTIONS OF NUCLEUS OF A CELL.pptxRASHMI M G
The nucleus is the part of a cell that contains DNA organized into chromosomes and is located in the middle of the cell. It is surrounded by the nuclear envelope, which is a double membrane that separates the nucleus from the cytoplasm. The nuclear envelope contains nuclear pores, which are gateways that allow molecules to move into and out of the nucleus.
The Cell: The Histology Guide
Nucleus - The Cell: The Histology Guide - University of Leeds
The nucleus is found in the middle of the cells, and it contains DNA arranged in chromosomes. It is surrounded by the nuclear envelope, a double nuclear membrane (outer and inner), which separates the nucleus from the cytoplasm. The outer membrane is continuous with the rough endoplasmic reticulum.
open.baypath.edu
Nucleus – BIO109 Biology I Introduction to Biology
The boundary of the nucleus, called the nuclear envelope, is a double membrane that contains small openings called nuclear pores. These pores are gateways that allow molecules to move into and out of the nucleus, enabling it to communicate with the rest of the cell.
The nucleus has three main parts:
Nuclear membrane: A protective barrier of the nucleus
Nucleoplasm: The cytoplasm of the nucleus, which is a semifluid matrix that contains chromatin, the less condensed form of DNA that organizes into chromosomes during mitosis or cell division
Nucleolus: A spherical structure that produces and assembles the cell's ribosomes
The nucleus controls and regulates the activities of the cell, such as growth and metabolism.
What are the 4 types of nucleus?
What are the 3 parts of a nucleus?
How many nuclei are in a cell?
Ask a follow up
CONTRIBUTION OF PANCHANAN MAHESHWARI.pptxRASHMI M G
Panchanan Maheswari, FRS (9 November 1904 – 18 May 1966 in Jaipur Rajasthan) a prominent Indian botanist noted chiefly for his invention of the technique of test-tube fertilization of angiosperms. This invention has allowed the creation of new hybrid plants that could not previously be crossbred naturally.He also emphasised the need for initiation of work on artificial culture of immature embryos
PHLOEM NECROSIS OF COFFEE PLANTDISEASE.pptxRASHMI M G
HOST- COFFEE
PATHOGEN- Phytomonas leptovasorum
Necrosis is the commonest and most destructive type of effect. As a result of successful infection of host plant by the pathogen a number of physiological changes occur in plant. Respiration, photosynthesis, nitrogen metabolism and transpiration are affected. There will be reduced rate of photosynthesis.
This in turn occurs a huge economically losses to the owner of plantation as it causes low yield and low quality of yield.
BENTHAM AND HOOKER SYSTEM OF CLASSIFICATION.pptxRASHMI M G
Bentham and Hooker system of plant classification is the best example of natural system of classification
Their contribution to the field of taxonomy and plant systematics is enormous
Their classification is of practical importance even today
The 3 volume work ‘Genera Plantarum’ published by them It consists of descriptions with names and classification of about 97,205 seed plants (flowering plants) belonging to 7569 genera of 200 families of flowering plants.
PRIONS-structure, multiplication, diseases.pptxRASHMI M G
PRIONS are infectious agents composed primarily of sialoglycoprotein.
This protein is called prion protein (PrP)
They contain no nucleic acid.
They cause a variety of neurodegenerative diseases in humans and animals.
According to STANLEY PRUSINER,
Prions- ‘which means proteinaceous and infectious (-on by analogy to virion) that lacks nucleic acid’.
It refers to a previously undescribed form of infection due to protein misfolding . While the infectious agent was named prion, and the specific protein that make the prion was named PrP i.e. ‘protease resistant protein’.
PRIONS proteins in the form of fibres which also occur as fold rods.
The normal protein found in a variety of tissues is referred to as PrPC (C refers to cellular or common PrP), whereas the misfolded form of PrPC is called PrPSc which is responsible for the formation of amyloid plaques that results in neurodegeneration.
PrPSc is the infectious form of PrPC, (Sc refers to scrapie, a prion disease occurring in sheep) .
PrPc is a Alpha helical while PrPSc is a beta pleated sheet
PrPc do not contain beta sheet.
PrPc protein can adopt 2 distinct different stable conformations.
All known prions induce the formation of an amyloid fold in which the protein polymerizes into an aggregate consisting of tightly packed beta sheets.
This altered structure is extremely stable and accumulates in the infected tissue causing cell death and tissue damage resulting in death of animals.
It is supposed that the diseased form of PRION (PrPSc) originated spontaneously or transmitted through ingestion of food/feed directly interacts with the normal endogenous form PrPC and enables to rearrange its structure.
As a result of interaction the normal form PrPC is converted to abnormal form (PrPSc) .
It is assumed that an unidentified cellular protein (protein X) helps the conversion of PrPC to PrPSc by bringing a molecule of each of the two together into a complex.
Main reason for the cause of prions is ‘cannibalism’ i.e. eating of one human by another human.
2 types of cannibalism – endocannibalism (eating humans from the same community) and exocannibalism ( eating humans from other communities).
The tribal ground up the brain into a pale grey soup, heated it and ate it.
Therefore, ingestion of brain tissue of dead relatives for religious reasons was likely the route of transmission.
In cattles
-BOVINE SPONGIFORM ENCEPHALOPATHY
(mad cow disease).
2. In humans
-ALZHEIMER’S DISEASE
DOWN’S SYNDROME
FATAL FAMILIAL INSOMNIA
KURU LEPROSY
BIOTECHNOLOGICAL TO PLANT DISEASE MANAGEMENT.pptxRASHMI M G
The document discusses plant diseases and biotechnology. It defines disease as a malfunctioning process in plants caused by continuous irritation that results in suffering. Plant pathology deals with studying the nature, development and control of plant diseases. The objectives of plant pathology include understanding disease etiology, pathogenesis, epidemiology, and control. Biotechnology techniques like tissue culture and genetic engineering can be used for crop improvement by allowing rapid propagation, disease elimination, hybrid development, and genetic modification to add traits like herbicide or insect resistance. These techniques help meet growing food demands as the human population increases.
THALLUS ORGANISATION OF CHLOROPHYCEAE.pptxRASHMI M G
This document discusses the different types of thallus organization found in algae, particularly the Chlorophyceae class. It describes unicellular motile and non-motile forms, multicellular flagellated and non-flagellated colonial forms, plamelloid forms, filamentous forms, heterotrichous forms, and siphonous forms. A wide variety of thallus structures have evolved to allow algae to survive in their environments, with all necessary cellular activities occurring within their thallus organization.
Lipids-definition, functions.
Fatty acids- saturated and unsaturated fatty acids-definition, examples
Essential and non essential fatty acids, melting point of fatty acids.
Triacylglycerol and wax, phospholipids, glycolipids, Eicosanoids, plasma lipoproteins
B-DNA, Z-DNA, A-DNA, stability of dsDNA helix, DNA denaturation, factors affecting Tm ,GC content, ionic strength, DNA as a genetic material, Griffith’s experiment, Hershey-chase experiment
Main Java[All of the Base Concepts}.docxadhitya5119
This is part 1 of my Java Learning Journey. This Contains Custom methods, classes, constructors, packages, multithreading , try- catch block, finally block and more.
it describes the bony anatomy including the femoral head , acetabulum, labrum . also discusses the capsule , ligaments . muscle that act on the hip joint and the range of motion are outlined. factors affecting hip joint stability and weight transmission through the joint are summarized.
A review of the growth of the Israel Genealogy Research Association Database Collection for the last 12 months. Our collection is now passed the 3 million mark and still growing. See which archives have contributed the most. See the different types of records we have, and which years have had records added. You can also see what we have for the future.
How to Manage Your Lost Opportunities in Odoo 17 CRMCeline George
Odoo 17 CRM allows us to track why we lose sales opportunities with "Lost Reasons." This helps analyze our sales process and identify areas for improvement. Here's how to configure lost reasons in Odoo 17 CRM
This presentation was provided by Steph Pollock of The American Psychological Association’s Journals Program, and Damita Snow, of The American Society of Civil Engineers (ASCE), for the initial session of NISO's 2024 Training Series "DEIA in the Scholarly Landscape." Session One: 'Setting Expectations: a DEIA Primer,' was held June 6, 2024.
This presentation includes basic of PCOS their pathology and treatment and also Ayurveda correlation of PCOS and Ayurvedic line of treatment mentioned in classics.
How to Build a Module in Odoo 17 Using the Scaffold MethodCeline George
Odoo provides an option for creating a module by using a single line command. By using this command the user can make a whole structure of a module. It is very easy for a beginner to make a module. There is no need to make each file manually. This slide will show how to create a module using the scaffold method.
How to Fix the Import Error in the Odoo 17Celine George
An import error occurs when a program fails to import a module or library, disrupting its execution. In languages like Python, this issue arises when the specified module cannot be found or accessed, hindering the program's functionality. Resolving import errors is crucial for maintaining smooth software operation and uninterrupted development processes.
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Physiology and chemistry of skin and pigmentation, hairs, scalp, lips and nail, Cleansing cream, Lotions, Face powders, Face packs, Lipsticks, Bath products, soaps and baby product,
Preparation and standardization of the following : Tonic, Bleaches, Dentifrices and Mouth washes & Tooth Pastes, Cosmetics for Nails.
2. Is a biocatalyst that increases the rate of
chemical reactions without itself being
changed in the overall process
Virtually all cellular reactions or processes
are mediated by enzymes
It has several properties which makes them
unique
3. 1. Most but not all enzymes are proteins. With the
exception of small group of catalytic RNA
molecule, all enzymes are protein
2. Enzymes are highly specific. They are
specialized proteins and have a high degree of
specificity for their substrates
3. They exhibit enormous catalytic power. It
increases the rate of reaction by lowering the
activation energy
4. They do not change the equilibrium state of a
biochemical reaction. It changes only the rate
at which equilibrium is achieved
4. proteinaceous enzymes
Simple enzymes
Consists entirely of amino acids
Conjugated enzymes
Consists of proteins as well as non
protein components
Non protein component is called
cofactor, which is required for
catalytic activity.
Removal of cofactor form a
conjugated enzyme leaves only
protein component called as
apoenzyme which is generally
biologically inactive
The complete biologically active
conjugated enzyme is called a
holoenzyme
5. vitamin Coenzyme form Reaction/ process
promoted
thiamine Thiamine pyrophosphate decarboxylation,
aldehyde group transfer
riboflavin FAD and FMN Redox reaction
pyridoxine Pyridoxal phosphate Amino group transfer
Nicotinic acid NAD+ and NADP+ Redox reaction
Pantothenic acid Coenzyme A Acyl group transfer
biotin bicytin carboxylation
Folic acid Tetrahydrofolic acid One carbon group
transfer
Vitamin B12 deoxyadenosylcobalami
n
Intramolecular
rearrangements
6. Many enzymes have common names
Ex. Trypsin a proteolytic enzymes, is secreted
by the pancreas
Common names- provide little information about
their reactions that enzyme catalyze
Many enzymes are named for their substrates
and for reactions that they catalyze, with the
suffix –ase added
Ex. ATPase that helps breaking down ATP
whereas
ATP synthase which helps in synthesis of ATP
7. International commission of enzymes was established to
create a systematic basis for enzyme nomenclature
Rules for naming enzymes-
Each enzyme is classified and named according to the
type of chemical reaction it catalyze
The ENZYME COMMISSION (EC)has given each enzyme
a number with 4 parts, like, EC 2.7.1.2 (hexokinase)
The 1st 3 numbers define major class, subclass and sub-
subclass respectively
The last number is a serial number in the sub- class,
indicating the order in which each enzyme is added to the
list
8. Common name and EC number of some
enzymes
Alcohol dehydrogenase EC 1.1.1.1
phosphofructokinase EC 2.7.1.11
Glutamine synthetase EC 6.3.1.2
Acetyl cholinesterase EC 3.1.1.7
9. The first integer in the EC number
designates the class of enzymes
There are 6 classes to which different
enzymes belong. These classes are-
EC1 oxidoreductase
EC 2 transferase
EC 3 hydrolases
EC 4 lyases
EC 5 isomerases
11. EC 2 TRANSFERASES
Catalyzes reactions that involve the transfer of
groups from one molecule to another. Examples
of such groups include amino, carboxyl,
carbonyl, methyl, phosphoryl and acyl common
trivial names for the transferases often include
the prefix trans
A-B + C A + B-C
Ex. Transcarboxylases, kinases,
transaminases, phosphorylases
12. EC 3 HYDROLASES
Catalyzes reactions in which the cleavage of
bond is accomplished by adding water
A-B + H2O A-H + B-OH
Ex. Phosphodiesterases, phosphatases,
peptidases
13. EC 4 LYASES
Catalyzes the breaking of C-C, C-O, C-N, C-
S and other bonds by means other than
hydrolysis or oxidation
A=B + HX A-X + B-H
Ex. aldolases, synthases, dehydratases,
decarboxylases
14. EC 5 ISOMERASES
Catalyzes several types of intramolecular
rearrangements and yield isomeric forms
A-B B-A
Ex. Mutases, cis trans isomerases,
epimerases, racemases
15. EC 6 LIGASES
Catalyzes the formation of C-C, C-S, C-O,
C-N bonds with simultaneous hydrolysis of
ATP
A+ B+ ATP A-B + ADP
Ex. Carboxylases
16. It increases the rate of a chemical reaction by
lowering the activation energy
The free energy of reaction, ∆G, remains
unchanged in the presence of an enzyme, so
the relative amounts of reactants and products
at equilibrium are unchanged it only accelerates
the attainment of equilibria but do not shift their
positions
The formation of an enzyme- substrate complex
is the first step in enzymatic catalysis
17. The binding between the enzyme and substrate is highly specific
The given enzyme usually binds to only one kind of substrate
Active site is the region of the enzyme where substrate binds and catalysis occurs
The substrate binds to active site of an enzyme by multiple weak
non covalent interactions
Formation of an enzyme substrate complex
Enzyme first binds to the substrate, the compound to be
catalyzed
18. LOCK AND KEY MODEL
Assumes a high degree of complementarity
between the shape of the substrate and
geometry of binding site on the enzyme
The complementarity between enzymes and
their substrates is the basis of the lock and
key model of enzyme function
This model was proposed by Emil Fischer
19.
20. INDUCED FIT MODEL
Enzymes are flexible and that the shapes of
the active site can be markedly modified by
binding of substrate
The binding of substrate induces a
conformational change in the enzyme that
results in a complementary fit once the
substrate is bound the binding site has a
different 3 dimensional shape before the
substrate is bound
21.
22. An enzyme catalyzed chemical
reaction in which substrate S
changes into product
P goes through transition state
The substrate and product
correspond to low free energy
structures
The point of highest free energy is
the transition state in which the
substrates are partially converted to
products
23. Amounts of enzymes can either be expressed
as molar amounts or measured in terms of
activity
Enzymes are usually present in very small
quantities so a convenient method of enzyme
quantification is a measurement of catalytic
activity
There are 2 standard units to express enzyme
activity
Enzyme unit –U
Katal - KAT
24. Inhibition of enzyme activity may be reversible or
irreversible
In reversible inhibition, inhibitor called irreversible
inhibitor binds tightly to the enzyme
Inhibitor dissociates very slowly from the enzyme
and enzyme’s catalytic activity is permanently
inhibited
The antibiotic penicillin acts as an irreversible
inhibitor of the enzyme glycopeptide transpeptidase
Aspirin binds covalently with enzyme
cyclooxygenase, reducing the synthesis of
prostaglandin
25. In reversible inhibitions, inhibitors called
reversible inhibitor binds non covalently to
the enzyme and dissociates rapidly from the
enzyme the effect of a reversible inhibitor is
reversed after dissociation of inhibitor from
enzyme
There are 3 types of reversible inhibition
Competitive
Uncompetitive
Non competitive
26. The structure of a competitive inhibitor closely
resembles that of the enzyme’s normal substrate.
Because of its structure, a competitive inhibitor
binds reversibly to the enzyme’s active site
The inhibitor forms an enzyme- inhibitor
complex(EI) that is equivalent to the ES complex
the effect of a competitve inhibitor on activity can
be reversed by increasing the concentration of
substrate
At high S all the active sites are filled with substrate
and reaction velocity reaches the value observed
without an inhibitor
27. The inhibitor binds to the enzyme at a site other than the
active site
Inhibitor binding alters the enzyme’s 3 dimensional
configuration and blocks the reaction
There are 2 types of non competitive inhibition- pure and
mixed
In pure non competitive inhibition- substrate and inhibitor
binds at different sites on enzyme and binding of inhibitor
does not affect binding of substrate
In mixed non competitive inhibition- the binding of inhibitor
with enzyme influences the binding of substrate with
enzyme
28. The inhibitor binds at the site distinct from
the substrate
It will bind only to the ES complex
On the other hand non competitive inhibitor
binds to either free enzyme or the ES
complex