Enzyme ppt
•Download as PPT, PDF•
0 likes•147 views
Enzymes are proteins that act as catalysts to accelerate chemical reactions in living organisms. They are highly specific and reusable. Most enzymes have tertiary and quaternary protein structures and contain an active site that binds to substrates. The substrate induces a fit between the enzyme and substrate that lowers the activation energy of the reaction. Environmental conditions like temperature and pH can impact enzyme activity, as can cofactors, coenzymes, and enzyme inhibitors which may compete for or alter the active site.
Report
Share
Report
Share
Recommended
Enzymes for hbs
Enzymes are proteins that act as biological catalysts and are necessary for most chemical reactions in living cells. They help reactions occur by lowering their activation energy. Enzymes have a unique three-dimensional shape with active sites that allow them to specifically bind to substrates and rearrange the molecules involved in chemical steps. While they are not consumed in these reactions, enzymes increase the rates of reactions and can be reused, making them highly efficient biological catalysts.
Lecture 9
The document contains sample questions about nucleic acids and enzymes. For nucleic acids, it asks about nucleosides, the difference between RNA and DNA sugars, gel electrophoresis of DNA fragments, light absorption of nucleotides and proteins, components found in RNA but not DNA, and base pairing rules. It also includes questions about translating mRNA and forming codon-anticodon interactions. For enzymes, it discusses them as catalysts, mechanisms of catalysis including transition states and active sites, classes of enzymes, coenzymes, and factors affecting enzyme activity. Sample multiple choice questions test understanding of enzyme function, naming, components, effects of temperature, and catalytic mechanisms.
Enzymes and digestion2
The document discusses the role of digestive enzymes in breaking down food molecules in the digestive system. Starch is broken down by amylase and maltase. Proteins are broken down by trypsin and peptidases. Lipase breaks down fats into fatty acids and glycerol. The structure and specificity of enzymes is also described.
enzyme ppt
This document provides an overview of enzymes. It explains that enzymes are proteins that act as catalysts to accelerate chemical reactions without being permanently altered. Enzymes are specific and reusable, and their names typically end in "-ase". The document also describes how enzymes work by weakening bonds to lower activation energy. Additionally, it explains that enzymes bind to substrates at active sites and may undergo an induced fit when binding. Finally, the document outlines factors that can affect enzyme activity, such as environmental conditions, cofactors/coenzymes, and competitive or noncompetitive inhibitors.
Enzymes for Engineers, Biologists, Physicists and Chemists
Enzymes: Purpose: To convey that without catalysis life would not have
existed on earth. Enzymology: How to monitor enzyme catalysed reactions.
How does an enzyme catalyse reactions? Enzyme classification. Mechanism
of enzyme action. Discuss at least two examples. Enzyme kinetics and
kinetic
How does an enzyme catalyse reactions? Enzyme classification. Mechanism
of enzyme action. Discuss at least two examples. Enzyme kinetics and
kinetic
Biochem p3 g6
Enzymes are protein molecules that act as catalysts to speed up biochemical reactions. They work by providing an alternative reaction pathway requiring less activation energy. An enzyme only catalyzes the reaction if the substrate fits within its active site like a lock and key. Enzymes are essential to the chemical processes that sustain life as they allow reactions to occur within cells, tissues, and organs that keep the body functioning.
Enzyme
Enzymes are protein catalysts that accelerate chemical reactions without being permanently altered themselves. They work by lowering the activation energy of reactions. Most enzymes are highly specific and only catalyze one or a few related reactions. The part of the enzyme where substrates bind is called the active site. Enzymes can be affected by various environmental factors like temperature and pH, as well as by inhibitors that prevent substrate binding and reaction. Enzymes are crucial to countless metabolic processes in living organisms.
Enzynes
Enzymes are protein catalysts that accelerate chemical reactions without being permanently altered. They work by weakening bonds between reactants to lower the activation energy needed for the reaction. Enzymes have an active site that binds specifically to substrates. When the substrate binds, an induced fit may occur where the active site changes shape to better accommodate the substrate. Environmental conditions like temperature and pH can affect enzyme activity, as can cofactors that are sometimes required for proper function. Enzyme inhibitors can also decrease activity by competing for the active site or binding elsewhere and inducing a shape change in the enzyme.
Recommended
Enzymes for hbs
Enzymes are proteins that act as biological catalysts and are necessary for most chemical reactions in living cells. They help reactions occur by lowering their activation energy. Enzymes have a unique three-dimensional shape with active sites that allow them to specifically bind to substrates and rearrange the molecules involved in chemical steps. While they are not consumed in these reactions, enzymes increase the rates of reactions and can be reused, making them highly efficient biological catalysts.
Lecture 9
The document contains sample questions about nucleic acids and enzymes. For nucleic acids, it asks about nucleosides, the difference between RNA and DNA sugars, gel electrophoresis of DNA fragments, light absorption of nucleotides and proteins, components found in RNA but not DNA, and base pairing rules. It also includes questions about translating mRNA and forming codon-anticodon interactions. For enzymes, it discusses them as catalysts, mechanisms of catalysis including transition states and active sites, classes of enzymes, coenzymes, and factors affecting enzyme activity. Sample multiple choice questions test understanding of enzyme function, naming, components, effects of temperature, and catalytic mechanisms.
Enzymes and digestion2
The document discusses the role of digestive enzymes in breaking down food molecules in the digestive system. Starch is broken down by amylase and maltase. Proteins are broken down by trypsin and peptidases. Lipase breaks down fats into fatty acids and glycerol. The structure and specificity of enzymes is also described.
enzyme ppt
This document provides an overview of enzymes. It explains that enzymes are proteins that act as catalysts to accelerate chemical reactions without being permanently altered. Enzymes are specific and reusable, and their names typically end in "-ase". The document also describes how enzymes work by weakening bonds to lower activation energy. Additionally, it explains that enzymes bind to substrates at active sites and may undergo an induced fit when binding. Finally, the document outlines factors that can affect enzyme activity, such as environmental conditions, cofactors/coenzymes, and competitive or noncompetitive inhibitors.
Enzymes for Engineers, Biologists, Physicists and Chemists
Enzymes: Purpose: To convey that without catalysis life would not have
existed on earth. Enzymology: How to monitor enzyme catalysed reactions.
How does an enzyme catalyse reactions? Enzyme classification. Mechanism
of enzyme action. Discuss at least two examples. Enzyme kinetics and
kinetic
How does an enzyme catalyse reactions? Enzyme classification. Mechanism
of enzyme action. Discuss at least two examples. Enzyme kinetics and
kinetic
Biochem p3 g6
Enzymes are protein molecules that act as catalysts to speed up biochemical reactions. They work by providing an alternative reaction pathway requiring less activation energy. An enzyme only catalyzes the reaction if the substrate fits within its active site like a lock and key. Enzymes are essential to the chemical processes that sustain life as they allow reactions to occur within cells, tissues, and organs that keep the body functioning.
Enzyme
Enzymes are protein catalysts that accelerate chemical reactions without being permanently altered themselves. They work by lowering the activation energy of reactions. Most enzymes are highly specific and only catalyze one or a few related reactions. The part of the enzyme where substrates bind is called the active site. Enzymes can be affected by various environmental factors like temperature and pH, as well as by inhibitors that prevent substrate binding and reaction. Enzymes are crucial to countless metabolic processes in living organisms.
Enzynes
Enzymes are protein catalysts that accelerate chemical reactions without being permanently altered. They work by weakening bonds between reactants to lower the activation energy needed for the reaction. Enzymes have an active site that binds specifically to substrates. When the substrate binds, an induced fit may occur where the active site changes shape to better accommodate the substrate. Environmental conditions like temperature and pH can affect enzyme activity, as can cofactors that are sometimes required for proper function. Enzyme inhibitors can also decrease activity by competing for the active site or binding elsewhere and inducing a shape change in the enzyme.
Biochemistry lecture notes enzymes
Enzymes are protein catalysts that greatly increase the rates of biochemical reactions. They achieve this by lowering the activation energy of reactions. Enzymes are highly specific and only catalyze one or a small number of reaction types. The enzyme binds to its substrate at its active site, and uses functional groups to facilitate the reaction, ultimately releasing the product. Many factors can influence an enzyme's activity level, including its concentration, the substrate concentration, temperature, pH, and the presence of inhibitors.
Enzymes.pptx
An enzyme is a biological catalyst and is almost always a protein. It speeds up the rate of a specific chemical reaction in the cell. The enzyme is not destroyed during the reaction and is used over and over.
5. Biochemistry of enzymes edited 2024.pptx
Enzymes are biological catalysts that regulate biochemical reactions. This document discusses the composition, mechanisms, and factors that influence enzyme activity. It describes how enzymes lower activation energy and use an active site to bind substrates and stabilize reaction intermediates. The Michaelis-Menten equation models how reaction rate varies with substrate concentration in relation to parameters like Vmax and Km. Environmental factors like temperature and pH can impact enzyme activity.
Enzymes
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.
Enzymes
Enzymes are protein catalysts that speed up biochemical reactions without being consumed. They work by lowering the activation energy of reactions. Enzymes have specific active sites that bind substrates and induce a conformational change through induced fit. This allows the enzyme to accelerate the reaction and produce products. The rate of enzyme reactions can be affected by environmental factors like temperature, pH, and concentrations of enzymes and substrates.
Catalysis lecture 4
This document provides an overview of enzyme catalysis. It discusses that enzymes are protein molecules that act as catalysts to speed up organic reactions in living cells. Enzymes have high selectivity and efficiency, with one molecule able to catalyze millions of reactions per minute. The rate of enzyme-catalyzed reactions is maximum at the optimum temperature and pH. Enzymes can be inhibited or destroyed by other substances but their activity is enhanced by activators or coenzymes. The mechanism of enzyme catalysis involves the substrate binding to the active site of the enzyme in a lock-and-key fashion to form a complex that then decomposes to release the products.
Overview of enzyme
This slideshow is about overview of enzyme. It describes important properties of enzymes, classification, functions and mode of action.
Enzymes Topic - Power Point Presentation
Enzymes are proteins that act as biological catalysts to speed up chemical reactions in the body without being consumed. They achieve this by lowering the activation energy of reactions. Enzymes are highly specific and only catalyze particular substrate molecules. They function by inducing a temporary change in shape at their active site to accommodate the substrate before releasing the products. Enzyme activity can be affected by environmental conditions like temperature and pH, as well as cofactors and inhibitors that influence the enzyme's structure and ability to bind substrates.
Enzymes (An Introductory Approach)
1. Enzymes are biological catalysts that speed up reactions by lowering activation energy.
2. Enzymes have specific active sites that substrates bind to, and can break down or join substrates.
3. Enzymes are proteins but some are RNA molecules called ribozymes, and their activity is affected by temperature, pH, substrate concentration and other factors.
Enzyme structure and Mechanism of Action
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.
CHAPTER 6.pptx
- Enzymes are protein biocatalysts that increase the rate of chemical reactions without being consumed. They are specific in their action and composed of apoenzyme and coenzyme.
- The active site of an enzyme binds specifically to substrates and contains residues that help hold the substrate. Changes to the active site shape affect enzyme function.
- Factors like temperature, pH, substrate/product concentration, and presence of activators or inhibitors can regulate an enzyme's activity rate. Studying an enzyme's kinetics reveals its catalytic mechanism.
- Regulation allows cells to control metabolic pathways by modulating enzyme activity. Competitive inhibitors bind the active site while non-competitive inhibitors cause conformational changes. I
Enzymes.pptx
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.
enzyme cmlt 2nd year.pptx
1. Enzymes are protein catalysts that regulate chemical reactions in living cells without undergoing any permanent changes themselves.
2. They function by binding to a specific substrate and lowering the activation energy of a reaction, greatly increasing the reaction rate.
3. The active site of an enzyme is where substrate binding and catalysis occur. Factors like temperature, pH, and inhibitor binding can impact enzyme activity levels.
Enzyme ppt by yograj
Enzymes are proteins that act as catalysts to accelerate chemical reactions without being permanently changed themselves. They are specific to the substrates they catalyze and contain an active site, a restricted region that binds to the substrate. When the substrate binds, an induced fit may occur where the enzyme's shape changes to better accommodate the substrate. Enzyme activity can be affected by environmental conditions like temperature and pH, cofactors and coenzymes that are required for activity, and enzyme inhibitors that compete with the substrate for the active site or bind elsewhere and alter the enzyme's shape.
ENZYMES.pptx
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.
Enzyme part A
Most enzymes are Proteins (tertiary and quaternary structures)
Act as Catalyst to accelerates a reaction
Not permanently changed in the process
Enzymes
1. Enzymes are protein catalysts that speed up chemical reactions without being consumed in the process. They achieve specificity by inducing conformational changes that tightly bind substrates in the active site.
2. The induced fit model proposes that weak initial interactions between the enzyme and substrate induce structural changes that strengthen binding.
3. Key factors that affect enzyme activity include temperature, pH, enzyme concentration, and substrate concentration. Activity is optimized within narrow ranges for each factor.
Unit 4: Plasma Enzyme tests in diagnosis
This document provides an overview of plasma enzyme tests and their use in diagnosis. It discusses factors that affect enzyme reaction rates, the clinical usefulness of measuring serum enzyme levels, and specific enzymes that are useful in diagnosing various disorders, including cardiac, hepatic, bone, muscle, malignancies and acute pancreatitis. The document also covers enzyme kinetics, the advantages and disadvantages of enzyme assays, how enzyme activity is measured and calculated, and the classification of different enzyme types.
Enzymes-.pdf
Metabolism involves the breakdown (catabolism) and building (anabolism) of molecules in the body. Enzymes are proteins that catalyze metabolic reactions and are made up of amino acids folded into shapes with active sites. Enzymes require cofactors like vitamins and minerals to function as holoenzymes in reactions. Enzyme activity is affected by factors like temperature, substrate concentration, and pH - with each enzyme having optimal conditions for maximum reaction rates.
ESA/ACT Science Coffee: Diego Blas - Gravitational wave detection with orbita...
ESA/ACT Science Coffee: Diego Blas - Gravitational wave detection with orbita...Advanced-Concepts-Team
Presentation in the Science Coffee of the Advanced Concepts Team of the European Space Agency on the 07.06.2024.
Speaker: Diego Blas (IFAE/ICREA)
Title: Gravitational wave detection with orbital motion of Moon and artificial
Abstract:
In this talk I will describe some recent ideas to find gravitational waves from supermassive black holes or of primordial origin by studying their secular effect on the orbital motion of the Moon or satellites that are laser ranged.Immersive Learning That Works: Research Grounding and Paths Forward
We will metaverse into the essence of immersive learning, into its three dimensions and conceptual models. This approach encompasses elements from teaching methodologies to social involvement, through organizational concerns and technologies. Challenging the perception of learning as knowledge transfer, we introduce a 'Uses, Practices & Strategies' model operationalized by the 'Immersive Learning Brain' and ‘Immersion Cube’ frameworks. This approach offers a comprehensive guide through the intricacies of immersive educational experiences and spotlighting research frontiers, along the immersion dimensions of system, narrative, and agency. Our discourse extends to stakeholders beyond the academic sphere, addressing the interests of technologists, instructional designers, and policymakers. We span various contexts, from formal education to organizational transformation to the new horizon of an AI-pervasive society. This keynote aims to unite the iLRN community in a collaborative journey towards a future where immersive learning research and practice coalesce, paving the way for innovative educational research and practice landscapes.
More Related Content
Similar to Enzyme ppt
Biochemistry lecture notes enzymes
Enzymes are protein catalysts that greatly increase the rates of biochemical reactions. They achieve this by lowering the activation energy of reactions. Enzymes are highly specific and only catalyze one or a small number of reaction types. The enzyme binds to its substrate at its active site, and uses functional groups to facilitate the reaction, ultimately releasing the product. Many factors can influence an enzyme's activity level, including its concentration, the substrate concentration, temperature, pH, and the presence of inhibitors.
Enzymes.pptx
An enzyme is a biological catalyst and is almost always a protein. It speeds up the rate of a specific chemical reaction in the cell. The enzyme is not destroyed during the reaction and is used over and over.
5. Biochemistry of enzymes edited 2024.pptx
Enzymes are biological catalysts that regulate biochemical reactions. This document discusses the composition, mechanisms, and factors that influence enzyme activity. It describes how enzymes lower activation energy and use an active site to bind substrates and stabilize reaction intermediates. The Michaelis-Menten equation models how reaction rate varies with substrate concentration in relation to parameters like Vmax and Km. Environmental factors like temperature and pH can impact enzyme activity.
Enzymes
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.
Enzymes
Enzymes are protein catalysts that speed up biochemical reactions without being consumed. They work by lowering the activation energy of reactions. Enzymes have specific active sites that bind substrates and induce a conformational change through induced fit. This allows the enzyme to accelerate the reaction and produce products. The rate of enzyme reactions can be affected by environmental factors like temperature, pH, and concentrations of enzymes and substrates.
Catalysis lecture 4
This document provides an overview of enzyme catalysis. It discusses that enzymes are protein molecules that act as catalysts to speed up organic reactions in living cells. Enzymes have high selectivity and efficiency, with one molecule able to catalyze millions of reactions per minute. The rate of enzyme-catalyzed reactions is maximum at the optimum temperature and pH. Enzymes can be inhibited or destroyed by other substances but their activity is enhanced by activators or coenzymes. The mechanism of enzyme catalysis involves the substrate binding to the active site of the enzyme in a lock-and-key fashion to form a complex that then decomposes to release the products.
Overview of enzyme
This slideshow is about overview of enzyme. It describes important properties of enzymes, classification, functions and mode of action.
Enzymes Topic - Power Point Presentation
Enzymes are proteins that act as biological catalysts to speed up chemical reactions in the body without being consumed. They achieve this by lowering the activation energy of reactions. Enzymes are highly specific and only catalyze particular substrate molecules. They function by inducing a temporary change in shape at their active site to accommodate the substrate before releasing the products. Enzyme activity can be affected by environmental conditions like temperature and pH, as well as cofactors and inhibitors that influence the enzyme's structure and ability to bind substrates.
Enzymes (An Introductory Approach)
1. Enzymes are biological catalysts that speed up reactions by lowering activation energy.
2. Enzymes have specific active sites that substrates bind to, and can break down or join substrates.
3. Enzymes are proteins but some are RNA molecules called ribozymes, and their activity is affected by temperature, pH, substrate concentration and other factors.
Enzyme structure and Mechanism of Action
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.
CHAPTER 6.pptx
- Enzymes are protein biocatalysts that increase the rate of chemical reactions without being consumed. They are specific in their action and composed of apoenzyme and coenzyme.
- The active site of an enzyme binds specifically to substrates and contains residues that help hold the substrate. Changes to the active site shape affect enzyme function.
- Factors like temperature, pH, substrate/product concentration, and presence of activators or inhibitors can regulate an enzyme's activity rate. Studying an enzyme's kinetics reveals its catalytic mechanism.
- Regulation allows cells to control metabolic pathways by modulating enzyme activity. Competitive inhibitors bind the active site while non-competitive inhibitors cause conformational changes. I
Enzymes.pptx
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.
enzyme cmlt 2nd year.pptx
1. Enzymes are protein catalysts that regulate chemical reactions in living cells without undergoing any permanent changes themselves.
2. They function by binding to a specific substrate and lowering the activation energy of a reaction, greatly increasing the reaction rate.
3. The active site of an enzyme is where substrate binding and catalysis occur. Factors like temperature, pH, and inhibitor binding can impact enzyme activity levels.
Enzyme ppt by yograj
Enzymes are proteins that act as catalysts to accelerate chemical reactions without being permanently changed themselves. They are specific to the substrates they catalyze and contain an active site, a restricted region that binds to the substrate. When the substrate binds, an induced fit may occur where the enzyme's shape changes to better accommodate the substrate. Enzyme activity can be affected by environmental conditions like temperature and pH, cofactors and coenzymes that are required for activity, and enzyme inhibitors that compete with the substrate for the active site or bind elsewhere and alter the enzyme's shape.
ENZYMES.pptx
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.
Enzyme part A
Most enzymes are Proteins (tertiary and quaternary structures)
Act as Catalyst to accelerates a reaction
Not permanently changed in the process
Enzymes
1. Enzymes are protein catalysts that speed up chemical reactions without being consumed in the process. They achieve specificity by inducing conformational changes that tightly bind substrates in the active site.
2. The induced fit model proposes that weak initial interactions between the enzyme and substrate induce structural changes that strengthen binding.
3. Key factors that affect enzyme activity include temperature, pH, enzyme concentration, and substrate concentration. Activity is optimized within narrow ranges for each factor.
Unit 4: Plasma Enzyme tests in diagnosis
This document provides an overview of plasma enzyme tests and their use in diagnosis. It discusses factors that affect enzyme reaction rates, the clinical usefulness of measuring serum enzyme levels, and specific enzymes that are useful in diagnosing various disorders, including cardiac, hepatic, bone, muscle, malignancies and acute pancreatitis. The document also covers enzyme kinetics, the advantages and disadvantages of enzyme assays, how enzyme activity is measured and calculated, and the classification of different enzyme types.
Enzymes-.pdf
Metabolism involves the breakdown (catabolism) and building (anabolism) of molecules in the body. Enzymes are proteins that catalyze metabolic reactions and are made up of amino acids folded into shapes with active sites. Enzymes require cofactors like vitamins and minerals to function as holoenzymes in reactions. Enzyme activity is affected by factors like temperature, substrate concentration, and pH - with each enzyme having optimal conditions for maximum reaction rates.
Similar to Enzyme ppt (20)
Recently uploaded
ESA/ACT Science Coffee: Diego Blas - Gravitational wave detection with orbita...
ESA/ACT Science Coffee: Diego Blas - Gravitational wave detection with orbita...Advanced-Concepts-Team
Presentation in the Science Coffee of the Advanced Concepts Team of the European Space Agency on the 07.06.2024.
Speaker: Diego Blas (IFAE/ICREA)
Title: Gravitational wave detection with orbital motion of Moon and artificial
Abstract:
In this talk I will describe some recent ideas to find gravitational waves from supermassive black holes or of primordial origin by studying their secular effect on the orbital motion of the Moon or satellites that are laser ranged.Immersive Learning That Works: Research Grounding and Paths Forward
We will metaverse into the essence of immersive learning, into its three dimensions and conceptual models. This approach encompasses elements from teaching methodologies to social involvement, through organizational concerns and technologies. Challenging the perception of learning as knowledge transfer, we introduce a 'Uses, Practices & Strategies' model operationalized by the 'Immersive Learning Brain' and ‘Immersion Cube’ frameworks. This approach offers a comprehensive guide through the intricacies of immersive educational experiences and spotlighting research frontiers, along the immersion dimensions of system, narrative, and agency. Our discourse extends to stakeholders beyond the academic sphere, addressing the interests of technologists, instructional designers, and policymakers. We span various contexts, from formal education to organizational transformation to the new horizon of an AI-pervasive society. This keynote aims to unite the iLRN community in a collaborative journey towards a future where immersive learning research and practice coalesce, paving the way for innovative educational research and practice landscapes.
MICROBIAL INTERACTION PPT/ MICROBIAL INTERACTION AND THEIR TYPES // PLANT MIC...
MICROBIAL INTERACTION PPT/ MICROBIAL INTERACTION AND THEIR TYPES // PLANT MIC...ABHISHEK SONI NIMT INSTITUTE OF MEDICAL AND PARAMEDCIAL SCIENCES , GOVT PG COLLEGE NOIDA
Microbial interaction
Microorganisms interacts with each other and can be physically associated with another organisms in a variety of ways.
One organism can be located on the surface of another organism as an ectobiont or located within another organism as endobiont.
Microbial interaction may be positive such as mutualism, proto-cooperation, commensalism or may be negative such as parasitism, predation or competition
Types of microbial interaction
Positive interaction: mutualism, proto-cooperation, commensalism
Negative interaction: Ammensalism (antagonism), parasitism, predation, competition
I. Mutualism:
It is defined as the relationship in which each organism in interaction gets benefits from association. It is an obligatory relationship in which mutualist and host are metabolically dependent on each other.
Mutualistic relationship is very specific where one member of association cannot be replaced by another species.
Mutualism require close physical contact between interacting organisms.
Relationship of mutualism allows organisms to exist in habitat that could not occupied by either species alone.
Mutualistic relationship between organisms allows them to act as a single organism.
Examples of mutualism:
i. Lichens:
Lichens are excellent example of mutualism.
They are the association of specific fungi and certain genus of algae. In lichen, fungal partner is called mycobiont and algal partner is called
II. Syntrophism:
It is an association in which the growth of one organism either depends on or improved by the substrate provided by another organism.
In syntrophism both organism in association gets benefits.
Compound A
Utilized by population 1
Compound B
Utilized by population 2
Compound C
utilized by both Population 1+2
Products
In this theoretical example of syntrophism, population 1 is able to utilize and metabolize compound A, forming compound B but cannot metabolize beyond compound B without co-operation of population 2. Population 2is unable to utilize compound A but it can metabolize compound B forming compound C. Then both population 1 and 2 are able to carry out metabolic reaction which leads to formation of end product that neither population could produce alone.
Examples of syntrophism:
i. Methanogenic ecosystem in sludge digester
Methane produced by methanogenic bacteria depends upon interspecies hydrogen transfer by other fermentative bacteria.
Anaerobic fermentative bacteria generate CO2 and H2 utilizing carbohydrates which is then utilized by methanogenic bacteria (Methanobacter) to produce methane.
ii. Lactobacillus arobinosus and Enterococcus faecalis:
In the minimal media, Lactobacillus arobinosus and Enterococcus faecalis are able to grow together but not alone.
The synergistic relationship between E. faecalis and L. arobinosus occurs in which E. faecalis require folic acid
Sustainable Land Management - Climate Smart Agriculture
Sustainable Land Management - Climate Smart AgricultureInternational Food Policy Research Institute- South Asia Office
PPT on Sustainable Land Management presented at the three-day 'Training and Validation Workshop on Modules of Climate Smart Agriculture (CSA) Technologies in South Asia' workshop on April 22, 2024.
JAMES WEBB STUDY THE MASSIVE BLACK HOLE SEEDS
The pathway(s) to seeding the massive black holes (MBHs) that exist at the heart of galaxies in the present and distant Universe remains an unsolved problem. Here we categorise, describe and quantitatively discuss the formation pathways of both light and heavy seeds. We emphasise that the most recent computational models suggest that rather than a bimodal-like mass spectrum between light and heavy seeds with light at one end and heavy at the other that instead a continuum exists. Light seeds being more ubiquitous and the heavier seeds becoming less and less abundant due the rarer environmental conditions required for their formation. We therefore examine the different mechanisms that give rise to different seed mass spectrums. We show how and why the mechanisms that produce the heaviest seeds are also among the rarest events in the Universe and are hence extremely unlikely to be the seeds for the vast majority of the MBH population. We quantify, within the limits of the current large uncertainties in the seeding processes, the expected number densities of the seed mass spectrum. We argue that light seeds must be at least 103 to 105 times more numerous than heavy seeds to explain the MBH population as a whole. Based on our current understanding of the seed population this makes heavy seeds (Mseed > 103 M⊙) a significantly more likely pathway given that heavy seeds have an abundance pattern than is close to and likely in excess of 10−4 compared to light seeds. Finally, we examine the current state-of-the-art in numerical calculations and recent observations and plot a path forward for near-future advances in both domains.
fermented food science of sauerkraut.pptx
This ppt contains the production of a fermented food name - sauerkraut
Pests of Storage_Identification_Dr.UPR.pdf
InIndia-post-harvestlosses-unscientificstorage,insects,rodents,micro-organismsetc.,accountforabout10percentoftotalfoodgrains
Graininfestation
Directdamage
Indirectly
•theexuviae,skin,deadinsects
•theirexcretawhichmakefoodunfitforhumanconsumption
About600speciesofinsectshavebeenassociatedwithstoredgrainproducts
100speciesofinsectpestsofstoredproductscauseeconomiclosses
SDSS1335+0728: The awakening of a ∼ 106M⊙ black hole⋆
Context. The early-type galaxy SDSS J133519.91+072807.4 (hereafter SDSS1335+0728), which had exhibited no prior optical variations during the preceding two decades, began showing significant nuclear variability in the Zwicky Transient Facility (ZTF) alert stream from December 2019 (as ZTF19acnskyy). This variability behaviour, coupled with the host-galaxy properties, suggests that SDSS1335+0728 hosts a ∼ 106M⊙ black hole (BH) that is currently in the process of ‘turning on’. Aims. We present a multi-wavelength photometric analysis and spectroscopic follow-up performed with the aim of better understanding the origin of the nuclear variations detected in SDSS1335+0728. Methods. We used archival photometry (from WISE, 2MASS, SDSS, GALEX, eROSITA) and spectroscopic data (from SDSS and LAMOST) to study the state of SDSS1335+0728 prior to December 2019, and new observations from Swift, SOAR/Goodman, VLT/X-shooter, and Keck/LRIS taken after its turn-on to characterise its current state. We analysed the variability of SDSS1335+0728 in the X-ray/UV/optical/mid-infrared range, modelled its spectral energy distribution prior to and after December 2019, and studied the evolution of its UV/optical spectra. Results. From our multi-wavelength photometric analysis, we find that: (a) since 2021, the UV flux (from Swift/UVOT observations) is four times brighter than the flux reported by GALEX in 2004; (b) since June 2022, the mid-infrared flux has risen more than two times, and the W1−W2 WISE colour has become redder; and (c) since February 2024, the source has begun showing X-ray emission. From our spectroscopic follow-up, we see that (i) the narrow emission line ratios are now consistent with a more energetic ionising continuum; (ii) broad emission lines are not detected; and (iii) the [OIII] line increased its flux ∼ 3.6 years after the first ZTF alert, which implies a relatively compact narrow-line-emitting region. Conclusions. We conclude that the variations observed in SDSS1335+0728 could be either explained by a ∼ 106M⊙ AGN that is just turning on or by an exotic tidal disruption event (TDE). If the former is true, SDSS1335+0728 is one of the strongest cases of an AGNobserved in the process of activating. If the latter were found to be the case, it would correspond to the longest and faintest TDE ever observed (or another class of still unknown nuclear transient). Future observations of SDSS1335+0728 are crucial to further understand its behaviour. Key words. galaxies: active– accretion, accretion discs– galaxies: individual: SDSS J133519.91+072807.4
Compexometric titration/Chelatorphy titration/chelating titration
Classification
Metal ion ion indicators
Masking and demasking reagents
Estimation of Magnisium sulphate
Calcium gluconate
Complexometric Titration/ chelatometry titration/chelating titration, introduction, Types-
1.Direct Titration
2.Back Titration
3.Replacement Titration
4.Indirect Titration
Masking agent, Demasking agents
formation of complex
comparition between masking and demasking agents,
Indicators/Metal ion indicators/ Metallochromic indicators/pM indicators,
Visual Technique,PM indicators (metallochromic), Indicators of pH, Redox Indicators
Instrumental Techniques-Photometry
Potentiometry
Miscellaneous methods.
Complex titration with EDTA.
Farming systems analysis: what have we learnt?.pptx
Presentation given at the official farewell of Prof Ken Gillet at Wageningen on 13 June 2024
Alternate Wetting and Drying - Climate Smart Agriculture
Alternate Wetting and Drying - Climate Smart AgricultureInternational Food Policy Research Institute- South Asia Office
PPT on Alternate Wetting and Drying presented at the three-day 'Training and Validation Workshop on Modules of Climate Smart Agriculture (CSA) Technologies in South Asia' workshop on April 22, 2024. Direct Seeded Rice - Climate Smart Agriculture
Direct Seeded Rice - Climate Smart AgricultureInternational Food Policy Research Institute- South Asia Office
PPT on Direct Seeded Rice presented at the three-day 'Training and Validation Workshop on Modules of Climate Smart Agriculture (CSA) Technologies in South Asia' workshop on April 22, 2024.
CLASS 12th CHEMISTRY SOLID STATE ppt (Animated)
Description:
Dive into the fascinating realm of solid-state physics with our meticulously crafted online PowerPoint presentation. This immersive educational resource offers a comprehensive exploration of the fundamental concepts, theories, and applications within the realm of solid-state physics.
From crystalline structures to semiconductor devices, this presentation delves into the intricate principles governing the behavior of solids, providing clear explanations and illustrative examples to enhance understanding. Whether you're a student delving into the subject for the first time or a seasoned researcher seeking to deepen your knowledge, our presentation offers valuable insights and in-depth analyses to cater to various levels of expertise.
Key topics covered include:
Crystal Structures: Unravel the mysteries of crystalline arrangements and their significance in determining material properties.
Band Theory: Explore the electronic band structure of solids and understand how it influences their conductive properties.
Semiconductor Physics: Delve into the behavior of semiconductors, including doping, carrier transport, and device applications.
Magnetic Properties: Investigate the magnetic behavior of solids, including ferromagnetism, antiferromagnetism, and ferrimagnetism.
Optical Properties: Examine the interaction of light with solids, including absorption, reflection, and transmission phenomena.
With visually engaging slides, informative content, and interactive elements, our online PowerPoint presentation serves as a valuable resource for students, educators, and enthusiasts alike, facilitating a deeper understanding of the captivating world of solid-state physics. Explore the intricacies of solid-state materials and unlock the secrets behind their remarkable properties with our comprehensive presentation.
Mechanisms and Applications of Antiviral Neutralizing Antibodies - Creative B...
Neutralizing antibodies, pivotal in immune defense, specifically bind and inhibit viral pathogens, thereby playing a crucial role in protecting against and mitigating infectious diseases. In this slide, we will introduce what antibodies and neutralizing antibodies are, the production and regulation of neutralizing antibodies, their mechanisms of action, classification and applications, as well as the challenges they face.
BIRDS DIVERSITY OF SOOTEA BISWANATH ASSAM.ppt.pptx
Ahota Beel, nestled in Sootea Biswanath Assam , is celebrated for its extraordinary diversity of bird species. This wetland sanctuary supports a myriad of avian residents and migrants alike. Visitors can admire the elegant flights of migratory species such as the Northern Pintail and Eurasian Wigeon, alongside resident birds including the Asian Openbill and Pheasant-tailed Jacana. With its tranquil scenery and varied habitats, Ahota Beel offers a perfect haven for birdwatchers to appreciate and study the vibrant birdlife that thrives in this natural refuge.
The cost of acquiring information by natural selection
This is a short talk that I gave at the Banff International Research Station workshop on Modeling and Theory in Population Biology. The idea is to try to understand how the burden of natural selection relates to the amount of information that selection puts into the genome.
It's based on the first part of this research paper:
The cost of information acquisition by natural selection
Ryan Seamus McGee, Olivia Kosterlitz, Artem Kaznatcheev, Benjamin Kerr, Carl T. Bergstrom
bioRxiv 2022.07.02.498577; doi: https://doi.org/10.1101/2022.07.02.498577
Recently uploaded (20)
ESA/ACT Science Coffee: Diego Blas - Gravitational wave detection with orbita...
ESA/ACT Science Coffee: Diego Blas - Gravitational wave detection with orbita...
Immersive Learning That Works: Research Grounding and Paths Forward
Immersive Learning That Works: Research Grounding and Paths Forward
MICROBIAL INTERACTION PPT/ MICROBIAL INTERACTION AND THEIR TYPES // PLANT MIC...
MICROBIAL INTERACTION PPT/ MICROBIAL INTERACTION AND THEIR TYPES // PLANT MIC...
Sustainable Land Management - Climate Smart Agriculture
Sustainable Land Management - Climate Smart Agriculture
SDSS1335+0728: The awakening of a ∼ 106M⊙ black hole⋆
SDSS1335+0728: The awakening of a ∼ 106M⊙ black hole⋆
Compexometric titration/Chelatorphy titration/chelating titration
Compexometric titration/Chelatorphy titration/chelating titration
Farming systems analysis: what have we learnt?.pptx
Farming systems analysis: what have we learnt?.pptx
Alternate Wetting and Drying - Climate Smart Agriculture
Alternate Wetting and Drying - Climate Smart Agriculture
Juaristi, Jon. - El canon espanol. El legado de la cultura española a la civi...
Juaristi, Jon. - El canon espanol. El legado de la cultura española a la civi...
Mechanisms and Applications of Antiviral Neutralizing Antibodies - Creative B...
Mechanisms and Applications of Antiviral Neutralizing Antibodies - Creative B...
Introduction_Ch_01_Biotech Biotechnology course .pptx
Introduction_Ch_01_Biotech Biotechnology course .pptx
BIRDS DIVERSITY OF SOOTEA BISWANATH ASSAM.ppt.pptx
BIRDS DIVERSITY OF SOOTEA BISWANATH ASSAM.ppt.pptx
The cost of acquiring information by natural selection
The cost of acquiring information by natural selection
Enzyme ppt
- 2. 2 What Are Enzymes?What Are Enzymes? • Most enzymes are ProteinsProteins ((tertiary and quaternary structures) • Act as CatalystCatalyst to accelerates a reaction • Not permanentlyNot permanently changed in the process
- 3. 3 EnzymesEnzymes • Are specific for what they will catalyzecatalyze • Are ReusableReusable • End in –asease -Sucrase-Sucrase -Lactase-Lactase -Maltase-Maltase
- 4. 4 How do enzymes Work?How do enzymes Work? Enzymes work by weakeningweakening bondsbonds whichwhich lowerslowers activationactivation energyenergy
- 5. 5 EnzymesEnzymes Free Energy Progress of the reaction Reactants Products Free energy of activationFree energy of activation Without Enzyme With Enzyme
- 6. 6
- 7. 7 Enzyme-Substrate ComplexEnzyme-Substrate Complex The substancesubstance (reactant) an enzymeenzyme acts on is the substratesubstrate EnzymeSubstrate Joins
- 8. 8 Active SiteActive Site • A restricted regionrestricted region of an enzymeenzyme molecule which bindsbinds to the substratesubstrate. Enzyme Substrate Active Site
- 9. 9 Induced FitInduced Fit • A change in the shapeshape of an enzyme’s active site • InducedInduced by the substrate
- 10. 10 Induced FitInduced Fit • A changechange in the configurationconfiguration of an enzyme’s activeenzyme’s active sitesite (H+ and ionic bonds are involved). • InducedInduced by the substratesubstrate.. Enzyme Active Site substrate induced fit
- 11. 11 What Affects Enzyme Activity?What Affects Enzyme Activity? • Three factors:Three factors: 1.1. Environmental ConditionsEnvironmental Conditions 2.2. Cofactors and CoenzymesCofactors and Coenzymes 3.3. Enzyme InhibitorsEnzyme Inhibitors
- 12. 12 1. Environmental Conditions1. Environmental Conditions 1. Extreme1. Extreme TemperatureTemperature are the mostare the most dangerousdangerous -- high tempshigh temps may denature (unfold)denature (unfold) the enzyme.enzyme. 2.2. pHpH (most like 6 - 8 pH near(most like 6 - 8 pH near neutral)neutral) 3.3. Ionic concentrationIonic concentration (salt ions)(salt ions)
- 13. 13 2. Cofactors and Coenzymes2. Cofactors and Coenzymes • Inorganic substancesInorganic substances (zinc, iron)(zinc, iron) and vitaminsvitamins (respectively) are sometimes need for proper enzymatic activityenzymatic activity. • Example:Example: IronIron must be present in the quaternaryquaternary structurestructure -- hemoglobinhemoglobin in order for it to pickpick up oxygen.up oxygen.
- 14. 14 Two examples of EnzymeTwo examples of Enzyme InhibitorsInhibitors a.a. Competitive inhibitorsCompetitive inhibitors:: are chemicals that resembleresemble an enzyme’s normal substrateenzyme’s normal substrate and competecompete with it for the activeactive sitesite. Enzyme Competitive inhibitor Substrate
- 15. 15 InhibitorsInhibitors b.b. Noncompetitive inhibitorsNoncompetitive inhibitors:: Inhibitors that do not enter thedo not enter the active siteactive site, but bind tobind to another partanother part of the enzymeenzyme causing the enzymeenzyme to change its shapechange its shape, which in turn alters the active sitealters the active site. Enzyme active site altered Noncompetitive Inhibitor Substrate
- 16. 16