3 Enzymes.pptx Enzymes, it's types and functionAbdulGhayur1
Enzymes are biological molecules that catalyze chemical reactions and increase their rates. They are selective for specific substrates and only catalyze a few reactions. Enzymes work by lowering activation energy and can accelerate reactions by millions of times. They are not consumed in reactions and do not alter equilibrium. Enzyme activity is affected by factors like temperature, pH, inhibitors, and more. The lock and key and induced fit models describe how enzymes and substrates interact specifically in the active site. Cofactors like metal ions and coenzymes are required for some enzyme activity. Enzymes perform critical functions in cell signaling, movement, and metabolism and are targets of drugs and involved in diseases.
Enzymes are protein catalysts that speed up biochemical reactions. They work by lowering the activation energy of reactions through their specific three-dimensional structure. This structure complements that of substrates, facilitating the formation of enzyme-substrate complexes. Factors like temperature, pH, enzyme and substrate concentrations can affect reaction rates by impacting enzyme shapes and complex formation. Inhibitors also regulate enzymes by competing for or altering their active sites.
This document discusses allosteric regulation of enzymes. It defines allosteric regulation as the regulation of an enzyme by binding an effector molecule at a site other than the active site. Effectors that increase enzyme activity are called positive allosteric effectors, while those that decrease activity are negative effectors. Allosteric enzymes can exist in more or less active conformations depending on the binding of effectors. Feedback inhibition is also described, where the end product of a pathway inhibits an earlier regulatory enzyme. Allosteric enzymes do not always follow Michaelis-Menten kinetics and can display sigmoidal substrate binding curves.
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.
This ppt describes the overview of enzyme regulation and Allosterism. Presented since October 23,2017GC at Addis Ababa University, School of Medicine, Department of medical biochemistry.
Enzymes are biological catalysts. They are involved in all metabolic reactions inside the body. But we know that for the normal working of a body we do not require every metabolism to take place at a particular time. Thus, there must be a regulative mechanism for the enzymes.
How is these enzymes regulated? Let's explore molecular details and the biochemistry behind it
- 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
3 Enzymes.pptx Enzymes, it's types and functionAbdulGhayur1
Enzymes are biological molecules that catalyze chemical reactions and increase their rates. They are selective for specific substrates and only catalyze a few reactions. Enzymes work by lowering activation energy and can accelerate reactions by millions of times. They are not consumed in reactions and do not alter equilibrium. Enzyme activity is affected by factors like temperature, pH, inhibitors, and more. The lock and key and induced fit models describe how enzymes and substrates interact specifically in the active site. Cofactors like metal ions and coenzymes are required for some enzyme activity. Enzymes perform critical functions in cell signaling, movement, and metabolism and are targets of drugs and involved in diseases.
Enzymes are protein catalysts that speed up biochemical reactions. They work by lowering the activation energy of reactions through their specific three-dimensional structure. This structure complements that of substrates, facilitating the formation of enzyme-substrate complexes. Factors like temperature, pH, enzyme and substrate concentrations can affect reaction rates by impacting enzyme shapes and complex formation. Inhibitors also regulate enzymes by competing for or altering their active sites.
This document discusses allosteric regulation of enzymes. It defines allosteric regulation as the regulation of an enzyme by binding an effector molecule at a site other than the active site. Effectors that increase enzyme activity are called positive allosteric effectors, while those that decrease activity are negative effectors. Allosteric enzymes can exist in more or less active conformations depending on the binding of effectors. Feedback inhibition is also described, where the end product of a pathway inhibits an earlier regulatory enzyme. Allosteric enzymes do not always follow Michaelis-Menten kinetics and can display sigmoidal substrate binding curves.
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.
This ppt describes the overview of enzyme regulation and Allosterism. Presented since October 23,2017GC at Addis Ababa University, School of Medicine, Department of medical biochemistry.
Enzymes are biological catalysts. They are involved in all metabolic reactions inside the body. But we know that for the normal working of a body we do not require every metabolism to take place at a particular time. Thus, there must be a regulative mechanism for the enzymes.
How is these enzymes regulated? Let's explore molecular details and the biochemistry behind it
- 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 are protein catalysts that support biochemical reactions in cells and tissues. They have active sites that substrates must fit into in order to undergo reaction. Enzymes are classified based on their reactions and components. Some require coenzymes like B vitamins or metal ions. Enzyme activity is affected by factors like substrate, enzyme, and product concentration; temperature; pH; and presence of activators or inhibitors. Clinical enzyme tests can indicate tissue damage, such as elevated liver enzymes in hepatitis or muscle enzymes in infarction. Together with other markers, enzymes help diagnose and monitor various conditions.
Enzymes are biological catalysts that speed up chemical reactions without being consumed. They are typically proteins that act by lowering the activation energy of reactions. Enzymes achieve a high degree of reaction specificity by possessing an active site that only certain substrates can fit into. The document provides an overview of enzymes, including how they are named, regulated, and can be competitive or noncompetitively inhibited. Key features like optimal pH and temperature ranges are also summarized.
This document provides an overview of enzymes and enzyme kinetics taught in the Principles of Biochemistry course (HFB324) by Dr. Siham Gritly. It defines key enzyme terms and concepts, describes enzyme classification systems, the components and localization of enzymes in the body, and models of enzyme catalysis including active sites and enzyme-substrate binding. It also explains Michaelis-Menten kinetics and how various factors influence the velocity of enzyme reactions such as substrate concentration, temperature, and inhibitors.
This document provides information about enzymes. It defines enzymes as proteins that act as catalysts in biochemical reactions. Enzymes have cofactors like coenzymes and metal ions that help facilitate reactions. Enzymes are named based on their substrates and the type of reactions they catalyze. The document discusses different types of enzyme inhibition, including competitive, non-competitive, and irreversible inhibition. It also covers enzyme regulation mechanisms such as allosteric regulation, covalent modification, induction and repression, compartmentalization, and isoenzymes. The key roles of regulation are to efficiently use substrates and control metabolic pathways.
Enzymes are biological catalysts that are proteins which accelerate biochemical reactions in living organisms. They were discovered in yeast and are highly specific. Enzymes differ from chemical catalysts in having higher reaction rates under milder conditions and greater substrate specificity. The first enzyme was isolated from jack beans in 1926. Most enzymes are proteins, but some are RNA molecules. Enzymes can exist as single or multiple polypeptide chains and require cofactors like metal ions for activity. The active site is the region where substrates bind for catalysis. Many factors like temperature, pH, and product concentration influence an enzyme's activity rate.
Enzymes are protein catalysts that accelerate biochemical reactions without being consumed. They achieve this by lowering the activation energy of reactions and stabilizing transition states. Enzymes require cofactors like metal ions or organic coenzymes to function. The active site of an enzyme binds specifically to substrates to catalyze reactions. Many factors influence enzyme activity, such as temperature, pH, substrate and product concentration.
Molecular biology in department life scienceisamshafal
This document discusses enzyme inhibitors and how they regulate metabolism. It covers several types of enzyme inhibitors - competitive inhibitors that compete with substrates for the catalytic site, noncompetitive inhibitors that bind elsewhere and alter the enzyme's shape, and allosteric inhibitors that bind to regulatory sites and cause conformational changes. The document also discusses how cells regulate metabolic pathways through controlling enzyme concentration, compartmentalization of enzymes and substrates, and feedback inhibition where end products inhibit early enzymes in the pathway. Enzymes are also involved in other cellular functions like transport, movement, replication and chemotaxis through receptor proteins, signal transduction pathways and methyl-accepting chemotaxis proteins.
This document discusses reproductive hormones and their functions. It begins by listing the major endocrine glands and the hormones they produce, including the hypothalamus, pituitary gland, adrenal glands, thyroid gland, pancreas, ovaries, and testes. It then discusses steroid hormones in more detail, describing their basic structures. The rest of the document focuses on estrogen, including its synthesis in the ovaries, metabolism, mechanisms of action, effects on various body systems, common pharmaceutical preparations, clinical uses, and potential side effects.
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.
This document provides an overview of drug metabolism. It discusses that drugs must undergo metabolism to become water soluble enough to be excreted from the body. Metabolism occurs in two phases - phase I involves reactions like oxidation and phase II involves conjugation. Key enzymes like cytochrome P450 catalyze phase I reactions in the liver. Factors like age, sex, disease state, environment, and genetic variation can impact a person's drug metabolism and influence how drugs are processed in their body. Understanding metabolism is important for predicting drug interactions and individualizing drug therapy.
Unit 4: Plasma Enzyme tests in diagnosis DrElhamSharif
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.
1. Enzyme activity can be regulated through several mechanisms including allosteric regulation, feedback inhibition, proenzymes, and protein modification.
2. Allosteric enzymes have effector molecules that bind and induce a conformational change that increases or decreases enzyme activity. Feedback inhibition occurs when a metabolic end product inhibits an earlier enzyme.
3. Proenzymes are inactive precursors that are activated by proteolytic cleavage. Protein modification like phosphorylation can also regulate enzymes by changing their structure.
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.
This document discusses enzymology and the key properties of enzymes. It defines enzymes as specialized proteins that act as catalysts and mediate chemical reactions in the body. Enzymes are important in clinical settings, with many enzyme assays accounting for 40-50% of laboratory work. The document outlines that enzymes are protein catalysts synthesized by living systems, and have properties like being catalytic, substrate-specific, and able to function under moderate pH and temperature ranges. It also describes characteristics like active sites, compartmentalization in cells, and the formation of enzyme-substrate complexes during catalysis.
This document provides information on enzymes. It begins by defining enzymes as soluble, colloidal organic catalysts formed by living cells that are specific, protein in nature, and inactive at 0°C. It notes that all enzymes are proteins and that activity is lost through denaturation or dissociation. The document discusses enzymes as proteins that often require cofactors. It provides details on different types of enzymes based on their structure, location, and method of secretion. The rest of the document covers enzyme nomenclature, classification, specificity, and mechanisms of action. It discusses factors that affect enzyme activity such as temperature, pH, product concentration, and more.
This document summarizes key concepts about enzymes including:
1) Enzymes work as catalysts to lower the activation energy of biochemical reactions and increase reaction rates. They specifically bind to substrates in their active sites.
2) Environmental factors like temperature and pH can impact enzyme activity by causing enzyme denaturation at extreme levels.
3) Enzyme activity is regulated by various mechanisms including allosteric regulation, covalent modification through phosphorylation, and proteolytic activation of zymogens to active enzymes.
Enzymes are protein catalysts that support biochemical reactions in cells and tissues. They have active sites that substrates must fit into in order to undergo reaction. Enzymes are classified based on their reactions and components. Some require coenzymes like B vitamins or metal ions. Enzyme activity is affected by factors like substrate, enzyme, and product concentration; temperature; pH; and presence of activators or inhibitors. Clinical enzyme tests can indicate tissue damage, such as elevated liver enzymes in hepatitis or muscle enzymes in infarction. Together with other markers, enzymes help diagnose and monitor various conditions.
Enzymes are biological catalysts that speed up chemical reactions without being consumed. They are typically proteins that act by lowering the activation energy of reactions. Enzymes achieve a high degree of reaction specificity by possessing an active site that only certain substrates can fit into. The document provides an overview of enzymes, including how they are named, regulated, and can be competitive or noncompetitively inhibited. Key features like optimal pH and temperature ranges are also summarized.
This document provides an overview of enzymes and enzyme kinetics taught in the Principles of Biochemistry course (HFB324) by Dr. Siham Gritly. It defines key enzyme terms and concepts, describes enzyme classification systems, the components and localization of enzymes in the body, and models of enzyme catalysis including active sites and enzyme-substrate binding. It also explains Michaelis-Menten kinetics and how various factors influence the velocity of enzyme reactions such as substrate concentration, temperature, and inhibitors.
This document provides information about enzymes. It defines enzymes as proteins that act as catalysts in biochemical reactions. Enzymes have cofactors like coenzymes and metal ions that help facilitate reactions. Enzymes are named based on their substrates and the type of reactions they catalyze. The document discusses different types of enzyme inhibition, including competitive, non-competitive, and irreversible inhibition. It also covers enzyme regulation mechanisms such as allosteric regulation, covalent modification, induction and repression, compartmentalization, and isoenzymes. The key roles of regulation are to efficiently use substrates and control metabolic pathways.
Enzymes are biological catalysts that are proteins which accelerate biochemical reactions in living organisms. They were discovered in yeast and are highly specific. Enzymes differ from chemical catalysts in having higher reaction rates under milder conditions and greater substrate specificity. The first enzyme was isolated from jack beans in 1926. Most enzymes are proteins, but some are RNA molecules. Enzymes can exist as single or multiple polypeptide chains and require cofactors like metal ions for activity. The active site is the region where substrates bind for catalysis. Many factors like temperature, pH, and product concentration influence an enzyme's activity rate.
Enzymes are protein catalysts that accelerate biochemical reactions without being consumed. They achieve this by lowering the activation energy of reactions and stabilizing transition states. Enzymes require cofactors like metal ions or organic coenzymes to function. The active site of an enzyme binds specifically to substrates to catalyze reactions. Many factors influence enzyme activity, such as temperature, pH, substrate and product concentration.
Molecular biology in department life scienceisamshafal
This document discusses enzyme inhibitors and how they regulate metabolism. It covers several types of enzyme inhibitors - competitive inhibitors that compete with substrates for the catalytic site, noncompetitive inhibitors that bind elsewhere and alter the enzyme's shape, and allosteric inhibitors that bind to regulatory sites and cause conformational changes. The document also discusses how cells regulate metabolic pathways through controlling enzyme concentration, compartmentalization of enzymes and substrates, and feedback inhibition where end products inhibit early enzymes in the pathway. Enzymes are also involved in other cellular functions like transport, movement, replication and chemotaxis through receptor proteins, signal transduction pathways and methyl-accepting chemotaxis proteins.
This document discusses reproductive hormones and their functions. It begins by listing the major endocrine glands and the hormones they produce, including the hypothalamus, pituitary gland, adrenal glands, thyroid gland, pancreas, ovaries, and testes. It then discusses steroid hormones in more detail, describing their basic structures. The rest of the document focuses on estrogen, including its synthesis in the ovaries, metabolism, mechanisms of action, effects on various body systems, common pharmaceutical preparations, clinical uses, and potential side effects.
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.
This document provides an overview of drug metabolism. It discusses that drugs must undergo metabolism to become water soluble enough to be excreted from the body. Metabolism occurs in two phases - phase I involves reactions like oxidation and phase II involves conjugation. Key enzymes like cytochrome P450 catalyze phase I reactions in the liver. Factors like age, sex, disease state, environment, and genetic variation can impact a person's drug metabolism and influence how drugs are processed in their body. Understanding metabolism is important for predicting drug interactions and individualizing drug therapy.
Unit 4: Plasma Enzyme tests in diagnosis DrElhamSharif
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.
1. Enzyme activity can be regulated through several mechanisms including allosteric regulation, feedback inhibition, proenzymes, and protein modification.
2. Allosteric enzymes have effector molecules that bind and induce a conformational change that increases or decreases enzyme activity. Feedback inhibition occurs when a metabolic end product inhibits an earlier enzyme.
3. Proenzymes are inactive precursors that are activated by proteolytic cleavage. Protein modification like phosphorylation can also regulate enzymes by changing their structure.
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.
This document discusses enzymology and the key properties of enzymes. It defines enzymes as specialized proteins that act as catalysts and mediate chemical reactions in the body. Enzymes are important in clinical settings, with many enzyme assays accounting for 40-50% of laboratory work. The document outlines that enzymes are protein catalysts synthesized by living systems, and have properties like being catalytic, substrate-specific, and able to function under moderate pH and temperature ranges. It also describes characteristics like active sites, compartmentalization in cells, and the formation of enzyme-substrate complexes during catalysis.
This document provides information on enzymes. It begins by defining enzymes as soluble, colloidal organic catalysts formed by living cells that are specific, protein in nature, and inactive at 0°C. It notes that all enzymes are proteins and that activity is lost through denaturation or dissociation. The document discusses enzymes as proteins that often require cofactors. It provides details on different types of enzymes based on their structure, location, and method of secretion. The rest of the document covers enzyme nomenclature, classification, specificity, and mechanisms of action. It discusses factors that affect enzyme activity such as temperature, pH, product concentration, and more.
This document summarizes key concepts about enzymes including:
1) Enzymes work as catalysts to lower the activation energy of biochemical reactions and increase reaction rates. They specifically bind to substrates in their active sites.
2) Environmental factors like temperature and pH can impact enzyme activity by causing enzyme denaturation at extreme levels.
3) Enzyme activity is regulated by various mechanisms including allosteric regulation, covalent modification through phosphorylation, and proteolytic activation of zymogens to active enzymes.
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Cell fractionation is the process used to separate cellular components while preserving individual functions of each component.
It is a process of producing pure fractions of cell components.
The process involves two basic steps namely: disruption of the tissue and lysis of the cells, followed by centrifugation.
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This document outlines a 10-day devotion to the Holy Spirit written by Francisca Javiera del Valle. It includes opening and closing prayers for each day, as well as considerations and offerings. The introduction explains that the devotion aims to help souls seeking holiness learn the sure way through an interior life taught by a wise Teacher (the Holy Spirit). It encourages joining this school of the Holy Spirit to learn about God and oneself. The devotion is presented as a path to sanctification and possession of God through love in this life and eternity.
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2. Describe how dipoles generated by the heart produce the waveforms of the ECG
3. Describe the components of a normal electrocardiogram of a typical bipolar lead (limb II)
4. Differentiate between intervals and segments
5. Enlist some common indications for obtaining an ECG
6. Describe the flow of current around the heart during the cardiac cycle
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8. Describe the normal electrocardiograms recorded from the limb leads and explain the physiological basis of the different records that are obtained
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2. Chapter 9, Human Physiology - From Cells to Systems, Lauralee Sherwood, 9th edition
3. Chapter 29, Ganong’s Review of Medical Physiology, 26th edition
4. Electrocardiogram, StatPearls - https://www.ncbi.nlm.nih.gov/books/NBK549803/
5. ECG in Medical Practice by ABM Abdullah, 4th edition
6. Chapter 3, Cardiology Explained, https://www.ncbi.nlm.nih.gov/books/NBK2214/
7. ECG Basics, http://www.nataliescasebook.com/tag/e-c-g-basics
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2. Enzyme regulation
• Metabolism is the right integration of
varous processes. There are four
principles ways in which this is
achieved:
• Allosteric control
• Multiple forms of enzymes
• Reversible covalent modification
• Proteolytic activation
3. Isozymes
Isozymes (isoenzymes) are enzymes that differ in
sequence but catalyze the same reaction
• They usually display different kinetic behavior,
have differing substrate affinities or are regulated
in different manners
• The existence of isozymes allows the fine-
tuning of processes (e.g. metabolism) by using
different amounts of each isozyme
4. Isozymes: Lactate
Dehydrogenase
• Humans have two forms of lactate
dehydrogenase H form found in heart
• M form found in skeletal muscle
• The two forms are 75% identical and both exist
as homotetramers (H4 and M4)
• The H4 form has a higher affinity for substrate
Combinations are possible (e.g. H3M, H2M2)
allowing for different affinities
6. Isoenzyme in Heart attack
• The pattern of isoenzymes found in the
plasma serve as a means of identifying
the site of tissue damage. For example,
the plasma levels of creatine kinase (CK)
are commonly determined in the diagnosis
of myocardial infarction.
7.
8. Regulation via Covalent
Modification
• The covalent attachment of a molecule to an
enzyme (or other protein) can alter its activity
• Most such covalent modifications are reversible
e.g. phosphorylation, acetylation
• Some are irreversible e.g. attachment of a lipid
group that localizes the protein to the membrane
9. Phosphorylation
• Many proteins regulated via
phosphorylation - addition of
phosphoryl group to hydroxyl oxygen of
serine, threonine or tyrosine
• Terminal (γ) phosphoryl group from ATP
transferred to specific serine, threonine
and tyrosine residues Catalyzed by
Protein kinases
10. Phosphorylation
• Under physiological condition,
phosphorylation (and dephosphorylation)
is essentially irreversible
• - kinases and phosphatases are required
State of phosphorylation is then dependant
upon the relative activities of kinases and
phosphatases
11. Allosteric Regulation
• Allosteric modulators bind at a site other
than the active site and cause activation or
inhibition
• Can include the substrate itself
• Protein has quaternary structure
• Non-Michaelis-Menten kinetics
13. Why Sigmoid Curve.
Affinity for substrate increases with increasing substrate
concentration. A plot of product formation as a function of
substrate concentration produces a sigmoidal curve because
the binding of substrate to one active site favors the
conversion of the entire enzyme into the R state, increasing
the activity at the other active sites. Thus, the active sites
show cooperativity.
14. Allosteric Enzyme
• Allosteric enzymes have two conformations:
active (R-state) and less active (T-state)
• 1. T-state: less active, stabilized by inhibitors
• 2. R-state: more active, stabilized by substrate
and activators
• 3. Allosteric enzymes have multiple subunits.
Cooperativity results from the R to T transition of
subunits and the interaction of these subunits
(quaternary structure)
16. Sequential model
• subunits convert from R
to T individually (pos. or
neg. coop.)
• Positive cooperativity
means activity increases
as substrate
concentration increases.
• B. Negative cooperativity
means activity decreases
as substrate
concentration increases.
17.
18. Heterotropic effectors:
• The effector may be different from the substrate, in which
case the effect is said to be heterotropic. For example, the
feedback inhibition . The enzyme that converts D to E has
an allosteric site that binds the endproduct, G.
• If the concentration of G increases (for example, because it
is not used as rapidly as it is synthesized), the first
irreversible step unique to the pathway is typically inhibited.
Feedback inhibition provides the cell with a product it needs
by regulating the flow of substrate molecules through the
pathway that synthesizes that product. Heterotropic
effectors are commonly encountered, for example, the
glycolytic enzyme phosphofructokinase-1 is allosterically
inhibited by citrate, which is not a substrate for the enzyme
21. Regulation via Proteolytic
Cleavage
Many enzymes are active as soon as they are
synthesized and have folded
Others are synthesized somewhere you don’t want them
to be active - they are activated after being
transported to the appropriate place
These enzymes can be synthesized as zymogens –as
inactive precursors
• Zymogens are activated by proteolytic cleavage,
which can occur outside the cell
22. Examples of Zymogens
1. Digestive enzymes: pepsin, chymotrypsin,
trypsin, elastase, carboxypeptidase
2. Blood clotting - activated by a cascade of
proteolytic activations
3. Some hormones: insulin
4. Collagen -Collagenase - enzyme that
breaks down collagen
5. Caspases - proteolytic enzymes involved in
apoptosis (programmed cell death
23. Zymogen Active site
• Trypsinogen
• Chymotrypsinogen
• Pepsinogen
• Prothrombin
• Zymogen provides protection to the body. As the active E may
destroy body substances if activated in absence of S.e.g. if
thormbinis formed in the body, it will convert Fibrinogen to Fibrin.
This will form clot in blood causing heart attack and Stroke.
TRypsin + peptide
Enterokinas
Chymotrypsin + peptide
Pepsin + Peptide
•HCl
Thrombin + Peptide
Clotting
Factor
Trypsin