powerpoint
... E P k 2 [ ES ] Rate of dissociation of ES to E + S E S k 3 [ ES ] Rate of conversion of ES to E + P ...
... E P k 2 [ ES ] Rate of dissociation of ES to E + S E S k 3 [ ES ] Rate of conversion of ES to E + P ...
question sheet - Sackville School
... Commercial uses of enzymes Enzymes are used in industrial processes and the development of enzyme technology has resulted in the large-scale production of enzymes from microorganisms. These microbial enzymes are used in the production of paper, textiles, food and biological detergents. Pectinases ar ...
... Commercial uses of enzymes Enzymes are used in industrial processes and the development of enzyme technology has resulted in the large-scale production of enzymes from microorganisms. These microbial enzymes are used in the production of paper, textiles, food and biological detergents. Pectinases ar ...
File
... Competitive inhibitors can be overcome by increasing the substrate concentration but that is not the case with noncompetitive inhibitors With enough substrate concentration, the rate of reaction can be just as high as without an inhibitor ...
... Competitive inhibitors can be overcome by increasing the substrate concentration but that is not the case with noncompetitive inhibitors With enough substrate concentration, the rate of reaction can be just as high as without an inhibitor ...
Enzymology Part 2
... PABA is required for the synthesis of folic acid Sulphanamida is a drug that competes with PABA for the enzymes in the folic acid synthesis pathway. ...
... PABA is required for the synthesis of folic acid Sulphanamida is a drug that competes with PABA for the enzymes in the folic acid synthesis pathway. ...
HANDOUT- Enzymes! (Enzyme Reaction Rates)
... you wanted to compare the effectiveness of catalase obtained from potato with that of catalase obtained from liver. It is best to compare the reactions when the rates are constant. In the first few minutes of an enzymatic reaction such as this, the number of substrate molecules is usually so large c ...
... you wanted to compare the effectiveness of catalase obtained from potato with that of catalase obtained from liver. It is best to compare the reactions when the rates are constant. In the first few minutes of an enzymatic reaction such as this, the number of substrate molecules is usually so large c ...
Enzyme - Mercer Island School District
... • All the previous factors also affect an enzyme’s rate of reaction. • Since enzymes are ______________ with specifically shaped _______________, the ________________ (unfolding) of an enzyme also affects its ability to _________________ . • Extreme _____________ and extreme ______conditions denatur ...
... • All the previous factors also affect an enzyme’s rate of reaction. • Since enzymes are ______________ with specifically shaped _______________, the ________________ (unfolding) of an enzyme also affects its ability to _________________ . • Extreme _____________ and extreme ______conditions denatur ...
2013 Enzymes ppt
... formed Products have a different shape from the substrate Once formed, they are released from the active site Leaving it free to become attached to another substrate ...
... formed Products have a different shape from the substrate Once formed, they are released from the active site Leaving it free to become attached to another substrate ...
Thermodynamics and enzymes
... d. solutes diffuse from a region of high concentration to regions of lower concentration 12. In a given reaction, the amount of product produced is 5 times the amount of reactant that remains. This reaction would have a. a Keq > 1. b. a Keq < 1. c. a Keq = 1. d. a Keq = 0. 13. Allosteric modulators ...
... d. solutes diffuse from a region of high concentration to regions of lower concentration 12. In a given reaction, the amount of product produced is 5 times the amount of reactant that remains. This reaction would have a. a Keq > 1. b. a Keq < 1. c. a Keq = 1. d. a Keq = 0. 13. Allosteric modulators ...
Proteins and Nucleic Acids
... Two changes cause a change in the shape of the protein…this is known as DENATURATION. So if the shape changes, what’s affected? The Function of the Protein! Other Causes of Protein Denaturation salt concentration and environmental factors ...
... Two changes cause a change in the shape of the protein…this is known as DENATURATION. So if the shape changes, what’s affected? The Function of the Protein! Other Causes of Protein Denaturation salt concentration and environmental factors ...
Enzymes
... energy of a particular reaction. It may encourage Reactant the breaking of a particular chemical bond in the reactant. Course of reaction ...
... energy of a particular reaction. It may encourage Reactant the breaking of a particular chemical bond in the reactant. Course of reaction ...
An introduction to enzyme structure and function
... A more recent explanation to the fitting of enzymes is the induced-fit hypothesis. This hypothesis still states that one substrate fits one active site, this is scientific fact. But this hypothesis suggests that the enzyme molecule slightly changes shape when it collides with substrate, making the a ...
... A more recent explanation to the fitting of enzymes is the induced-fit hypothesis. This hypothesis still states that one substrate fits one active site, this is scientific fact. But this hypothesis suggests that the enzyme molecule slightly changes shape when it collides with substrate, making the a ...
Slideshow
... enzyme acts is called the substrate. • The substrate is a complementary shape to the active site • The two fit to form the enzyme- substrate complex. • Temporary bonds form between the amino acids of the active site and groups on the substrate molecule. ...
... enzyme acts is called the substrate. • The substrate is a complementary shape to the active site • The two fit to form the enzyme- substrate complex. • Temporary bonds form between the amino acids of the active site and groups on the substrate molecule. ...
CHapter 2b Practice problems answers
... Enzymes only work with specific substrates because each substrate — a. actively interferes with other substrates around it b. has a specific activation site for enzyme attachment c. can only use a specific ionic bond with the enzyme d. destroys its specific enzyme ...
... Enzymes only work with specific substrates because each substrate — a. actively interferes with other substrates around it b. has a specific activation site for enzyme attachment c. can only use a specific ionic bond with the enzyme d. destroys its specific enzyme ...
Enzymes
... Enzymes are proteins (tertiary and quaternary structures) that catalyze (act as catalysts) the rate of a chemical reaction (increase). They do this by decreasing the amount of activation energy required for a reaction. ...
... Enzymes are proteins (tertiary and quaternary structures) that catalyze (act as catalysts) the rate of a chemical reaction (increase). They do this by decreasing the amount of activation energy required for a reaction. ...
Bio301 Biochemistry I
... e) If enough substrate is added, the normal Vmax of an enzyme-catalyzed reaction can be attained even in the presence of a noncompetitive inhibitor. f) The sigmoidal shape of the v versus [S] curve for some regulatory enzymes indicates that the affinity of the enzyme for substrate decreases as the s ...
... e) If enough substrate is added, the normal Vmax of an enzyme-catalyzed reaction can be attained even in the presence of a noncompetitive inhibitor. f) The sigmoidal shape of the v versus [S] curve for some regulatory enzymes indicates that the affinity of the enzyme for substrate decreases as the s ...
Enzyme Kinetics Lab
... Enzymes are a class of proteins that greatly speed up (catalyze) reactions between specific substances, usually at their functional groups. The substances that each type of enzyme acts upon are called its substrates. Enzymes have four common features: 1. They don’t make anything happen that couldn’t ...
... Enzymes are a class of proteins that greatly speed up (catalyze) reactions between specific substances, usually at their functional groups. The substances that each type of enzyme acts upon are called its substrates. Enzymes have four common features: 1. They don’t make anything happen that couldn’t ...
Enzymes
... • The active site on the enzyme changes (wraps around) to fit the shape of the substrate • Results in enzymatic activity and product formation • This means that an enzyme can work on more that one substrate if this model is used. • This model is not as rigid as the lock and key theory. It suggests t ...
... • The active site on the enzyme changes (wraps around) to fit the shape of the substrate • Results in enzymatic activity and product formation • This means that an enzyme can work on more that one substrate if this model is used. • This model is not as rigid as the lock and key theory. It suggests t ...
Rate of enzymatic reactions
... reaction increases as the temperature is raised. Higher temperature generally causes more collisions among the molecules and therefore increases the rate of a reaction. More collisions increase the likelihood that substrate will collide with the active site of the enzyme, thus increasing the rate of ...
... reaction increases as the temperature is raised. Higher temperature generally causes more collisions among the molecules and therefore increases the rate of a reaction. More collisions increase the likelihood that substrate will collide with the active site of the enzyme, thus increasing the rate of ...
Enzyme Kinetics II
... II. Kinetic Behavior of Enzymes Catalyzing Bimolecular Reactions? [S37] a. Here is a classic example where there has to be an A and B b. There are two different substrates that it has to bind c. Gives rise to the complex A E and B together d. Two substrates will have to become P and Q – the products ...
... II. Kinetic Behavior of Enzymes Catalyzing Bimolecular Reactions? [S37] a. Here is a classic example where there has to be an A and B b. There are two different substrates that it has to bind c. Gives rise to the complex A E and B together d. Two substrates will have to become P and Q – the products ...
Enzyme - fiveless|notes
... Both enzyme and substrate change shape straining bonds during reaction. Strained form of the substrate (transition state) exist for short while ...
... Both enzyme and substrate change shape straining bonds during reaction. Strained form of the substrate (transition state) exist for short while ...
enzyme
... After the cycle, the enzyme is then free to take another substrate molecule into its active site Enzymes emerge from the reaction in their original form ...
... After the cycle, the enzyme is then free to take another substrate molecule into its active site Enzymes emerge from the reaction in their original form ...
File
... Each type of enzyme has a specific ‘active site conformation’ that is essential for its catalytic activity. The ‘active site conformation’ includes the presence of some specific amino acid(s) at the active site besides the three dimensional structure of protein. These amino acids are involved in bi ...
... Each type of enzyme has a specific ‘active site conformation’ that is essential for its catalytic activity. The ‘active site conformation’ includes the presence of some specific amino acid(s) at the active site besides the three dimensional structure of protein. These amino acids are involved in bi ...
Enzymes: “Helper” Protein molecules
... Enzymes are not changed by the reaction used only temporarily re-used again for the same reaction with other molecules very little enzyme needed to help in many reactions ...
... Enzymes are not changed by the reaction used only temporarily re-used again for the same reaction with other molecules very little enzyme needed to help in many reactions ...
Enzyme kinetics
Enzyme kinetics is the study of the chemical reactions that are catalysed by enzymes. In enzyme kinetics, the reaction rate is measured and the effects of varying the conditions of the reaction are investigated. Studying an enzyme's kinetics in this way can reveal the catalytic mechanism of this enzyme, its role in metabolism, how its activity is controlled, and how a drug or an agonist might inhibit the enzyme.Enzymes are usually protein molecules that manipulate other molecules — the enzymes' substrates. These target molecules bind to an enzyme's active site and are transformed into products through a series of steps known as the enzymatic mechanismE + S <——> ES <——> ES*< ——> EP <——> E + P. These mechanisms can be divided into single-substrate and multiple-substrate mechanisms. Kinetic studies on enzymes that only bind one substrate, such as triosephosphate isomerase, aim to measure the affinity with which the enzyme binds this substrate and the turnover rate. Some other examples of enzymes are phosphofructokinase and hexokinase, both of which are important for cellular respiration (glycolysis).When enzymes bind multiple substrates, such as dihydrofolate reductase (shown right), enzyme kinetics can also show the sequence in which these substrates bind and the sequence in which products are released. An example of enzymes that bind a single substrate and release multiple products are proteases, which cleave one protein substrate into two polypeptide products. Others join two substrates together, such as DNA polymerase linking a nucleotide to DNA. Although these mechanisms are often a complex series of steps, there is typically one rate-determining step that determines the overall kinetics. This rate-determining step may be a chemical reaction or a conformational change of the enzyme or substrates, such as those involved in the release of product(s) from the enzyme.Knowledge of the enzyme's structure is helpful in interpreting kinetic data. For example, the structure can suggest how substrates and products bind during catalysis; what changes occur during the reaction; and even the role of particular amino acid residues in the mechanism. Some enzymes change shape significantly during the mechanism; in such cases, it is helpful to determine the enzyme structure with and without bound substrate analogues that do not undergo the enzymatic reaction.Not all biological catalysts are protein enzymes; RNA-based catalysts such as ribozymes and ribosomes are essential to many cellular functions, such as RNA splicing and translation. The main difference between ribozymes and enzymes is that RNA catalysts are composed of nucleotides, whereas enzymes are composed of amino acids. Ribozymes also perform a more limited set of reactions, although their reaction mechanisms and kinetics can be analysed and classified by the same methods.