Q1. (a) An enzyme catalyses only one reaction. Explain why
... Our knowledge of the relationship between protein structure and function has led to the development of the new technology of protein engineering. This involves changing the amino 10 acid sequence of a protein and altering its tertiary structure. Altering the tertiary structure changes the protein’s ...
... Our knowledge of the relationship between protein structure and function has led to the development of the new technology of protein engineering. This involves changing the amino 10 acid sequence of a protein and altering its tertiary structure. Altering the tertiary structure changes the protein’s ...
Taylor_Sheridan_Biochemwebquest
... basically a bag full of chemical reactions, which are created by the enzymes. 2. What type of organic molecules (carbohydrate, lipid, protein, nucleic acid) are most enzymes? Proteins are the organic molecules which are most enzymes. 3. What does the shape of an enzyme have to do with how well the e ...
... basically a bag full of chemical reactions, which are created by the enzymes. 2. What type of organic molecules (carbohydrate, lipid, protein, nucleic acid) are most enzymes? Proteins are the organic molecules which are most enzymes. 3. What does the shape of an enzyme have to do with how well the e ...
Chapter 15
... Allosterism: Enzyme regulation based on an event occurring at a place other than the active site but that creates a change in the active site. • An enzyme regulated by this mechanism is called an allosteric enzyme. • Allosteric enzymes often have multiple polypeptide chains. • Negative modulation: I ...
... Allosterism: Enzyme regulation based on an event occurring at a place other than the active site but that creates a change in the active site. • An enzyme regulated by this mechanism is called an allosteric enzyme. • Allosteric enzymes often have multiple polypeptide chains. • Negative modulation: I ...
Chapter 15 Enzymes
... Allosterism: Enzyme regulation based on an event occurring at a place other than the active site but that creates a change in the active site. • An enzyme regulated by this mechanism is called an allosteric enzyme. • Allosteric enzymes often have multiple polypeptide chains. • Negative modulation: I ...
... Allosterism: Enzyme regulation based on an event occurring at a place other than the active site but that creates a change in the active site. • An enzyme regulated by this mechanism is called an allosteric enzyme. • Allosteric enzymes often have multiple polypeptide chains. • Negative modulation: I ...
amino acid
... - More energy is released when new bonds are formed in the products than was needed to break the old bonds in the reactants ...
... - More energy is released when new bonds are formed in the products than was needed to break the old bonds in the reactants ...
Exam II
... a. Hydrogen bonding to a histidine residue assists stabilization of the Fe2+ -O2 complex in both hemoglobin and myoglobin. b. Myoglobin is a single polypeptide chain folded about a heme prosthetic group. c. The iron in both hemoglobin and myoglobin has two coordination sites that bind to oxygen. d. ...
... a. Hydrogen bonding to a histidine residue assists stabilization of the Fe2+ -O2 complex in both hemoglobin and myoglobin. b. Myoglobin is a single polypeptide chain folded about a heme prosthetic group. c. The iron in both hemoglobin and myoglobin has two coordination sites that bind to oxygen. d. ...
Enzyme
... chance to an enzyme-substrate complex forming. Some times, the inorganic ions are free and does not bind to the enzyme or substrate, ...
... chance to an enzyme-substrate complex forming. Some times, the inorganic ions are free and does not bind to the enzyme or substrate, ...
File - Biology withMrs. Ellsworth
... Draw the pH scale. Label the numbers of the scale. Indicate which number is neutral. Indicate the acid range. Indicate the base range. Indicate which side is more concentrated with OH- and Indicate which side is more concentrated with H+. ...
... Draw the pH scale. Label the numbers of the scale. Indicate which number is neutral. Indicate the acid range. Indicate the base range. Indicate which side is more concentrated with OH- and Indicate which side is more concentrated with H+. ...
Control and Integration of Metabolism
... substrate e.g. modulator molecule other than their substrate e.g. threonine dehydratase, the substrate is threonine and the modulator is L-isolecuien. • In Homotropic enzymes, the substrate also functions as the modulator. Homotropic enzymes contain two or more binding sites for the substrate- Modul ...
... substrate e.g. modulator molecule other than their substrate e.g. threonine dehydratase, the substrate is threonine and the modulator is L-isolecuien. • In Homotropic enzymes, the substrate also functions as the modulator. Homotropic enzymes contain two or more binding sites for the substrate- Modul ...
Microbial Metabolism
... What are enzymes? • Without enzymes, collision theory rules – Need sufficient activation energy – Number of molecules above this activation level = reaction rate ...
... What are enzymes? • Without enzymes, collision theory rules – Need sufficient activation energy – Number of molecules above this activation level = reaction rate ...
Exam II ReviewQuestions
... 13. Liver alcohol dehydrogenases (ADH) is relatively nonspecific. Its normal substrate is ethanol, however, it will oxidize other primary alcohols, such as methanol, to their corresponding aldehydes. In the case of methanol this produces formaldehyde, which is quite toxic and can lead to blindness. ...
... 13. Liver alcohol dehydrogenases (ADH) is relatively nonspecific. Its normal substrate is ethanol, however, it will oxidize other primary alcohols, such as methanol, to their corresponding aldehydes. In the case of methanol this produces formaldehyde, which is quite toxic and can lead to blindness. ...
Enzymatic
... 43. Based off of your observations of the enzyme shown, which of the following is true? A. The denaturation of the enzyme DOES NOT affect the enzyme’s function. B. The denaturation of this enzyme by pH changes is irreversible. In other words, restoring the pH to an optimal level DOES NOT fix the enz ...
... 43. Based off of your observations of the enzyme shown, which of the following is true? A. The denaturation of the enzyme DOES NOT affect the enzyme’s function. B. The denaturation of this enzyme by pH changes is irreversible. In other words, restoring the pH to an optimal level DOES NOT fix the enz ...
Ch_02_Chemical_Elements
... • Enzymes are large biological molecules responsible for the thousands of chemical interconversions that sustain life. They are highly selective catalysts, greatly accelerating both the rate and specificity of metabolic reactions, from the digestion of food to the synthesis of DNA. Most enzymes are ...
... • Enzymes are large biological molecules responsible for the thousands of chemical interconversions that sustain life. They are highly selective catalysts, greatly accelerating both the rate and specificity of metabolic reactions, from the digestion of food to the synthesis of DNA. Most enzymes are ...
File
... Outline the process of glycolysis. one hexose sugar / glucose is converted to two 3-carbon compounds / pyruvate; at start 2 ATP are used / phosphorylation of glucose; net gain of 2 ATP / 4 ATP produced in total; ...
... Outline the process of glycolysis. one hexose sugar / glucose is converted to two 3-carbon compounds / pyruvate; at start 2 ATP are used / phosphorylation of glucose; net gain of 2 ATP / 4 ATP produced in total; ...
Biochemistry (Unit 1) Exam Review
... are these enzymes activated and regulated? temperature, ph and inhibitors all affect enzyme activity because each enzyme has optimum conditions. Some enzymes are limited by inorganic cofactors that bind to the substrate or active site. enzymes regulated by competitive inhibitors that adhere to the s ...
... are these enzymes activated and regulated? temperature, ph and inhibitors all affect enzyme activity because each enzyme has optimum conditions. Some enzymes are limited by inorganic cofactors that bind to the substrate or active site. enzymes regulated by competitive inhibitors that adhere to the s ...
Name
... Enzymes: Activity of Catalase Enzymes are specialized proteins that make it possible for our cells to perform all of the chemical reactions that they need to. Simply put, each reaction that occurs in the body has a cost. The currency for the cell, however, is not dollars and cents, but rather energy ...
... Enzymes: Activity of Catalase Enzymes are specialized proteins that make it possible for our cells to perform all of the chemical reactions that they need to. Simply put, each reaction that occurs in the body has a cost. The currency for the cell, however, is not dollars and cents, but rather energy ...
2-1 The Nature of Matter
... 2-4 Chemical Reactions and Enzymes Everything that happens inside an organism is based on ____________ reactions: ex: growth, interaction w/environment, reproduction, movement ____________________- process that changes or transforms 1set of chemicals into another -reactants react to make products -c ...
... 2-4 Chemical Reactions and Enzymes Everything that happens inside an organism is based on ____________ reactions: ex: growth, interaction w/environment, reproduction, movement ____________________- process that changes or transforms 1set of chemicals into another -reactants react to make products -c ...
Enzyme
Enzymes /ˈɛnzaɪmz/ are macromolecular biological catalysts. Enzymes accelerate, or catalyze, chemical reactions. The molecules at the beginning of the process are called substrates and the enzyme converts these into different molecules, called products. Almost all metabolic processes in the cell need enzymes in order to occur at rates fast enough to sustain life. The set of enzymes made in a cell determines which metabolic pathways occur in that cell. The study of enzymes is called enzymology.Enzymes are known to catalyze more than 5,000 biochemical reaction types. Most enzymes are proteins, although a few are catalytic RNA molecules. Enzymes' specificity comes from their unique three-dimensional structures.Like all catalysts, enzymes increase the rate of a reaction by lowering its activation energy. Some enzymes can make their conversion of substrate to product occur many millions of times faster. An extreme example is orotidine 5'-phosphate decarboxylase, which allows a reaction that would otherwise take millions of years to occur in milliseconds. Chemically, enzymes are like any catalyst and are not consumed in chemical reactions, nor do they alter the equilibrium of a reaction. Enzymes differ from most other catalysts by being much more specific. Enzyme activity can be affected by other molecules: inhibitors are molecules that decrease enzyme activity, and activators are molecules that increase activity. Many drugs and poisons are enzyme inhibitors. An enzyme's activity decreases markedly outside its optimal temperature and pH.Some enzymes are used commercially, for example, in the synthesis of antibiotics. Some household products use enzymes to speed up chemical reactions: enzymes in biological washing powders break down protein, starch or fat stains on clothes, and enzymes in meat tenderizer break down proteins into smaller molecules, making the meat easier to chew.