HO. но- OH O-R 26. What is the purpose of achieving the transition state of the substrate in the active site of the enzyme? A. It allows ionic charges to form. B. It leads to formation of product. C. It relieves strain in covalent bonds. D. It keeps the substrate activated.
Q: 14.Which explanation best fits the graph for pH's effect on an enzyme? Opi p O A. As the pH gets…
A: Each enzyme performs optimally at a certain pH level. The optimal pH for an enzyme is determined by…
Q: %23 In this below equation, enzyme X belongs to which class of enzymes?" Enzyme X Substrate H20…
A: Biochemical reactions are of different types. The enzymes that influence the rate of these reactions…
Q: Please answer number 5 and highlighted answers are wrong please provide me a explanation why it is…
A: Hemoglobin is the metalloprotein that contains iron ion in it. in the human body, hemoglobin is an…
Q: 20. The following reaction would be catalyzed by what type of enzyme? HO COO coO .cOO "OC CO- H2 H2…
A: There are different types of enzymes used to catalyze a different kind of reaction.
Q: 9. For the graph below, which arrow indicates the ACTIVATION ENERGY for an ENZYME CATYLIZED…
A:
Q: 20. Which of the following is often involved in reactions that change -CH2-CH2- portions of…
A: Coenzymes are organic non-protein compound that was bonded to an enzyme to catalyze the reaction.…
Q: Why would an enzyme no longer function once it denatures?
A: In living systems catalysts are found and they termed Enzymes. That plays the role of accelerating…
Q: 13. A human digestive enzyme breaks down its substrate at a fast rate al What would occur if the…
A: As it is stated that it is a human digestive enzyme, its optimal temperature is around 25-40oC. So,…
Q: D: Reaction? PPi АТР B: Enzyme? NH2 OH NH2 NH, A: Name? C: Name?
A: Amino acids are the building blocks of proteins. Amino acid glutamate has the capability to act as a…
Q: 6. Enzyme X exhibits maximum activity at pH = 6.9. X shows a fairly sharp decrease in its activity…
A: Enzymes are biocatalysts that speed up biological reactions. Active site of enzymes are the pockets…
Q: All of the chemical reactions of a specific organism that result in the synthesis of ATP and supply…
A: Anabolism is the synthesis of complex molecules in living organisms from simpler ones together with…
Q: 4. Match the figure and the letter. Glycolytic reaction: Participants: A. Fructose-1,6-bisphosphate.…
A: Glycolysis in the cytosol of all the cells. It occurs in both aerobic and anaerobic conditions. It…
Q: 2. Which explanation best fits the graph for pH's effect on an enzyme? Substrate concentration a.As…
A: pH has the greatest effect on the enzyme catalysis as well as denaturing the protein structure.
Q: 2. Match the figure and the letter. The diagram of glycogen degradation: Metabolite: медицинсий…
A:
Q: heat FIGURE 6 substrate active site enzyme substrate denatured enzyme substrate cannot enter binding…
A: Enzymes are protein molecules acting as biological catalysts that are able to accelerate the rate of…
Q: Catalyst Activation Energy Function of Enzyme: Diagram of Energy graph with an Enz Enzyme-Substrate…
A: Nearly all biological reactions are catalysed by catalysts called the enzymes , which functions onn…
Q: kcat = ? an enzyme has an aspartic acid in the active site with a pKa = 4.0 and the kcat for this…
A: pKa 4 pH changed from 4 to 3.5 Ionization percentage([A]/[HA]) =10^(pH-pKa)…
Q: True or False? The site on an enzyme to which the substrate binds is called the allosteric site. O…
A: Enzymes are proteinaceous substances which acts as biocatalysts in living organisms which increases…
Q: 10. Which of the following statements about enzymes is true? a. they are made of lipids and control…
A: Proteins that serve as biological catalysts are known as enzymes. Catalysts help to speed up…
Q: TRUE OR FALSE 25. The Lineweaver-Burk plot shows a linear pattern of product formation. 26.…
A: Lineweaver-Burk plot: This is a plot that determines Km and Vmax. It is also known as a Double…
Q: 5. What molecules are missing from boxes in the gluconeogenesis reaction shown below 203PO- OPO,2…
A: Gluconeogenesis is the synthesis of glucose from non-carbohydrate precursors. Gluconeogenesis is a…
Q: What can a pH-activity profile of an enzyme tell you? Select one: а. The kinetic mechanism b. How…
A: The pH activity profile of an enzyme describes the enzyme activity. Enzyme activity is at its…
Q: GTP GDP, CO2 the task is to DRAW a reasonable mechanism for reaction listed. Not all products or…
A: Conversion of oxaloacetate to phosphoenolpyruvate is the major step in gluconeogenesis.…
Q: Describe the reaction oh Hatch-Slack (enzyme names are not required). While doing so make sure to…
A: C4 Pathway It was Hatch and Slack , who discovered the C4 pathway in 1966. Plants that are adapted…
Q: 7. Fill in the blank with the correct terms. Phosphorylation and dephosphorylation are what type of…
A: Introduction: Enzymes are biological catalysts that mean they are catalysts of life that increase…
Q: H2C HO CH2 H. N. CH H2C. Enzyme X is an aspartyl protease. Here is the tetrahedral intermediate in…
A: Aspartyl proteases are proteases that contain two conserved aspartic acid residues at the active…
Q: Select true if the statement is CORRECT and false if OTHERWISE 1. Enzymes are catalysts and…
A: "Since you have posted a question with multiple sub-parts, we will solve the first three sub-parts…
Q: 10. Carboxypeptidase cleaves amino acids, one at a time, from the carboxyl end of the peptide chain.…
A: Enzymes are highly specialized proteins that have extraordinary catalytic power, greater than that…
Q: available. Research an enzyme that is needed in the human body. Address the following topics: 1.…
A: Enzymes are very much essential for our body functions. So understanding their structure, function,…
Q: 1. During a metabolic redox reaction, the coenzyme that gains an electron has been a reduced and now…
A: “Since you have asked multiple questions, we will solve the first question for you. If you want any…
Q: 5. Salivary a-amylase cleaving a(1 example for which type of specificity? a) Group specificity b)…
A: Group specificity : Enzyme will catalyze the reaction on a function group of different molecules…
Q: 8. An enzyme has the ability to catalyze reactions of several unrelated compounds. The mechanism of…
A: The enzyme catalyzed reaction is the reaction in which biocatalyst known as enzyme binds to the…
Q: Compare and contrast the activation free energy and the free energy change for an enzyme-catalyzed…
A: The thermodynamic free energy (change) can be defined as the maximum amount of work that can be…
Q: 8. In patients with diabetes mellitus type I, the biochemical disorders result from changes in fuel…
A: When body fluid contains too much acid, the condition is called acidosis. In Diabetes mellitus type…
Q: the substrates must be a high erall reaction is exergonic
A: Answer Substrate level phosphorylation in which One of the substrates must be a higher free energy…
Q: . Which of the following is not part of ATP composition? A. Three phosphate groups B. Ribose…
A: Since you have asked multiple questions , we will solve the first question for you. If you want any…
Q: Why is the reaction rate low at pH7? Be specific and say something about the enzyme structure at the…
A: Reaction rate is often described as how fast the reaction takes place or proceeds. Enzymes are often…
Q: 4. Using structures show the hydrolytic breakdown of cellobiose and maltose. 5. Identify the type of…
A: Hydrolysis is defined as a type of chemical reaction where water breaks down the chemical bonds…
Q: RANCIDITY: I. Oxygen acts as an oxidizing agent at carbon to carbon double bonds II. The products…
A: Rancidity is the slow oxidation of oil and fat which is present in the food and other products and…
Q: 2. Circle the carbon atoms of the carbohydrate rings of these sugars at which the oxidation takes…
A: If a sugar(Monosaccharide, Disaccharide or Polysaccharide) can cause reduction of other compounds…
Q: I. An enzyme is what type of organic compound? II. What four elements are part of this organic…
A: if we perform analysis on a plant tissue, animal tissue or microbial based we obtain a list of…
Q: what happens if an enzyme is not made correctly?
A: “Since you have asked multiple question, we will solve the first question for you. If you want any…
Q: 11. Compound X permanently bind by covalent bonds to allosteric site of enzyme C thus completely…
A: According to the given question, Compound X bind with a covalent linkage the enzyme allosteric site…
Q: 23. The graph below is a graph of Vmax (a) Label the graph clearly with both the Vmax and the Km.…
A: As given in the question, V/Vmax was plotted with substrate concentration. V= rate of a reaction…
Q: BONUS: JA transition state can decay either to products or substrates. What factor determines which…
A: The state of transition is the transitory molecular structure in which the molecule is no longer a…
Q: 2. Write a more complete reaction scheme for the metabolic process depicted below. Be sure to…
A: Codeine is a opioid receptor analgesic prodrug that acts by biotransformation into morphine by…
Q: 2. Describe the relationship between substrate and the product. What happens when you increase the…
A: Substrate- It is a molecule on which enzyme acts. Substrate binds to the active site of enzyme and…
Q: Which statement is NOT completely true? O In the Induced-fit theory, the conformation of the active…
A: The reaction that can transform of type of chemical substance to other is called a chemical…
Q: Explain why those biological reactions that have their equilibria shifted towards the products have…
A: Thermodynamically favorable reactions have a negative value of the change in Gibb's Free Energy. In…
8
Step by step
Solved in 5 steps
- Which of the following statements about inhibition is true? a. Allosteric inhibitors and allosteric activators are competitive for a given enzyme. b. If an inhibitor binds the active site, it is considered noncompetitive. c. If an inhibitor binds to a site other than the active site, this competitive inhibition. d. A noncompetitive inhibitor is believed to change the shape of the enzyme, making its active site inoperable. e. Competitive inhibition is usually not reversible.Which of the following statements about the allosteric site is true? a. The allosteric site is a second active site on a substrate in a metabolic pathway. b. The allosteric site on an enzyme can allow the product of a metabolic pathway to inhibit that enzyme and stop the pathway. c. When the allosteric site of an enzyme is occupied, the reaction is irreversible and the enzyme cannot react again. d. An allosteric activator prevents binding at the active site. e. An enzyme that possesses allosteric sites does not possess an active site.Why is the reaction rate low at pH7? Be specific and say something about the enzyme structure at the molecular level!
- a) what happens if an enzyme is not made correctly? b) what is the function of the major RNA is it proteins synthesis? c) what is the primary source of all glucose, and why is it such an important monosaccharide?You need to include its molecular formula. d) when you react ammonia with a halogenated alkane will you get only one organic product? Why or why not? (do not talk about inorganic products) e) emulsifiers are pretty important compounds for daily life, externally and internally to us humans. Describes the two parts of an emulsifier molecule, and how most emulsifiers work and what they actually do. f) consider the ring structure of B-D glucose. it will give a positive test as a reducing sugar. Describe how that can happen in a pH=7 solution such as fehlings'?You are observing an enzyme driven reaction. To the reaction mixture you add a chemical X which inhibits the reaction. If you add more substrate, the reaction rate approaches the Vmax of the uninhibited reaction. Furthermore, the structure of X is similar to the natural substrate. What kind of inhibitor is X?Describe the basics of enzyme structure and function. Be sure to address what makes enzymes specific, how active sites function and how substrates create an induced fit. Also, explain how enzymes can be inhibited by both a competitive inhibitor and a noncompetitive inhibitor.
- Describe the reaction oh Hatch-Slack (enzyme names are not required). While doing so make sure to summarize the energetics.Using an energy diagram, show why the lock-and-key model could lead to an inefficient enzyme mechanism. Hint: Remember that the distance to the transition state must be minimized for an enzyme to be an effective catalyst.1a-Enzymes serve as catalysts for chemical reactions. What does this mean? Select all that apply. Select one or more: a. Enzymes make reactions more likely to occur. b. Enzymes increase the activation energy. c. Enzymes decrease the free energy (?G) of a reactio d. Enzymes increase the free energy (?G) of a reaction. 1b-When ATP is hydrolysed: Select one: a. The energy will be released as heat if the reaction is not coupled to a substrate, b. The potential energy associated with the resulting ADP molecule increases. c. The terminal phosphate is transferred to a substrate, lowering the potential energy of the substrate d. Water is formed and released as a reaction product.
- Which of the following statements are correct? explain your answers.a. The active site of an enzyme usually occupies only a small fraction of the enzyme surface.B. catalysis by some enzymes involves the formation of a covalent bond between an amino acid side chain and a substrate molecule.c. a β sheet can contain up to five strands, but no more.d. The specificity of an antibody molecule is contained exclusively in loops on the surface of the folded light-chain domain.e. The possible linear arrangements of amino acids are so vast that new proteins almost never evolve by alteration of old ones. f. allosteric enzymes have two or more binding sites. G. noncovalent bonds are too weak to influence the three- dimensional structure of macromolecules.a. Describe in your own words, 5 assumptions that must be made in order to apply a Michaelis-Menten kinetic model to an enzymatic reaction. providing a mathematical expression or inequivalent (">" or "In the following graph: A represents the product. B represents the energy of activation when enzymes are present. C is the free energy difference between A and D. C is the energy of activation without enzymes. E is the difference in free energy between the reactant and the products.