Explain how the position in the active site and function of the oxyanion hole of chymotrypsin supports the theory that enzymes preferentially bind the transition state of the reactions they catalyze
Q: Consider the mechanism of the aldolase reaction given in figure 9.25. In chapter 12, we saw that the…
A: Aldolase are class of enzyme that performs an aldol reaction (formation of an aldol) or its reverse…
Q: The mechanism involved in the reaction catalyzed by phosphoglyceromutase is known to involve a…
A: Glycolysis is breakdown of glucose to provide energy. Phosphoglyceromutase catalyze the conversion…
Q: You have discovered a new enzyme that has a nearly identical active site to chymotrypsin. This new…
A: As given peptide is Asn-Phe-lys, and discovered enzyme cleaves at C terminal of non ionizable polar…
Q: When enzyme solutions are heated, there is a progressive loss of catalytic activity over time due to…
A: Enzyme is a protein and its denatured at high temperature. High temperature broke its peptide bond.…
Q: Compare and contrast Pyruvate Dehydrogenase with a-ketoglutarate dehydrogenase Outline the…
A: The tricarboxylic acid cycle is the metabolic pathway that generates NADH and FADH2 from the…
Q: Beginning with the 1st tetrahedral intermediate, show the complete steps in chymotrypsin mechanism…
A: The peptides are formed by linking different amino acids through peptide bonds. The enzyme involved…
Q: Although most enzymes are quite specific, they can catalyze side reactions with compounds that are…
A: NAD NAD is Nicotinamide adenine dinucleotide NAD is the coenzyme form of Vitamin B5 (Niacin). It…
Q: This question should be answered with two or three sentences using relevant biochemical vocabulary.
A: Serine endopeptidases or serine proteases are enzymes with nucleophilic serine at active sites which…
Q: Lithium ion inhibits the synthesis of inositol trisphosphate by inhibiting a reaction in the…
A: Hydrolysis of phosphatidylinositol 4,5-bisphosphate (PIP2) gives Inositol triphosphate, which is a…
Q: The reaction catalyzed by malate dehydrogenase has a ΔG°′ value of +29.7 kJ⋅mol−1. Given what this…
A: Free energy changes in biochemical reactions are denoted by ΔG°', the biochemical standard…
Q: Phosphonacetyl-L-aspartate (PALA) is a potent inhibitor of aspartate transcarbamoylase because it…
A: Enzymes are biocatalysts that catalyse biochemical reactions. They contain an active site where the…
Q: b) Enzymes accelerate reactions by facilitating the formation of the transition state. Define…
A: Enzymes are catalytic protein, which plays a crucial role to catalyze the chemical reaction and…
Q: Chymotrypsin, trypsin, and elastase all share the same catalytic mechanism, but have different…
A: Proteases are enzymes that cleave polypeptide chains. They all hydrolyze the peptide bond present in…
Q: Anabolic reactions like fatty acid synthesis are inherently endergonic and require exergonic driving…
A: The synthesis of fatty acids mainly palmitic acid from acetyl CoA involves seven enzyme reaction,…
Q: Show that the free energy change for the succinate dehydrogenase reaction catalyzed by Complex II is…
A: The complex II in electron transport chain is called as succinate dehydrogenase, the complex II…
Q: According to Paul Boyer, the mechanism of ATP synthesis involves the rotation of the y subunit which…
A: A key molecule that upon hydrolysis gives the energy to work with an assortment of cell measures…
Q: Explain how would an uncoupler Dinitrophenol of oxidative phosphorylation promote weight loss.
A: The organic chemical compound 2, 4-Dinitrophenol (DNP) is described. It is a biochemically active…
Q: You have discovered a new enzyme that has a nearly identical active site to chymotrypsin. This new…
A: It is mentioned that the newly discovered enzyme with a reaction mechanism similar to that of the…
Q: Sodium fluoroacetate (FH2CCOO- Na+) is highly toxic. Patients with fluoroacetate poisoning…
A: Fluoroacetate is poisonous to animals and humans as it inhibits some of the prime enzyme required in…
Q: Provide an explanation for why glucose-6-phopshate must be isomerized to fructose-6-phosphate in…
A: Chemical reactions that occur within the living body are collectively known as metabolism. The…
Q: Compare the allosteric regulation of phosphorylase in the liver and in muscle, and explain the…
A: Phosphorylase are enzymes that catalyse the addition of a phosphate group from an inorganic…
Q: What is the quaternary structure of glycogen phosphorylase? How would you characterize the…
A: The allosteric effect is generally the binding of a ligand to one part on a protein molecule and…
Q: write the reactions using structural formulas by which a 7-carbon fatty acid is activated and…
A: The 7 carbon fatty acid is first activated to its acyl-CoA form. Then it undergoes beta-oxidation to…
Q: The mechanism of chymotrypsin is used as a model for studying enzyme reaction mechanisms. Answer…
A: A catalytic triad is a group of three amino acids, which is found in the active site of certain…
Q: Malonate competes with succinate in the succinate dehydrogenase reaction. Explain why increasing the…
A: Enzymatic inhibitors decrease enzyme activity. Where the enzyme inhibition is of 3 types…
Q: Fructose 2,6-bisphosphate is a potent stimulator of phosphofructokinase. Explain how fructose…
A: Glycolysis is a process in which glucose is metabolized into the pyruvate with the production of…
Q: Describe two types of regulation of the enzyme glutamine synthetase and explain why the regulation…
A: When amino acids are degraded in the tissue, they release ammonia. Ammonia is toxic to the cell so…
Q: Cells often use the same enzyme reaction pattern for analogous metabolic conversions. For example,…
A: The first phase of fatty acid oxidation is called beta oxidation. It is a cyclic process. Each cycle…
Q: Dicyclohexylcarbodiimide (DCCD) is a reagent that reacts with Asp or Glu residues. Explain why the…
A: ATPase is the enzyme complex, which is known to synthesize ATP by transferring protons and…
Q: Write out the balanced chemical equation for the FIRST round of oxidation of C16:cis-9.
A: in the first round of beta oxidation, we will have a 2C short acyl Co A, an acetyl Co A, FADH2 and…
Q: The following are the negative regulators of phosphofructokinase except Select one: a. AMP +b. H…
A: Introduction: The series of chemical reaction that covert glucose into pyruvate and ATP is known as…
Q: HCO3 + Glutamine + ATP Carbamoyl phosphate + Aspartate AT Case N-carbamoylaspartate -UMP UTP CTP
A: Enzymes are biological catalysts that increases the rate of biochemical reactions.The activity of…
Explain how the position in the active site and function of the oxyanion hole of chymotrypsin supports the theory that enzymes preferentially bind the transition state of the reactions they catalyze
Trending now
This is a popular solution!
Step by step
Solved in 2 steps with 1 images
- Most individuals with genetic defects in oxidative phosphorylation are found to have relatively high concentrations of alanine in their blood. how this in biochemical terms? please help :)Phosphonacetyl-L-aspartate (PALA) is a potent inhibitor of aspartate transcarbamoylase because itmimics the two physiological substrates of the enzyme. However, in the presence of substrates, lowconcentrations of PALA increase the reaction rate of aspartate transcarbamoylase. Explain this result.Put these steps in the mechanism of chymotrypsin catalysis in order from first to last. Note that some references may not break out each of these steps individually, but all steps should be ordered. There will be eight steps.
- ATP is a (+) allosteric effector, and CTP is a (-) allosteric effector of theenzyme ATCase. Both of these heterotropic effectors bind to the regulatorysubunits on ATCase. The substrates of ATCase, aspartate and carbamoylphosphate, bind the enzyme active site with positive cooperativity (i.e.,they exert a “+” homotropic effect on activity). As the concentrations ofthe substrates change from values where [S] ≪ KM to values where [S] issaturating ([S]≫ KM), how will the binding constants for each of the twoallosteric effectors change? In other words, does ATP bind ATCase withhigher affinity when [S] is low or high? Does CTP bind ATCase with higheraffinity when [S] is low or high?A solution of the enzyme hexokinase incubated at 45 °C lost 50% of its activity in 12 min, but when incubated at 45 °C in the presence of a very large concentration of one of its substrates, it lost only 3% of its activity in 12 min. Suggest why thermal denaturation of hexokinase was retarded in the presence of one of its substrates. It is impossible for this result to be true. OA. Adding the substrate increases the weak forces that stabilize the enzyme. OB. The high concentration of substrate forms a barrier around the hexokinase. D. Adding the substrate results in protective covalent bonding.There is another class of aldolase enzymes known as Class II. These enzymes are found in fungi, algae, and some bacteria. This class differs for Class I in that these enzymes do not have a Lys residue associated with their active sites, but contain a divalent cation (usually Zn2+ or Fe2+) in the active site. Outline a possible mechanism for a Class II aldolase and explain the function of the metal ion in the reaction.
- An example of an enzyme-catalyzed reaction proceeding via a transition-state stabilization mechanism is the hydrolysis of peptides by chymotrypsin while, Lysozyme is often cited as an example of an enzyme which operates by strain mechanism. Discuss both mechanisms in the context of each enzyme.When enzyme solutions are heated, there is a progressive loss of catalytic activity over time due to denaturation of the enzyme. A solution of the enzyme hexokinase incubated at 45 °C lost 50% of its activity in 12 min, but when incubated at 45 °C in the presence of a very large concentration of one of its substrates, it lost only 3% of its activity in 12 min. Suggest why thermal denaturation of hexokinase was retarded in the presence of one of its substrates.When enzyme solutions are heated, there is a progressive loss of catalytic activity over time due to denaturation of the enzyme. A solution of the enzyme hexokinase incubated at 450C lost 50% of its activity in 12 minutes, but when incubated at 450C in the presence of a very large concentration of one of its substrates, it lost only 3% of its activity in 12 minutes. Suggest why thermal denaturation of hexokinase was retarded in the presence of one substrates
- In the liver, fructose can be converted into glyceraldehyde 3- phosphate and dihydroxyacetone phosphate without passing through the phosphofructokinase-regulated reaction. Show the reactions that make this conversion possible. Why might ingesting high levels of fructose have deleterious physiological effects?Lithium ion inhibits the synthesis of inositol trisphosphate by inhibiting a reaction in the breakdown of inositol trisphosphate. Explain this apparent paradox.The mechanism of chymotrypsin is used as a model for studying enzyme reaction mechanisms. Answer the following questions related to chymotrypsin: 1. List the 3 amino acids in the catalytic triad of chymotrypsin. 2. List the types of catalytic mechanisms (from the 3 main types of catalytic mechanisms) displayed in the mechanism of chymotrypsin.