19) Consider the table of allosteric effectors and their effect on the following metabolic processes.
Q: How does the action of allosteric effectors differ in the reactions catalyzed by phosphofructokinase…
A: Glycolysis is breakdown of glucose. It is a ten step enzymatic process. Phosphofructokinase is an…
Q: What are the three reactions catalyzed by PLP? Just name them.
A: Pyridoxal phosphate (PLP) refers to a coenzyme present in a variety of reactions and it is the…
Q: List two ways in which glutathione functions in red blood cells.
A: Glutathione is a tripeptide which means it is composed of three amino acids, namely- glycine,…
Q: Why might a general ATP-binding inhibitor be a bad idea? Was this a problem with the drug that was…
A: Background information about ATP ATP is chemically Adenosine-Tri-phosphate means it is formed of…
Q: Discuss the role of enzymes in metabolic regulation by describing the following mechanisms.…
A: An enzyme is a biocatalyst that increase the rate of biochemical reaction without itself being…
Q: What is the biochemical relevance of cori cycle
A: Introduction: The chemical reactions that occur within the living body for the production of energy…
Q: Many studies that have revealed important biochemical processes in human beings, including those…
A: Biomedical research is possible by the use of some particular model animals. There are important…
Q: Define the term Allosteric Modulation?
A: The word, Allosteric, is derived from the Greek language in which Allos meaning 'other' and stereos…
Q: Different Types of Regulation require by Catabolic and Anabolic Pathways?
A: Catabolic pathway: It refers to the series of reactions that requires degradation of complex…
Q: Determine the type of inhibition by AMP? Explain
A: Inhibitors are substances which inhibit the enzyme activity by binding to the active site or…
Q: Hydroxyurea has been shown to increase the expression of fetal hemoglobin in adult red blood cells,…
A: Sickle cell anemia is the disorder in which abnormality in oxygen carrying hemoglobin present in red…
Q: Describe the two models that explain the binding of allosteric enzymes. Use either model to explain…
A: The allosteric site is a site that allows molecules to either activate or inhibit the enzyme…
Q: What are the four necessary conditions that define the biochemical standard state?
A: A typical situation is an irrational situation set for something in order to create a standard…
Q: How does the "sequential" model, used to describe allosteric regulation, explain negative…
A: Allosteric regulation and negative cooperativity - Allosteric regulation of enzymes suggest that…
Q: What would be the effect on the reactions following the aconitase-catalyzed step?
A: Acetyl-CoA enters the TCA cycle to form citrate reacting with oxaloacetate. Citrate is a symmetrical…
Q: What two types of defensins contribute to the biochemical barrier?
A: Biochemical barriers are the chemical molecules synthesized within the body that act as a defence…
Q: Carbon monoxide competes with hemoglobin for 02 binding, resulting in toxicity. Is it possible that…
A: Aerobic cellular respiration, which needs oxygen, may provide energy. All of a live system's…
Q: Human blood serum contains a class of enzymes known as acid phosphatases, which hydrolyze biological…
A: The activity of an enzyme catalyzed reaction is the number of product molecules formed per unit time…
Q: Briefly explain what the "committed step" of a pathway is. Also explain why it makes sense for…
A: Hi! Thank you for the questions. As you have posted a question with multiple subparts, I will be…
Q: Which of the following regulators are said to act in cis?
A: The regulation of molecular biological processes is important. Poor controls on regulation lead to…
Q: BPC is a heterotropic allosteric modulator. in which way does this compound change the uptake and…
A: Hemoglobin is the protein in RBC and helps in the transport of oxygen via blood. Proper oxygen…
Q: Briefly describe the role of nucleophilic catalysis in the mechanism of the chymotrypsin reaction.
A: Chymotrypsin is the enzyme synthesized in the pancreas in the form of the inactive state known as…
Q: Deficiencies of the components of Complexes I, III, and IV tend to have severe physiological…
A: The complex I, II, III, IV, and V are the cytochrome complexes that are part of the oxidative…
Q: Human blood serum contains a class of enzymes known as acid phosphatases, which hydrolyze biological…
A: Enzymes are proteins that act as biological catalysts to accelerate chemical reactions inside the…
Q: Indicate which reactions of purine or pyrimidine metabolism are affected by the inhibitors (a)…
A: Purine are nitrogenous bases including adenine and guanine. Pyrimidine are nitrogenous bases…
Q: In heterotropic effectors, the allosteric effector may be different from the substrate?
A: Heterotopic allosteric effector is not a substrate .It is a regulatory molecule which can either…
Q: What would be the effect of adequate concentration of AMP andGMP?
A: AMP: Adenosine Monophosphate GMP: Guanosine Monophosphate
Q: Briefly explain the role of the oxyanion hole for the catalysis of chymotrypsin.
A: Chymotrypsin is a seine protease. Serine protease is a class of enzyme in which catalytic mechanism…
Q: 74. Given the photo shown below, which among the following choices may cause such?
A: Right after the meal, if the samples would have been taken, it would have been increased glucose and…
Q: Ibuprofen is an inhibitor of prostaglandin endoperoxide synthase. By inhibiting the synthesis of…
A: An enzyme inhibitor is a molecule that binds to an enzyme and decreases its activity. By binding to…
Q: Discuss the reaction catalyzed by helicases and key aspects of their mechanisms.
A: During the DNA replication, the two strands are separated with the help of motor protein and result…
Q: List three examples of commonly employed combination of ligand and protein in affinity chromat
A: Affinity chromatography is a specific type of technique in which proteins are purified in a highly…
Q: (a) What is the role of Glu 270 in catalysis? (b) What is the role of Arg 145 in catalysis?
A: The formation of enzyme-substrate complex is the first step of enzymatic catalysis. The enzyme first…
Q: Discuss the role of feedback inhibition in the anabolism ofpurine-containing nucleotides.
A: DNA and RNA are two different forms of nucleic acids, which are biological polymers of monomer units…
Q: what kind of catalysis is the oxygen on Ser 195 participating in?
A: Enzymes catalyze (i.e. speed up) chemical reactions occurring in the body. Most enzymes are proteins…
Q: . Using the principles described in the text regarding pyridoxal phos- phate mechanisms, propose a…
A: Introduction- Serine hydroxy methyltransferase (SHMT) is known as a pyridoxal phosphate-dependent…
Q: Explain the biochemical defect that leads to Lesch-Nyhan syndrome and suggest how the defect might…
A: Introduction: Purines (adenine and guanine) and pyrimidines (cytosine, thymine, and uracil) play…
Q: Write a balanced equation for the synthesis of phosphatidylethanolamine by the de novo pathway,…
A: Phospholipids are a class of lipids that consist of two fatty acyl molecules which are esterified at…
Q: Why does a phosphorylation/dephosphorylation system allow more sensitive regulation of a metabolic…
A: Enzymes catabolize metabolic processes. The enzymes are regulated in various ways: allosteric…
Q: Aspartate transcarbamoylase, which is necessary for CTP production, is an essential enzyme for the…
A: Enzymes are the biological catalysts that have the ability to increase the rate of metabolic…
Q: Describe the possible roles of allosteric modulation in theregulation of metabolic pathways.
A: Enzymes are proteins that act as a catalyst, speeding up chemical reactions without changing…
Q: 3. b. If chymotrypsin is treated with dilsopropylfluorophosphate, catalysis cannot occur even In the…
A: Chymotrypsin is a serine protease (digestive enzyme), secreted in pancreas and acts in the duodenum,…
Q: How does fructose-2,6- bisphosphate play a role as an allosteric effector?
A: A molecule that binds to an enzyme and causes allosteric effects is known as an "allosteric…
Q: Which of the following regulators are said to act in cis?
A: Cis-regulatory elements (CREs) are non-coding DNA regions that influence nearby gene transcription.…
Q: Chymotrypsin preferentially binds the transition state. What is meant by that?
A: Transition state is free energy maximum state. It is an intermediate stage of enzyme-catalyzed…
Q: What biochemical reaction is catalyzed by γ-secretase? Why was it proposed that a chemical inhibitor…
A: Enzymes are proteins with catalytic power.
Q: The synthesis of compound 6 proceeds via the metabolic pathway given below. Which enzyme is most…
A: Free enzymes bind with substrate and turn into products and finally are released from the product.…
Trending now
This is a popular solution!
Step by step
Solved in 3 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?The interconversion of DHAP and GAP greatly favors the formation of DHAP at equilibrium. Yet the conversion of DHAP by triose phosphate isomerase proceeds readily. WhyGlucokinase acts as a glucose sensor in hepatocytes (livercells), a- and b-cells in the pancreas, enterocytes (intestinalwall cells), and the hypothalamus (a control center in thebrain of numerous physiological processes). Explain whyglucokinase can perform this role.
- Predict which one of the five steps of the a-ketoglutarate dehydrogenase complex reaction is metabolically irreversible under physiological conditions and explain why.The Vmax of muscle glycogen phosphorylase is much larger than that of the liver enzyme. Discuss the functional signifi cance of this phenomenon.Following this experiment, you would like to elucidate the mechanism of action of pyruvatekinase. Unfortunately, the crystal structure of pyruvate kinase is not available, whichrequires the enzyme to be modelled based on the available three-dimensional structures ofrelated enzymes. Suggest a bioinformatics approach that can be conducted to perform thisstudy.
- 10a) Outline the mechanism for the conversion of alpha-ketoglutarate to succinyl-CoA which is catalyzed by alpha-ketoglutarate dehydrogenase. b) Of the five steps involved with this process, which would most likely be metabolically irreversible under physiological conditions?Von Gierke’s disease is also known as glycogen storage disease type I. Patients with von Gierke’s disease lackglucose 6-phosphatase activity. Two prominent symptoms of this disorder are fasting hypoglycemia and lactic acidosis (elevated lactate levels in the blood), especially during strenuous exercise. Explain why these symptoms occur. What chemical reaction does this enzyme catalyze? Which pathways involve this enzyme? Lacking thisthe enzyme will cause impairment of which pathways?• Pls consider what pathways are affected by Von Gierke’s disease. Include in your explanation involving Cori’s cycle. can you please do not write by your hand? I mean computer if you can. thank you“Glycolysis and Gluconeogenesis are effectively two sides of the same coin”. With theaid of a diagram/s, explain what this statement means by describing the reactions ofeach pathway and discussing their regulation.
- Discuss the metabolic control for HMG CoA reductase synthesis and activityDefine beta-oxidation of fatty acids? Describe in detail three different steps of beta-oxidation of FAs.Pharmaceuticals in a class called the statins inhibit theenzyme HMG-CoA reductase. What is the primary effect ofthis drug on patients?