Why the catalytic residue mutants of Glycoside hydrolase still remain a lot activity ?
Q: Glycogen phosphorylase is an example of an enzyme that is regulated both by allosteric control and…
A: The enzyme's noncovalent contact can also be used to promote or inhibit the activity of the enzyme.…
Q: Residue Asn 204 in the glucose binding site of hexokinase IV was mutated, in two separate…
A: Enzymes are protein molecules that increase the rate of reaction by decreasing the activation…
Q: Beginning with molecule Y shown above, determine the net ATP equivalents that would be required to…
A: Glycogenolysis is the process of conversion of glycogen synthesis, in which glucose molecules are…
Q: The KMof the enzyme for the substrate adenosine is 3 × 10ꟷ5M. The product inosine acts as an…
A: Given values in the question: Km of the enzyme for the substrate adenosine = 3 × 10-5 MKi of the…
Q: If isolated regulatory subunits and catalytic subunits of ATCase are mixed, the native enzyme is…
A: ATcase (Aspartate transcarbamoylase) is an allosteric enzyme. It is involved in regulation of…
Q: a molecule that lowers cholesterol levels in humans interacts with the enzyme HMA-COG reductase. how…
A: Statins are the molecules responsible for lowering the levels of total bad cholesterol,…
Q: Complex allosteric regulation of the aspartate transcarbamoylase reaction is significant because it…
A: Aspartate transcarbomylase (ATCase) catalyzes the first step in pyrimidine biosynthesis. Aspartate…
Q: Phenylketonuria can result from a mutation in the( PAH) Phenyl Alanine Hydroxylase gene.
A: Phenylketonuria is a genetic defect that is caused by the deficiency of phenylalanine hydroxylase…
Q: Why might the compound shown below acts as a transition state analog of phosphoenolpyruvate…
A: Transition state analogue are the molecules which is present transiently during biochemical…
Q: Serine Proteases, such as chymotrypsin, contain Ser/Asp/His as a catalytic triad (i.e. three…
A: Enzymes are a class of proteins except for ribozymes (class of RNA) that enhance the rate of…
Q: Briefly discuss why each of the three common forms of galactosemia involves impaired utilization of…
A: Galactosemia is defined as a disorder that affects the body processes a sugar called galactose in…
Q: List the components of the enzyme complex involved in the transition step and Simply describe…
A: Components of the enzyme complex :-
Q: the impact of phosphorylation of glycogen phosphorylase on its heterotropic regulation.
A: The impact of phosphorylation of gylcogen phosphorylase on its heterotropic regulation…
Q: What TYPE of inhibition is observed in the following: S E Competitive Non-competitive Uncompetitive…
A: Inhibition of enzyme may be irreversible or reversible
Q: (Part A) Coenzyme-dependent enzymes can catalyze the general transformations shown below. What would…
A: Cofactors are non-protein components that are required for activity of a protein enzyme. Prosthetic…
Q: Hexokinase is an important enzyme in the metabolism of glucose. If theconcentration of hexokinase in…
A: Hexokinase phosphorylates the glucose in glycolysis which was a rate-limiting step that regulates…
Q: Lysozyme is an antibacterial enzyme found in animals. Residues Asp 101 and Arg 114 are required…
A: Introduction- Lysozyme helps in catalyzation of binding energy where it catalysis the peptidoglycan…
Q: Compounds A4 and A5 are inhibitors of a hydrolytic enzyme that hydrolyses A1 into products A2 and…
A: The general reaction mechanism for hydrolysis of A1 to A2 & A3 is given below. 'R' indicates…
Q: Some archaebacteria produce an enzyme with two active sites: one catalyzes the dephosphorylation of…
A: Archaebacteria contains an enzyme Fructose-1,6-bisphosphate aldolase which is a bifunctional enzyme…
Q: Why is isomerization of Glc-6-P to Fruc-6-P important in glycsolysis? To regulate the pathway To…
A: Glycolysis is the series of metabolic reactions where glucose is breakdown into pyruvate. This helps…
Q: From the complete oxidation of glucose (glucose → 6CO2), how many total nucleotide triphosphates are…
A: Glucose is metabolized through the glycolytic pathway to yield energy in the form of ATP and NADH.…
Q: Briefly discuss the Glyoxylate Pathway
A: Aerobic metabolism is a set of three basic metabolic processes that occur in cells to generate…
Q: Studies at diff erent pH’s show that an enzyme has two catalytically important residues whose pKs…
A: The pKa or pK value is the negative base-10 logarithm of the acid-base dissociation constant (Ka) of…
Q: “Caspase” describes the catalytic activity of this enzyme. What amino acyl residue participates in…
A: Caspases are enzymes which mainly take part in programmed cell death. A part from that they also…
Q: Assume that you used malate dehydrogenase as the starting material for engineering this enzyme.…
A: It is given that Malate dehydrogenase catalyse the following reaction; Malate + FAD → Oxaloacetate +…
Q: The hexokinases are a class of enzymes that catalyze the ATP-dependent phosphorylation of hexoses…
A: Enzymes are the vital biological proteins molecules that speed up the rate of reaction taking place…
Q: Regulatory enzymes are crucial for the proper functioning and coordination of glycolysis and…
A: Introduction: Enzymes are the biological catalysts that increase the rate of a chemical reaction…
Q: Bovine chymotrypsinogen has a molecular mass of 25.6 kDa. Amino acid analysis shows that this enzyme…
A: Protein is a nitrogenous organic macromolecule that is necessary for human health. It is responsible…
Q: Glutamine affects the regulatory system for E. coli glutamine synthetase so as to promote the…
A: Glutamine : It is an alpha amino acid that is used in the biosynthesis of proteins. Its side chain…
Q: In class, I mentioned that fructose is metabolized differently in the liver compared to glucose.…
A: Cellular respiration It is a series of reactions through which not only the breakdown of nutrients…
Q: The enzyme ATCase (Aspartate TransCarbamoylase) catalyzes an early step in the synthesis of the…
A: Enzymes are proteins that play a major role as biochemical catalysts by sppeding up a chemical…
Q: The allosteric properties of aspartate transcarbamoylase have been discussed in detail in this…
A: Aspartate Transcarbamoylase (ATCase) is a regulatory enzyme that has different catalytic and…
Q: A histidine residue in the active site of aspartate transcarbamoylase is thought to be important in…
A: Histidine is an alpha-amino acid that is sometimes known as a semi-essential amino acid. It is…
Q: The enzyme aspartate transcarbamoylase catalyzes an early step in pyrimidine biosynthesis. The two…
A: Pyrimidine biosynthesis is the synthesis of pyrimidine nitrogen Cytidine which occurs inside the…
Q: RuBP carboxylase is by no means an ideal enzyme. Describe some of the problems with its active site…
A: Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) catalyses the inorganic CO2 incorporation…
Q: Suppose an enzyme needed a cysteine thiol (sulfhydryl) group for its catalytic activity, and…
A: Cysteine is a sulfur-containing amino acid. Cysteine side-chains interact with each other and make…
Q: Serine esterase contains a catalytic triad at its active site. Which amino acid in serine esterase…
A: Serine esterase contains three amino acids, His 57,Ser 195 and Asp 102.These three residues form a…
Q: Residue Asn 204 in the glucose binding site of hexokinase IV was mutated, in two separate…
A: Hexokinase is the enzyme that catalyses the Phosphorylation of glucose to Glucose 6 phosphate in…
Q: In order to function as an oxidative phosphorylation uncoupler (page 648), 2,4-dinitrophenol must…
A: Uncouplers such as DNP decreases the formation of high energy phosphate and stimulate oxygen…
Q: What are the amino acids of the catalytic triad of chymotrypsin? State the mode catalysis shown by…
A: To get the remaining sub-parts solved, please repost the complete question and mention the sub-parts…
Q: Is the statement during fatty acid biosynthesis, the product detaches from fatty acid synthase…
A: Fatty acid biosynthesis is the metabolic process that involves in synthesis of long-chain fatty acid…
Q: Enolase has a strict requirement for two Mg* ions in its active site. Propose a role for these ions…
A: Enolase is a catalytic protein that is a metalloenzyme and helps in the conversion of 2 phospho (PG)…
Q: Enolase has a strict requirement for two Mg2+ ions in its active site. Propose a role for these ions…
A: Enolase enzyme is also known as phosphopyruvate hydrotase. This enzyme plays an important role in…
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: The pKa for histidine is pKa = 6.1 while that for cysteine is pKa = 8.0 2. Assume that both…
A: Histidine and cysteine are catalytic groups present in the given enzyme. The pka for histidine is…
Q: There are 3 isozymes of aspartokinase, the first enzyme in the catabolism of aspartic acid, each…
A: Introduction Aspartate kinase or Aspartokinase is an enzyme that catalyzes the phosphorylation…
Q: Lysozyme residues Asp 101 and Arg 114 are required for effi cient catalysis, although they are…
A: Catalytic activity : It increases in the rate of a specific chemical reaction caused by an enzyme or…
Q: What TYPE of inhibition is observed in the following: S E S
A: A chemical that binds to an enzyme and inhibits its activity is known as an enzyme inhibitor.…
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- The sedimentation value of aspartate transcarbamoylase decreases when the enzyme switches to the R state. On the basis of the allosteric properties of the enzyme, explain why the sedimentation value decreases.Why might the compound shown below acts as a transition state analog of phosphoenolpyruvate carboxykinase. Explain. A drawing of a normal transition state for this enzyme is needed.Why might the compound shown below act as a transition state analog of phosphoglucose isomerase? A drawing of the normal transition state for this enzyme is needed.
- Why is triose phosphate isomerase considered to be catalytically perfect?“Caspase” describes the catalytic activity of this enzyme. What amino acyl residue participates in the catalytic mechanism? What substrate motif does caspase-8 recognize?In what way is the observed mode of action of hexokinase consistent with the induced-fit theory of enzyme action?
- can somone please List the components of the enzyme complex involved in the transition step and Simply describe what does each component does? 1. 2. 3. ect..In what type of catalysis does Lys345 engage during the very first step of enolase's reaction cycle? Explain, in your own words, specifically why and how Lys345 falls into the category you chose.Which fatty acid cannot undergo β-oxidation in principle, why? Write all the β-oxidation steps for the fatty acid that can undergo β-oxidation, including the cofactors and products.
- Dicyclohexylcarbodiimide (DCCD) is a reagent that reacts with Asp or Glu residues. Explain why the reaction of DCCD with the c subunits of F1F0-ATP ase blocks its ATP-synthesizing activity.Using the appropriate graph and table above, explain what the N426S mutation appears to be doing to the enzyme’s function. Discuss the kinetic parameter changes and their meaning in this context, not the structure of the enzyme, which was not given to you.The hexokinases are a class of enzymes that catalyze the ATP-dependent phosphorylation of hexoses (sugars with six carbons). The hexokinases will bind only D-hexose sugars and not their L-counterparts. In general terms, describe the features of enzyme structure that make this specificity possible.