Why does activation of the phosphorylated b form of glycogen synthase by high concentrations of glucose 6-phosphate make good biochemical sense?

Q: Identify the biochemical advantages that the glyoxylate cycle provides.

A: The glyoxylate cycle bypasses the decarboxylation steps of the citric acid cycle. where the…

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 is the metabolic role of aspartate transcarbamoylase?

A: Aspartate transcarbamoylase catalyzes the first biochemical reaction in pyrimidine biosynthesis. It…

Q: What is alpha keto glutarate dehydrogenase complex?. explain very briefly.

A: Tri carboxylic acid (TCA) cycle is an amphibolic pathway that means it involves both catabolic and…

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: Is it true that beta-ketoacyl-ACP-reductase catalyzes the committed stepn in fatty acid…

A: Beta-ketoacyl-ACP-reductase main function is to produce fatty acids of various lengths for use by…

Q: Phosphoglycerate kinase shows induced fit resulting from the binding of both substrates to form the…

A: Phosphoglycerate kinase is a glycolysis enzyme that catalyses the seventh reaction in the ten-step…

Q: How does the action of allosteric effectors differ in the reactions catalyzed by phosphofructokinase…

A: Allosteric effectors are the molecules that bind with one of the active sites of an enzyme that are…

Q: An inhibitor that specifically labels chymotrypsin at histidine 57 is Ntosylamido-l-phenylethyl…

A: Proteases are enzymes that can degrade other proteins. Serine proteases are a type of proteases that…

Q: Explain the biochemical consequences of Glucose-6-Phosphatase deficiency that results in gout due to…

A: The enzyme glucose-6-phosphatase regulates the release of glucose from glycogen stored in the liver.…

Q: An inhibitor that specifically labels chymotrypsin at histidine 57 is N-tosylamido-l-phenylethyl…

A: Trypsin is an enzyme that helps to digest protein. It breaks down the process of digestion that…

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: What Role Does Transition-State Stabilization Play inEnzyme Catalysis?

A: The enzymes are the protein molecules used to catalyze a chemical reaction by speeding up the rate…

Q: Pharmacokinetics of cyclophosphamide

A: Pharmacokinetics is the term which describes the process that what our body does to a drug when the…

Q: What is the evidence that aspartate transcarbamoylase (ATCase) effects catalysis primarily by…

A: Aspartate carbamyl transferase or astartate transcarbamoylase, transfers a carbamoyl group from…

Q: What is ornithine transcarbamylase (OTC)deficiency ?

A: Ornithine transcarbamylase (OTC)deficiency is a rare x linked recessive genetic disorder…

Q: N-Acetylglutamate is required as a cofactor in the synthesis of carbamoyl phosphate. How is…

A: Cofactors are non-protein part of the enzymes that helps in the catalytic activity during a…

Q: What two biochemical roles does CCK play? GLP-1?

A: Cholecystokinin (CCK) is a peptide hormone of the gastrointestinal system and is responsible for…

Q: Explain the biochemical and subsequent medical consequences of a deficiency of Myoadenylate…

A: Myoadenylate deaminase insufficiency is a metabolic muscle disorder in which the muscle cell's…

Q: Why does it make metabolic sense for UTP to inhibit carbamoyl phosphate synthetase II, whereas ATP…

A: Feedback inhibition is a cellular control mechanism in which the activity of the enzyme is inhibited…

Q: What is the logic behind high levels of arginine positivelyregulating N-acetylglutamate synthase?

A: The urea cycle is the biochemical reaction cycle that leads to the production of urea from ammonia…

Q: Draw the detailed mechanism of the transamination reaction in the active site of an…

A: Transamination reaction involves transfer of an amino group to a ketoacid to form new amino acids.…

Q: What is the rationale in using hexokinase and G6PD in the in the reverse reaction of Oliver-Rosalki?

A: Oliver rosalki method: The method of analysis of creatine kinase by measuring the Absorbance of NADH…

Q: What is the biochemical advantage of sigmoidal kinetics?

A: Allosteric enzymes are an exception to the Michaelis-Menton model because they have more than two…

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: Insulin dependent diabetes is often accompanied by high levels of triacylglycerols in the blood.…

A: Triglycerides are 3 esters of glycerol which was bound to three fatty acid molecules. where they are…

Q: In what way is the observed mode of action of hexokinase consistent with the induced-fit theory of…

A: In enzymology, allosteric regulation is the inhibition or activation of an enzyme by a small…

Q: Why is citrate an appropriate inhibitor of phosphofructokinase?

A: Citrate allosterically inhibits  phosphofructokinase by enhancing the inhibitory effect of ATP

Q: Why is gluconeogenesis labeled as enzymatic by-pass reactions?

A: Glucose is a central carbohydrate in body. It is the instant energy generating molecule. Whenever…

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: What role do low-barrier hydrogen bonds play in serine protease catalysis?

A: A low barrier hydrogen bond is a special type of hydrogen bond which can occur when the pKa of the…

Q: Using the principles described in the text regarding pyridoxal phosphate mechanisms, propose a…

A: Introduction: The exchange of an amino (- NH2) group from an amino acid to a keto acid is known as…

Q: . Propose a chemical mechanism for the reaction catalyzed by the PLP-dependent glatamate…

A: Glutamate-1-semialdehyde 2,1-aminomutase is an enzyme which belongs to the family isomerases;…

Q: Why is phenylketonuria resulting from dihydropteridine reductase deficiency a more serious disorder…

A: Phenylketonuria (PKU) is a rare genetic condition that causes an amino acid called phenylalanine to…

Q: What is the biochemical rationale for the use of creatine?

A: Creatine Phosphate has higher phosphoryl transfer potential as compared to ATP

Q: flow chart of purification steps of Beta-fructofruanosidase (Invertase)

A: β-fructofuranosidases are industrially employed due to ease of downstreaming processes(Purification…

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: Briefly outline the role of UDPG in glycogen biosynthesis.

A: Glycogen synthesis from glucose involves phosphorylation to form G6P, and isomerization to for G1P.…

Q: What is the biochemical rationale for ATP serving as a positive regulator of ATCase?

A: Introduction: The first step in the pyrimidine biosynthetic pathway is catalysed by aspartate…

Q: Galactose 1-phosphate: UDP-glucose uridyltransferase (GALT) is an enzyme important for the…

A: Galactose 1-phosphate: UDP-glucose uridyltransferase (GALT): GALT is an enzyme of the Leloir pathway…

Q: The mitochondrial form of carbamoyl phosphate synthetase is allosterically activated by…

A: The organelle mitochondria is known as one of the most crucial organelle in the cell because there…

Q: Is trimethoprim a mechanism-based inhibitor of bacterial dihydrofolate reductase?

A: DHFR the dihydrofolate reductase it is an enzyme that helps in purine synthesis.

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: Why Phenylmethylsulfonyl fluoride (PMSF, shown in Fig.) does not inhibit aspartate protease as…

A: The chemical compounds which are used to protect the proteins from the digestive function of the…

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: Briefly describe the induced-fit conformational change when hexokinase binds its substrate.

A: Hexokinase is considered as the catalytic enzyme, which is involved in the glycolysis process.

Metabolic pathways

Metabolism is defined as the group of life-supporting, enzyme-mediated chemical reactions in organisms. A metabolic pathway is a set of these chemical reactions that involve anabolism (synthesis of complex biomolecules) and catabolism (breakdown of biomolecules into small molecules) that occur inside a cell. Metabolites are the reacting substances, products, and intermediate substances of an enzymatic process that are altered by a series of chemical events catalyzed by enzymes.