Azaserine inhibits amidotransferases. State the purine precursor that resembles azaserine. Which step in the purine biosynthetic pathway will be inhibited?
Q: How does chorismate mutase destabilize the ground state of its substrate?
A: Chorismate mutase It is an enzyme involved in shikimate pathway for the formation of phenylalanine…
Q: Draw in detail the pathway of de novo synthesis of deoxythymidine phosphate and provide a brief…
A: First carbamoyl phosphate is synthesized , which then enters the de-novo synthesis pathway for…
Q: . Most bacterial mutants that require isoleucine for growth also require valine. Why? Which enzyme…
A: A mutation is a permanent alteration in the sequence of nitrogenous bases of a DNA molecule.
Q: Define multiubiquitinylation.
A: In the cell, proteins are degraded or modified with the help of the ubiquitin pathway. In the cell,…
Q: Consider the pathway for catabolizing galactose. What are the potential control points for this…
A: Galactose is metabolized mainly in the liver, which is an important dietary sugar. Lactose gives…
Q: Explain why methotrexate inhibits the synthesis of histidine and methionine.
A: Competitive inhibition is the competition between a substrate and inhibitor that compete for the…
Q: Alkaptonuria is a rare organic aciduria involving a deficiency in homogentistic acid oxidase…
A: Alkaptonuria: It is a very rare metabolic disorder characterized by homogentisic acid accumulation…
Q: The enzyme chymotrypsin, catalyses the hydrolysis of nitrophenyl acetate and pther acyl esters. Name…
A: Chymotrypsin is a digestive enzyme belonging to a super family of enzymes called serine proteases.…
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: 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: What are the allosteric activators and inhibitors of de novo purine and pyramidine biosynthetic…
A: The allosteric regulation is also known as allosteric control. It is the regulation of the activity…
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: What are the biomolecules that are used to biosynthesize a purine ring in the de novo pathway –…
A: Purine synthesis occurs in liver by two pathways i.e denovo synthesis and salvage pathway. Denovo…
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: What are revision products? What type of reaction is it? What is the common intermediate reversion…
A: Carbohydrates are complex biomolecules made up of simple building units/monomers called sugars or…
Q: for GABA transaminase, ornithine decarboxylase, and alanine
A: PLP-dependent enzymes catalyse a wide range of reactions that result in bond cleavage at the carbons…
Q: Describe a common feature at the active site of serine proteases and acetyl cholinesterase
A: Acetylcholinesterase is an enzyme that catalyzes the hydrolysis of acetylcholine (which is a…
Q: After being stabilized with supplemental oxygen, a blood transfusion, and medication to help with…
A: Hydroxyurea: It is a class of antimetabolites. This class of drug is used to treat cancer. It is a…
Q: Explain why cleavage of the bond between arginine 15 and isoleucine 16 of chymotrypsinogen activates…
A: Enzymes are known as biological catalysts in which help to catalyze the different biochemical…
Q: Define the term thiolytic cleavage. In what biochemical process does it occur?
A: A reaction in which a bond to a sulfur atom is broken is known as the thiolytic cleavage. In the…
Q: The peptide Leu-Cys-Arg-Ser-Gln-Met is subjected to Edman degradation. After the first cycle of this…
A: Peptide refers to a chain of amino acids which contains about 2 to 50 amino acids. A peptide chain…
Q: Briefly discuss the synthesis of selenocysteine amino acid.
A: Selenocysteine(Sec): It is the 21 st amino acid of the genetic code and this amino acid contains…
Q: What cofactors are necessary for methyltransferases t Homocysteine Methionine o work?
A: Methyltransferases are primarily responsible for the transfer of methyl groups to other molecules.
Q: indicate at the structural level how 3TC works as a deoxycytosine analog, and why it is a chain…
A: The synthesis of a DNA molecule from the double stranded DNA template by the enzyme DNA polymerase…
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: Is liver catalase active within a narrow or broad ph ran
A: An enzyme is a molecule with speed up the rate of a biological reaction without being consumed in…
Q: Describe the nitrogenase complex. How is the enzymeorganized? What are its unique components?
A: Nitrogenase complex constitutes dinitrogenase reductase which is an iron-sulphur protein,…
Q: Reaction mechanism for the transamination of alanine based on this figure
A: Transamination is defined as the exchange of functional groups that happens between most amino acids…
Q: How is carbamoyl-phosphate synthetase I (CPS-I) controlled?
A: Introduction: The end product of the metabolism of amino acids is urea.
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: What is the action of deoxyribonuclease?
A: Deoxyribonucleases are one type of nuclease, a generic term for enzymes capable of hydrolyzing…
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: Explain the function of histidine 57 in the mechanism of chymotrypsin.
A: The function of Histidine 57 in the mechanism of chymotrypsin can be described in the following way:…
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: Which of the following is an example of an unacceptable missense?
A: Amino acids are organic compounds which contain amino group, carboxyl group and functional groups…
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: 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: The biosynthetic pathway for the two amino acides E and H is shown schematically in the Figure…
A: Feedback inhibition is a cellular control mechanism in which an enzyme's activity is inhibited by…
Q: Show the peptides that would result from cleavage by the indicated reagent: a.…
A: A peptide is a long chain of amino acids connected together via a peptide bond. Different peptides…
Q: Explain how the pKa for histidine 57 is important to its role in the mechanism of chymotrypsin…
A: Chymotrypsin is a digestive enzyme found in pancreatic juice that conducts proteolysis, or the…
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.
Q: What do carboxypeptidase andaminopeptidase have in common? Identify asmany differences between them…
A: Aminopeptidase and carboxypeptidase are the protease class of enzymes. Proteases hydrolyze the…
Q: Which biochemical processes might be affected by a deficiency of thiamine?
A: The normal function of the human body relies on proper nutrition which can be derived from vitamins…
Q: TWO of the following statements about Extended Spectrum ß-lactamases are CORRECT?
A: Numerous bacteria produce various enzymes and metabolites that are capable of making the bacteria…
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- Give full reaction for the synthesis of Cetirizine ?In a paragraph form, provide the experimental procedures in removal of the carbon dioxide present in the mechanism of reaction of protein that contain native serine residues by the reaction of oxazetidine-containing peptides and α-ketoacidHow would chymotrypsin's catalytic triad be affected by extremely low and extremely high pH values (assuming the rest of the protein remains intact)?
- In the pentose phosphate pathway reaction that produces subtrate used for nucleiuc acid synthesis, what are the substrates products, enzyme, and intermediate used for the mechanism?Name the anabolic pathway that synthesizes fatty acids.List the ketone bodies. Where are they synthesized and where are they used?