Reaction mechanism for the transamination of alanine based on this figure

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: 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: 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: Write the mechanism (in detail) for the conversion of aspartate and carbamoyl phosphate into N -…

A: Aspartate carbamoyl transferase helps in the initial step of biosynthetic pathway of pyrimidine…

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: In acute lymphoblastic leukemia, the cancerous white blood cells typically lack the enzyme…

A: Acute lymphoblastic leukemia is a cancer present in the lymphoid line of blood cells, which is…

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: Figure 2 shows the structure of Diidopropylphosphofluoridate. Explain how this compound inhibits…

A: Enzymes are those molecules that increase the pace of the reaction without undergoing any change to…

Q: Describe how the concentrations of the four deoxyribonucleotides are balanced by ribonucleotide…

A: Introduction: Ribonucleotide reductase (RNR) is a key enzyme that mediates the synthesis of…

Q: One mechanism by which lead exerts its poisonous effect on enzymes can be stopped by chelation…

A: Lead act as poison by binding to different enzymes. Lead is soluble in water when it is present in…

Q: Write out a mechanism for the serine triad hydrolysis ofglycylglycine.

A: The dipeptide unit of glycine is glycylglycine. Serine proteases are a group of enzymes that contain…

Q: Certain glutamine analogs irreversibly inactivate enzymes that bind glutamine. Identify the…

A: Nucleotides are ubiquitous as they are involved in majority of biochemical reactions. All of the…

Q: Transamination reactions have been described as ping-pong reactions. Use the reaction of alanine…

A: Ping pong mechanism is a double displacement reaction where Enzyme binds with the substrate to form…

Q: Show the reaction mechanism for the catabolism of proline.

A: Proline plays an important role in metabolism and is being recognised as an important amino acid in…

Q: Pyridoxal phosphate acts as an intermediate carrier of amino groups during transamination reactions.…

A: Pyridoxal phosphate is the active form of Vit B6. It is a coenzyme in a variety of enzymatic…

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: 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: Why is the malate–aspartate shuttle system important for gluconeogenesis?

A: Malate aspartate shuttle or malate shuttle performs in the outerside membrane of mitochondria.

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: The peptide bond on the C=O side of bulky hydrophobic residues is cleaved by a) Trypsin b) RNase H…

A: Proteins are long-chain peptides formed of amide bonds (also known as peptide bonds) between the…

Q: All the following amino acids produce an intermediate of the TCA cycle except Isoleucine Leucine…

A: TCA cycle or tricarboxylic acid cycle also known as Krebs cycle operates in the mitochondria

Q: The Hatch–Slack pathway is an alternative name for _____________.

A: Photosynthesis is a biochemical process where light energy is converted into chemical energy in…

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: Explain the regulatory processes of purine synthesis that would result in an increase in the…

A: de novo synthesis of purine begins with simple starting materials such as amino acids and…

Q: What step ends the first-half of the chymotrypsin mechanism? Attack of water on the acyl-enzyme…

A: Chymotrypsin is a proteolytic enzyme secreted by the pancreases  in the small intestine.

Q: [ALPHABETICAL ORDER] Name all of 13 glucogenic amino acids that convert to an intermediate product.

A: Based on the type of intermediates that are formed during the catabolism of amino acids, they can be…

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: 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: 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: 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: What are the measures to inhibit the Maillard reaction in undesirable situations. please explain…

A: Maillard reaction is a type of chemical reaction in the field of Biochemistry. It occurs between a…

Q: The end products of tryptophan degradation are acetyl CoA and acetoacetyl CoA, yet tryptophan is a…

A: Introduction The catabolism of carbon skeletons of amino acids results in seven metabolic products.…

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: . 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: Figure 1 shows the catalytic triad of a-chymotrypsin. Identify A, B and C. Describe the subsequent…

A: Chymotrypsin comes under the family of serine proteases. Serine proteases include digestive enzymes…

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: 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: Neuraminidase (NA) catalyzes a hydrolysis of the glycosidic linkages of sialic acids using a…

A: Neuraminidase inhibitors are the class of drugs which block the neuraminidase enzyme.They are…

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: Discuss the mechanism of action of the enzyme chymotrypsin.

A: Chymotrypsin is a serine protease that catalyses hydrolytic reactions. It specifically hydrolyses…

Q: Explain why, glucose-6-phosphate will prefer to go via the pentose phosphate route. What additional…

A: Metabolism includes biosynthesis/ reduction (an anabolic process) and oxidation (catabolic…

Q: The purinosome contains enzymes that convert the serine hydroxymethylgroup to the formyl group of…

A: Purinisome is a multi-enzyme complex. It catalyzes the de novo purine nucleotide biosynthesis in the…

Q: The purinosome contains enzymes that convert the serine hydroxymethyl group to the formyl group of…

A: Purinosome refers to a multi-enzyme complex, which is involved in carrying out the purine…

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.

Pharmacokinetics

Pharmacokinetics is made up of two words: pharmakon means drug, and kinetics which means moving. Pharmacokinetics could be defined in simple words as the movement of drugs through the whole body and out of the body.