Describe two types of regulation of the enzyme glutamine synthetase and explain why the regulation of this enzyme is soooo complex.

Q: Explain how the g-glutamyl cycle acts to transport aminoacids across a membrane. How does the…

A: Gamma-Glutamyl cycle is mainly a glutathione salvage pathway. It is an essential pathway for the…

Q: If ATP synthase completely stopped working, could glycolysis or the citric acid cycle still produce…

A: ATP synthase is part of the oxidative phosphorylation which oxidises the NADH and FADH2 to build the…

Q: rostaglandin-endoperoxide synthase 2, also known as cyclooxygenase- or COX-2, is an enzyme that in…

A: Prostaglandins directly act upon nerve endings to induce pain. They may also speed up the process of…

Q: Describe two different ways in which glucose oxidase is regulated. These mechanisms of regulation do…

A: Glucose oxidase: It is an oxidoreductase that catalyzes the conversion of glucose to hydrogen…

Q: Human xanthine oxidase catalyzes the oxidation of hypoxanthine to xanthine and can furthercatalyze…

A: Human xanthine oxidase is an enzyme that catalyzes the oxidation of hypoxanthine to xanthine 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: Explain the logic behind having [ADP] regulate the conversion of ribose-5-phosphate to PRPP. Does…

A: ADP is a nucleotide formed of adenine, ribose sugar, and two phosphate groups. Since adenine is a…

Q: Considering the gluconeogenesis that may occur after removal of the amino group from amino acids,…

A: Gluconeogenesis is the process of synthesis of glucose from pyruvate. This reaction runs backward of…

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: Serine Proteases, such as chymotrypsin, contain Ser/Asp/His as a catalytic triad (i.e. three…

A: The active site of enzymes are among the conserved regions of proteins. If evolution finds an active…

Q: Orotic aciduria results when one of the enzyme activities of UMP synthetase is absent. This syndrome…

A: Orotic aciduria is a hereditary disorder related to metabolism. Orotic aciduria is one of the…

Q: Snake venom contains many hydrolase enzymes, including several serine proteases. One such protease…

A: Enzymes are highly specialized proteins that have extraordinary catalytic power, greater than that…

Q: What is the smallest number of molecules of ATP and GTP consumed in the synthesis of a 200- residue…

A: ATP is adenosine triphosphate and is an organic compound. It is a hydrotrope that provides energy to…

Q: Describe the γ-glutamyl cycle. How many ATPs are required to synthesize glutathione from oxoproline?

A: γ-Glutamyl Cycle is glutathione salvage pathway, and is an essential pathway for the cell to…

Q: Explain the physiological role of transacetylase ?

A: Transacetylase is an enzyme that transfers an acetyl-CoA to galactosides and lactosides. It is coded…

Q: In this experiment, thearubigins were studied for their ability to inhibit the activity of amylase.…

A: Here i discuss about the questions regarding the experiment to check the amylase activity.

Q: The allosterically regulated enzyme ATCase binds aspartic acid as a substrate and acylates the…

A: Aspartate carbamoyltransferase(ATCase) is an enzyme that converts aspartate and carbamoyl phosphate…

Q: Diisopropylphosphofluoridate (DIPF) inactivates chymotrypsin by covalently modifying serine 195.…

A: Diisopropylphosphofluoridate (DIPF) is an irreversible inhibitor of chymotrypsin. It forms a…

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: 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: The interconverison of DHAP and GAP greatly favors the formation of DHAP at equilibirum. Yet the…

A: Enzymes are proteins that work as biological catalysts. Enzymes act on the molecules called…

Q: Why cant insulin serve as a allosteric activatior for the pyruvate dehydrogenase phospaphate enxyme…

A: The pyruvate dehydrogenase complex is consisting of three enzymes pyruvate dehydrogenase E1,…

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: During glycogen synthesis, glucose-1P is converted into a molecule called UDPG. This reaction also…

A: The glycogen synthesis takes place in animal tissues. The glycogen synthesis begins with glucose 6-…

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: Describe two different ways in which glucose oxidase is regulated.

A: Answer: - Glucose oxidase is a subset of oxidoreductase compounds that catalyzes the exchange of…

Q: Intramitochondrial ATP concentrations are about 5 mM, and phos- phate concentration is about 10 mM.…

A: ATP (Adenosine triphosphate) is the energy stored in the body which is produces as the result of…

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: Based on the data provided, are they going to authorize it as a medication or not? Explain?

A: Xanthine oxidase is responsible for the production of ROS (reactive oxygen species). It is involved…

Q: the structures of chymotrypsin and other serine proteases revealed that the active sites of these…

A: Chymotrypsin and trypsin are examples of serine proteases. Chymotrypsin cleaves the peptides of…

Q: Upon careful analysis, you discover that mutation causes the. patient's glucokinase to behave…

A: LB plot is called double reciprocal plot as it is plotted by taking inverse of substrate…

Q: Describe the mechanism of action of 1 cycle of the ubiquitin (Ub) ligase system. Describe how the…

A: Introduction  Proteins are the essential biomolecules that play a diverse role. Almost all cellular…

Q: From the complete oxidation of glucose (glucose  →  6CO2), how many total nucleotide triphosphates…

A: Glucose metabolism's major pathway is glycolysis. Which take place in both aerobic…

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: Human xanthine oxidase catalyzes the oxidation of hypoxanthine to xanthine and can further catalyze…

A: Human xanthine oxidase catalyzes the oxidation of hypoxanthine to xanthine and can further catalyze…

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: Compare the allosteric regulation of phosphorylase in the liver and in muscle, and explain the…

A: Phosphorylase are enzymes that catalyse the addition of a phosphate group from an inorganic…

Nitrogen metabolism

Nitrogen metabolism is the synthesis, utilization or uptake, breakdown, and excretion of nitrogenous compounds in the body. The nitrogen metabolism encompasses nitrogen fixation, biosynthesis, and the breakdown of amino acids, purines, and pyrimidine. Since nitrogen-containing compounds are required for various life processes, nitrogen is an important element of life.