BIOCHEM-ACHIEVE(FIRST DAY DISCOUNTED)
9th Edition
ISBN: 2818000069358
Author: BERG
Publisher: MAC HIGHER
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Question
Chapter 23, Problem 30P
Interpretation Introduction
Interpretation:
The way by which Argininosuccinic aciduria can be treated should be determined.
Concept introduction:
The urea cycle is a series of biochemical reactions which involve the formation of urea (NH2)2CO from the ammonia (NH3). It is also known as the ornithine cycle. It helps in the excretion of toxic ammonia by converting into urea. This cycle takes place in ureotelic organisms. Argininosuccinase or argininosuccinate lyase or ASL is an enzyme which catalyzes the reversible breakdown of argininosuccinate and produces arginine and fumarate.
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Explain why the symptoms of a partial defi ciency in a urea cycle enzyme can be attenuated by a low-protein diet.
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Chapter 23 Solutions
BIOCHEM-ACHIEVE(FIRST DAY DISCOUNTED)
Ch. 23 - Prob. 1PCh. 23 - Prob. 2PCh. 23 - Prob. 3PCh. 23 - Prob. 4PCh. 23 - Prob. 5PCh. 23 - Prob. 6PCh. 23 - Prob. 7PCh. 23 - Prob. 8PCh. 23 - Prob. 9PCh. 23 - Prob. 10P
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- explain the phenylketonuria disease mechanismarrow_forwardConsider this mechanism of enzyme action: Urease can catalyze the hydrolysis of Urea, H,N – C – NH, II but not H H the hydrolysis of diethyl urea N -C - C;H5 C2H5 Explain this action.arrow_forwardArgininosuccinic aciduria is a condition that results when the urea-cycle enzyme argininosuccinase is deficient. Argininosuccinate is present in the blood and urine. Suggest how this condition might be treated while still removing nitrogen from the body.arrow_forward
- Phenylketonuria. Clinical manifestations of pathology. Congenital enzyme defect.arrow_forwardProduction of the enzymes that catalyze the reactions of the urea cycle can increase or decrease according to the metabolic needs of the organism. High levels of these enzymes are associated with high-protein diets as well as starvation. Explain this apparent paradox.arrow_forwardSome amino acids are both glucogenic and ketogenic. Explain the difference between the two types and why some amino acids can be both.arrow_forward
- Including the carbamoyl phosphate synthetase step (CPS I) and the four steps of the urea cycle, how many ATP equivalents (phosphoanhydride bonds) are utilized to drive the formation of one urea molecule?arrow_forwardIn the majority of cases, amino acid catabolism can be broken down into a two-stepprocess; ‘transamination’ followed by ‘oxidative deamination’. Serine doesn’t followthis two-step process; fully explain the reaction and mechanism involved in thedegradation process used to form its α-keto acid.arrow_forwardDiscuss the two roles of N-acetylglutamate in the urea cycle. Include relevant chemical structures and reactions. What is the regulatory function of N-acetylglutamate in the urea cycle? What is the other role of N-acetylglutamate in relationship to the urea cycle? Glutamate is the precursor for N-acetylglutamate. How is glutamate involved in the connection between the urea cycle and the CAC?arrow_forward
- Explain why the amino acid tryptophan is both ketogenicand glucogenic.arrow_forwardHomocystinuria is caused by a defect in cystathionine beta-synthase (or 13-synthase), which leads to an accumulation of homocysteine in the blood. This accumulation causes symptoms such as a tall, thin frame, flushed cheeks, and osteoporosis (thinning of the bones). These individuals should limit their intake of proteins that contain methionine, such as egg whites. Using your understanding of biochemistry, explain why people with Homocystinuria should not consume egg whites and other such proteins.arrow_forwardWhat is phenylketonuria? Discuss its occurrence, symptoms if any, treatments if there are, and any prohibitions in the dietarrow_forward
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