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Questions and Answers
What is the first reaction of urea synthesis?
What is the first reaction of urea synthesis?
What is the cofactor of amino acid decarboxylases?
What is the cofactor of amino acid decarboxylases?
What is the biological role of amino acid decarboxylation in the human body?
What is the biological role of amino acid decarboxylation in the human body?
What is the main type of amino acid deamination in the human body?
What is the main type of amino acid deamination in the human body?
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Which vitamin derivative is a coenzyme of amino acid decarboxylases?
Which vitamin derivative is a coenzyme of amino acid decarboxylases?
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What is the cause of type I hyperammonemia?
What is the cause of type I hyperammonemia?
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In which metabolic pathway does urea synthesis occur?
In which metabolic pathway does urea synthesis occur?
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What is the result of a deficiency in the enzyme tyrosinase?
What is the result of a deficiency in the enzyme tyrosinase?
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What is the effect of histamine on blood vessels?
What is the effect of histamine on blood vessels?
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What is the condition characterized by the presence of acute pain in the joints, especially in the area of the big toe, and a large amount of uric acid in the blood and urine?
What is the condition characterized by the presence of acute pain in the joints, especially in the area of the big toe, and a large amount of uric acid in the blood and urine?
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What is the condition characterized by increased total acidity and free HCl in gastric juice?
What is the condition characterized by increased total acidity and free HCl in gastric juice?
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What is the process by which electrolytes, creatine, and albumin pass from the blood into the bile ducts?
What is the process by which electrolytes, creatine, and albumin pass from the blood into the bile ducts?
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Which reaction is common for the metabolism of carbohydrates, lipids, and proteins?
Which reaction is common for the metabolism of carbohydrates, lipids, and proteins?
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What intermediate substance connects the metabolism of proteins, carbohydrates, and lipids?
What intermediate substance connects the metabolism of proteins, carbohydrates, and lipids?
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Which amino acid deficiency can lead to fatty liver infiltration?
Which amino acid deficiency can lead to fatty liver infiltration?
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What is the common pathway of catabolism in the metabolism of proteins, carbohydrates, and lipids?
What is the common pathway of catabolism in the metabolism of proteins, carbohydrates, and lipids?
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In which metabolic pathway is ornithine cycle involved?
In which metabolic pathway is ornithine cycle involved?
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What is the biological role of transamination reactions?
What is the biological role of transamination reactions?
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Which enzyme is involved in the digestion of proteins in the stomach?
Which enzyme is involved in the digestion of proteins in the stomach?
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What is the disease that develops with homogentisate oxidase deficiency?
What is the disease that develops with homogentisate oxidase deficiency?
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What is the keto acid formed in the reaction catalyzed by AST?
What is the keto acid formed in the reaction catalyzed by AST?
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Which amino acid is involved in the synthesis of creatine?
Which amino acid is involved in the synthesis of creatine?
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What is the enzyme that catalyzes the transamination process?
What is the enzyme that catalyzes the transamination process?
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Determination of ALT activity is used for diagnosis of which disease?
Determination of ALT activity is used for diagnosis of which disease?
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Study Notes
Amino Acid Metabolism
- Amino acid deamination in the human body is mainly oxidative.
Urea Synthesis Cycle
- Ornithine carbamoyltransferase, argininosuccinate synthetase, and carbamoylphosphate synthetase are involved in the urea synthesis cycle.
- Asparagine is not involved in the urea synthesis cycle.
- The ornithine cycle is the main way of neutralizing ammonia in the body.
Amino Acid Decarboxylation
- Amino acid decarboxylation is an irreversible reaction in amino acid metabolism.
- The biological role of amino acid decarboxylation is the biosynthesis of biogenic amines.
- Pyridoxal phosphate is a cofactor of amino acid decarboxylases.
Amino Acid Metabolism Disorders
- Phenylketonuria is caused by the disruption of the transformation of phenylalanine to tyrosine.
- Albinism is caused by tyrosinase deficiency.
- Type I hyperammonemia is caused by a deficiency of carbamoylphosphate synthetase.
Uric Acid Metabolism
- Gout is characterized by the presence of uric acid in the blood and urine.
- Uric acid is formed through the breakdown of purine nucleotides.
Gastric Juice
- Hyperchlorhydria is characterized by an increase in total acidity and free HCl in gastric juice.
- Hypochlorhydria is characterized by a decrease in total acidity and free HCl in gastric juice.
Amino Acid Deficiencies
- Methionine deficiency can lead to fatty liver infiltration (hepatosis).
Metabolic Pathways
- Pyruvate is an intermediate substance that connects the metabolism of proteins, carbohydrates, and lipids.
- The common pathway of catabolism in the metabolism of proteins, carbohydrates, and lipids is the ornithine cycle.
Nitrogen Metabolism
- In the brain, ammonia is neutralized by the formation of asparagine and glutamine.
Creatine Synthesis
- Arginine is involved in the synthesis of creatine.
Amino Acid Diseases
- Alkaptonuria is caused by a deficiency of homogentisate oxidase.
Methylation Reactions
- S-adenosylmethionine is a universal donor of methyl groups.
Amino Acid Metabolism Enzymes
- Pepsin is involved in the digestion of proteins in the stomach.
- Alanine aminotransferase is an enzyme that catalyzes transamination processes.
Tissue Distribution of Enzymes
- The greatest ALT activity is observed in the liver.
- The greatest AST activity is observed in the heart.
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Description
Test your knowledge of amino acid deamination and the urea synthesis cycle in the human body. Identify the main type of amino acid deamination, the amino acid that undergoes direct oxidative deamination, and more.
