Amino Acids Metabolism

Which disease is characterized by protein deficiency with adequate energy intake in children?

At what age does Marasmus commonly occur?

Which disease is associated with the preservation of subcutaneous fat?

In which disease is fatty liver enlarged?

Which classification of amino acids is based on the polarity of side chains?

What is a common feature of both Kwashiorkor and Marasmus diseases?

What is the primary pathway where extracellular, membrane-associated, and long-lived intracellular proteins are degraded?

What percentage of total body protein do humans turn over daily?

Which organelle contains proteases for proteins, lipases for lipids, and many other hydrolases involved in non-specific protein degradation?

What is the term used to express the relative susceptibility of a protein to degradation?

In which processes do increased lysosomal activity play a significant role?

What percentage of amino acids liberated by protein degradation are reutilized?

What is the primary enzyme involved in proteolytic digestion in the stomach?

During which situations must protein synthesis exceed protein degradation?

Which enzyme cleaves peptide chains mainly at the carboxyl side of lysine or arginine?

What is the function of elastase in protein digestion?

What is the optimal pH for pepsin, the primary enzyme in stomach digestion?

Which type of bonds does chymotrypsin preferentially hydrolyze in protein digestion?

What is the main cellular mechanism responsible for the degradation of regulatory proteins with short half-lives and abnormal proteins?

Which molecule is required for the attachment of Ub molecules to the target protein during ubiquitination?

How does the number of Ub molecules attached to a protein affect its degradation rate?

What type of bond is formed between the carboxyl terminal of Ub and lysyl residues in the target protein during ubiquitination?

Which amino acid residues at the amino terminus of a protein affect its rate of ubiquitination?

Where does the subsequent degradation of Ub-tagged proteins take place?

Which amino acid is primarily extracted by the liver in the postabsorptive state?

Which amino acid serves as a source of ammonia for excretion by the kidney?

Which amino acid is predominantly taken up by the brain from muscle in the postabsorptive state?

In the fed state after a protein-rich meal, which tissues release amino acids?

Which organ provides a major source of serine for uptake by peripheral tissues in humans?

What is the function of ubiquitin in eukaryotic cells?

Which amino acid residues at the amino terminus accelerate the ubiquitination of a protein?

What macromolecule is responsible for the degradation of Ub-tagged proteins in eukaryotic cells?

What is the energy requirement for the addition of Ub molecules to proteins during ubiquitination?

Which type of residues at the amino terminus of a protein retard its ubiquitination?

Which cellular organelle is responsible for the degradation of regulatory proteins with short half-lives?

What determines the rate of degradation of a protein with Ub molecules attached to it?

In which cellular compartment does the degradation of Ub-tagged proteins mainly occur?

Which enzyme is responsible for adding Ub molecules to proteins during ubiquitination?

What is the role of lysosomal enzymes in chronic inflammatory diseases such as rheumatoid arthritis?

What determines the rate of degradation of normal proteins with comparable functions?

Which amino acid residues at the amino terminus of a protein accelerate its ubiquitination?

What is the function of PEST sequences in proteins?

Where does the degradation of polyubiquitinated proteins occur?

Which type of protein degradation occurs for abnormal proteins?

What role do enzymes at important metabolic control points play in protein degradation?

What is the primary reason for the net balance of circulating plasma amino acids between meals?

Which residues in the N-terminal region of a protein retard its ubiquitination?