Essential Biochemistry - Protein Metabolism (Section 10)
1
Where does the majority of protein digestion occur?
2
What disease results from a deficiency in cystathionine beta-synthase?
3
Which of the following is involved in the regulation of blood pressure?
4
What enzyme is responsible for triggering the activation of trypsinogen?
5
What is the significance of hyperammonemia?
6
What is the precursor for synthesis of ornithine?
7
Which of the following compounds is involved in the synthesis of creatinine?
8
Which of the following is NOT an endopeptidase?
9
Which amino acid is directly converted to pyruvate?
10
Which of the following is the primary role of asparagine?
Answer(B)
As a building block for proteins.
11
What molecule accepts amino groups in most transamination reactions?
12
Which molecule is a common acceptor of amino groups in transamination reactions?
13
In the synthesis of cysteine from methionine, which molecules are involved?
14
What is the role of glutamate dehydrogenase in amino acid metabolism?
Answer(B)
Catalyzes the oxidative deamination of glutamate
15
Which of the following conditions leads to the accumulation of homocysteine in the blood?
16
Tetrahydrobiopterin is used as coenzyme in the metabolism of:
17
Which of the following amino acids is exclusively ketogenic?
18
Which of the following amino acids is a precursor to proline synthesis?
19
Which condition is characterized by a negative nitrogen balance?
20
What is the final product of oxidative deamination of amino acids?
21
What is the main waste product of amino acid catabolism that is excreted in urine?
22
What are the three stages of the complete catabolism of amino acids?
Answer(A)
Transamination, deamination, urea cycle
23
Which of the following is directly converted to pyruvate during amino acid metabolism?
24
What is the role of serine in purine and pyrimidine synthesis?
Answer(B)
It provides the carbon atoms.
25
Which amino acids can be converted to pyruvate?
26
What does the urea cycle yield?
27
What is the fate of glycine?
Answer(D)
It may be catabolized to yield formate, and CO2
28
Where does the urea cycle primarily occur?
29
The fate of ammonia in brain is:
30
When does a negative nitrogen balance typically happen?
31
In what form is ammonia transported in the blood?
32
Which of the following amino acids serves as a source for the synthesis of creatine?
33
Which of the following processes utilizes a one-carbon unit?
34
What is the role of the urea cycle?
35
Which of the following are glucogenic amino acids?
36
Which amino acid is converted to histamine?
37
What is the process known as transamination?
38
Which of the following is an example of an exopeptidase?
39
Which of the following amino acids is NOT metabolized by the transamination reaction?
40
Which of the following amino acid cannot undergo transamination?
41
What is the metabolic fate of aspartate?
Answer(B)
Transamination to form oxaloacetate
42
What is the main role of serine hydroxymethyltransferase?
Answer(B)
To transfer a one-carbon unit.
43
Which of the following statements is true regarding the urea cycle?
Answer(A)
It occurs exclusively in the liver.
44
Which of the following molecules are required for the urea cycle?
45
What is the primary function of asparaginase in cancer treatment?
Answer(B)
To deplete asparagine, starving cancer cells
46
Which of the following molecules directly participate in the first step of the urea cycle?
47
Which amino acid is primarily involved in the formation of collagen?
48
What's the major role of HCl during protein digestion in the stomach?
49
Cystinuria is due to defective carrier transport of which amino acids?
Answer(A)
Cysteine, arginine, lysine, and ornithine
50
What is the metabolic role of alanine?
Answer(A)
Involved in gluconeogenesis