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Write a mechanism for the nonenzymatic transformation of glutamate semialdehyde into 1-pyrroline-5-carboxylate. Which amino acid is synthesized from 1-pyrroline-5-carboxylate in vivo? Write a mechanism for the nonenzymatic transformation of glutamate semialdehyde into 1-pyrroline-5-carboxylate. Which amino acid is synthesized from 1-pyrroline-5-carboxylate in vivo?

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11eab600_0803_23b7_9625_8fdbd0184057_TB6688_00 proline is synthesized from 1-pyrroline-5-carboxylate.

Draw the structure of the product formed when the substance shown below undergoes amide formation. Draw the structure of the product formed when the substance shown below undergoes amide formation.

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Which of the following is not an intermediate in the urea cycle?


A) arginine
B) citrulline
C) ornithine
D) lysine

E) B) and C)
F) A) and D)

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This many ATP equivalents are required to produce one molecule of urea from ammonia:


A) One ATP equivalent.
B) Two ATP equivalents.
C) Three ATP equivalents.
D) Four ATP equivalents.
E) Six ATP equivalents.

F) C) and D)
G) C) and E)

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C

The formation of amino acids from proteins


A) occurs during anabolism.
B) is endergonic.
C) occurs during digestion.
D) is a cellular process.
E) all of these

F) B) and D)
G) A) and E)

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The reaction, 2 NH4+ + α-ketoglutarate + NADPH + ATP → glutamine + NADP+ + ADP + Pi + H2O, is the combined result of what two enzymes?


A) nitrogenase and glutamate dehydrogenase (GDH)
B) GDH and glutamine synthetase (GS)
C) GS and nitrogenase
D) GDH and nitrogenase
E) all of these are correct

F) C) and E)
G) A) and E)

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The coenzyme pyridoxal phosphate (PLP) in its active form has all the following characteristics except:


A) It is covalently bonded to its enzyme.
B) It possesses a phosphate group.
C) It bonds to an amine group by means of the phosphate group.
D) All of these characteristics are true.
E) All of these characteristics are false.

F) D) and E)
G) A) and E)

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What amino acid is the following α-keto acid derived from? What amino acid is the following α-keto acid derived from?

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Suppose that the formation of a dipeptide is endergonic by +14.7 kJ/mol. If this reaction is coupled with the hydrolysis of ATP, will the net reaction be spontaneous or nonspontaneous? Explain your answer.

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The net reaction will be spontaneous since the ΔGnet value is −15.8 kJ/mol. This is based on coupling the endergonic reaction with a ΔG of +14.7 kJ/mol with the exergonic hydrolysis of ATP with a ΔG value of −30.5 kJ/mol. ΔGnet = −30.5 kJ/mol +14.7 kJ/mol = −15.8 kJ/mol.

In the process of amino acid biosynthesis, how are glutamic acid, glutamine, proline, and arginine all related?


A) They are all derived from α-ketoglutarate.
B) They are all derivatives of acetyl CoA.
C) They are all derivatives of pyruvate.
D) They are all derived from aspartate.
E) They are all derivatives of 3-phosphoglycerate.

F) A) and C)
G) A) and B)

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The key functional group in the PLP-dependent transamination of an α-amino acid is an activated


A) amine
B) imine
C) amide
D) enamine

E) B) and C)
F) A) and D)

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The following shows a part of the biosynthetic pathway of amino acids. If possible, draw an arrow to match the amino acid with its precursor. The following shows a part of the biosynthetic pathway of amino acids. If possible, draw an arrow to match the amino acid with its precursor.

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Glucogenic amino acids include all of the following, except:


A) Glycine
B) Alanine
C) Aspartic acid
D) Leucine
E) All of these amino acids are glucogenic.

F) C) and D)
G) B) and C)

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What product would be obtained from enzymatic transamination of 3-hydroxy-2-ketopropanoic acid? What product would be obtained from enzymatic transamination of 3-hydroxy-2-ketopropanoic acid?

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Consider the deamination of serine to answer the following questions. a)Draw the structure of the α-keto acid produced by the deamination of serine. b)What is the fate of the amino group in serine when this conversion occurs in a mammalian system?

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a) blured image b)The amino group is remov...

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What reaction does glutamate dehydrogenase (GDH) catalyze?


A) The oxidative deamination of glutamate to yield α-ketoglutarate.
B) Phosphorylation of carbamate to yield carbamoyl phosphate.
C) The amidation of the γ carboxyl group of glutamate to form glutamine.
D) The deadenylation of glutamine synthetase (GS) .
E) The adenylation of glutamine synthetase.

F) A) and B)
G) B) and D)

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Aspartate is formed from transamination of:


A) asparagine
B) aspartame
C) oxaloacetate
D) citrate
E) α-ketoglutarate

F) B) and C)
G) B) and E)

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3-Phosphoglycerate contains the carbon skeleton used to make


A) serine
B) cysteine
C) glycine
D) all of these

E) C) and D)
F) A) and D)

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Ornithine serves three metabolically important roles but is not found in proteins. Which of the following statements about ornithine is not true?


A) It is a precursor in the synthesis of citrulline.
B) It is an intermediate in the urea cycle.
C) It is a precursor in the synthesis of arginine.
D) It is biosynthesized from glutamine.
E) It is a product of arginine hydrolysis.

F) All of the above
G) None of the above

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Amino acids biosynthesized from aspartate include all except:


A) asparagine
B) threonine
C) methionine
D) lysine
E) glutamate

F) C) and D)
G) None of the above

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