Group 7: Protein Metabolism Flashcards

1
Q

the process by which peptide bonds are broken under acidic conditions at high temperatures, generating free amino acid residues.

A

Protein Hydrolysis

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2
Q

a proteolytic enzyme found in the small intestine; hydrolyze peptide bonds.

A

Trypsin

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3
Q

Total supply of free amino acids available for use in the human body.

A

Amino Acid Pool

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4
Q

The repetitive process in which proteins are degraded and resynthesized within the human body

A

protein turnover

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5
Q

Is the state that results when the amount of nitrogen taken into the human body is equals to the amount of nitrogen excreted from the body in waste materials.

A

Nitrogen Balance

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6
Q

Indicates that large amount of tissues are being synthesized, such as during growth, pregnancy and convalescence from emaciating illness.

A

Positive Nitrogen Balance

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7
Q

Accompanies a state of tissue wasting due to protein-poor diets, starvation and wasting illnesses.

A

Negative Nitrogen Balance

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8
Q

The transfer of genetic instructions in DNA to mRNA in the nucleus.

A

Transcription

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9
Q

Takes place on ribosomes in the cell cytoplasm, where mRNA is read and translated into the string of amino acid chains that make up the synthesized protein.

A

Translation

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10
Q

When the ribosomes attach at a specific site of the mRNA. The ribosome starts matching tRNA anticodon sequences to the mRNA codon sequence.

A

Initiation

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11
Q

When a translating ribosome encounters one of the three universally conserved stop codons UAA, UAG or UGA.

A

Termination

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12
Q

An amino acid that has a carbon-containing degradation product that can be used to produce glucose via gluconogenesis.

A

GlucogenicAmino Acids

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13
Q

An amino acid that has a carbon-containing degradation product that can be used to produce ketone bodies.

A

Ketogenic Amino Acids

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14
Q

is a biochemical reaction that involves the interchange of the amino group of an a-amino acid with the keto group of an a-keto acid

A

Transamination Reaction

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15
Q

are organic compounds that contain both amino and carboxylic acid functional groups.

A

Amino acids

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16
Q

is an endopeptidase that breaks down proteins into smaller peptides.

17
Q

The site where the enzyme trypsin is active

A

Small intestine

18
Q

The site where large polypeptides are produced

19
Q

The site where protein is denatured by Hydrochloric Acid

20
Q

Active transport moves amino acids into the bloodstream.

A

Intestinal Lining

21
Q

The enzyme aminopeptidase is active.

A

Small intestine

22
Q

Peptide bonds are hydrolyzed by the enzyme pepsin.

23
Q

Individual Amino Acids are Produced

A

Small intestine

24
Q

The enzyme carboxypeptidase is active.

A

Small intestine

25
The enzyme glutamate dehydrogenase is active. a. Oxidation b. Oxidative deamination c. Transamination d. All of the Above
b. Oxidative deamination
26
Coenzyme pyridoxal phosphate is needed. a. Oxidation b. Oxidative deamination c. Transamination d. All of the Above
c. Transamination
27
One of the reactants is an amino acid, and one of the products is an amino acid. a. Degeneration b. Oxidative deamination c. Transamination d. None of the Above
c. Transamination
28
One of the reactants is a keto acid, and one of the products is a keto acid. a. Degeneration b. Oxidative deamination c. Transamination d. None of the Above
c. Transamination
29
Enzymes with a specificity toward alpha-ketoglutamateare often active. a. Transamination b. Oxidative deamination c. Both d. None of the Above
a. Transamination
30
An amino acid is converted into a keto acid with release of ammonium ion. a. Both a and b b. Oxidative deamination c. Transamination d. None of the Above
b. Oxidative deamination
31
NAD+ is used as an oxidizing agent. a. Both a and b b. Oxidative deamination c. Transamination d. None of the Above
b. Oxidative deamination
32
An aminotransferase is enzyme is active. a. Both a and b b. Oxidative deamination c. Transamination d. None of the Above
c. Transamination