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BIOCHEMISTRY LEC > Protein Denaturation > Flashcards

Protein Denaturation Flashcards

1
Q

Sum total of all the biochemical reactions

A

Metabolism

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2
Q

Large biochemical molecules → smaller ones

A

Catabolism

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3
Q

Small biochemical molecules → larger ones

A

Anabolism

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4
Q

interconversion of chemical compounds in the body

A

Metabolism

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5
Q

Another term for catabolism

A

“exergonic/exothermic”

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6
Q

Another term for anabolism

A

“endergonic/endothermic”

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7
Q

occurs at the “crossroads” of metabolism

A

Amphibolism

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8
Q

pathways taken by individual molecules, their interrelationships

A

Metabolism

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9
Q

Produce more energy than they consume, releasing the chemical energy stored in organic molecules

A

Catabolism

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10
Q

Consume more energy than they produce

A

Anabolism

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11
Q

Acts as links between the anabolic and catabolic pathways

A

Amphibolism

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12
Q

Release energy producing reducing equivalents via the respiratory chain

A

Catabolism

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13
Q

mechanisms that regulate the flow of metabolites through the pathways

A

Metabolism

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14
Q

Involving oxidative reactions

A

Catabolism

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15
Q

Consume more energy than they produce

A

Anabolism

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16
Q

Occurs in the mitochondria

A

Catabolism

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17
Q

Occurs in the endoplasmic reticulum

A

Anabolism

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18
Q

Amphibolism steps

A

1st
breaks down metabolites (proteins, fats and carbohydrates) into smaller molecules and

2nd
produces energy - then used to synthesize more complex molecules from simple ones

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19
Q

Term for protein → amino acid → new protein

A

Protein turnover/interconversion

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20
Q

Series of consecutive biochemical reactions that convert a starting material into an end product

A

Metabolic Pathway

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21
Q

Types of Metabolic Pathway

A

Linear
Cyclic
Branched

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22
Q

series of reactions generates a final product

A

Linear Metabolic Pathway

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23
Q

series of reactions regenerates the first reactant

A

Cyclic Metabolic Pathway

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24
Q

reacting molecule (reactant) that binds to the enzyme (complex formation)

A

Substrate

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25
Q

catalyzes the reaction by acting upon the given substrates

A

Enzyme

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26
Q

Produced when substrate binds to the enzyme
Intermediate reaction species that is /are formed

A

Product

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27
Q

required by enzymes to further exert catalytic activity an organic molecule

A

CoEnzyme

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28
Q

Another term for Product

A

(enzyme-substrate complex)

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29
Q

Glutamate + Water products

A

a-ketoglutarate + Ammonium

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30
Q

a-ketoglutarate + Ammonium substrate

A

Glutamate + Water products

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31
Q

Glutamate + Water enzyme

A

Glutamate Dehydrogenase

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32
Q

Glutamate Dehydrogenase coenzyme

A

NAD
(Nicotinamide adenine dinucleotide)

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33
Q

Central Metabolic Pathway Steps

A

Stage 1: Digestion and Hydrolysis
Stage 2: Degradation
Stage 3: Oxidation (citric acid cycle and electron transport)

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34
Q

Digestion and Hydrolysis Pathway

A

Large Molecules
↓
Smaller Molecules
↓
Blood Stream

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35
Q

Degradation Pathway

A

Molecules
↓
two- and three-carbon compounds

36
Q

Oxidation (citric acid cycle and electron transport) Pathway

A

Small molecules
↓
ATP

37
Q

proteins are degraded and resynthesized

A

Protein Turnover

38
Q

Uses of Amino Acids from Amino Acid Pool

A
  1. Protein synthesis
  2. Synthesis of non-protein nitrogen-containing compounds
  3. Synthesis of non-essential amino acids
  4. Production of energy
39
Q
  • 75% of the free amino acids;
    replace old tissue (protein turnover) and build new tissue (growth)
A

Protein synthesis

40
Q

Synthesis of non-protein nitrogen-containing compounds

A

purines and pyrimidines of nucleic acids,

the heme of hemoglobin,

neurotransmitters such as acetylcholine and serotonin,

hormones such as insulin

41
Q

Location where partial digestion by the enzyme pepsin and its acid

A

Stomach

42
Q

Location where further protein digestion by enzymes released by the organ

A

Pancreas

43
Q

Location where final digestion of protein to amino acids takes place mostly inside the cells of this organ

A

Small intestine

44
Q

Location where the amino acid absorbed into the portal wein and transported to this organ where they enter the general bloodstream

A

liver

45
Q

Location where dietary protein present in the feces

A

Anus

46
Q

Protein Digestion in the Stomach Chemical Reactions:

A

A. Protein denaturation
B. Protein hydrolysis

47
Q

breakdown of the tertiary and secondary structure of proteins to expose them

A

Protein denaturation

48
Q

Protein denaturation enzyme

A

Hydrochloric acid in gastric juice

49
Q

Hydrochloric acid in gastric juice pH

A

(pH 1.5 to 2.0)

50
Q

The cleaving into smaller peptide chains

A

Protein hydrolysis

51
Q

HCl Activates _________ to ___________:

A

zymogen pepsinogen to pepsin

52
Q

Pepsin affects hydrolysis of ________ of peptide bonds
in proteins

A

10%

53
Q

Digested protein by the stomach

A

chyme

54
Q

which cells produce HCl acid in the stomach

A

Parietal cells

55
Q

Breakdown of peptide bonds

A

Protein Digestion

56
Q

secreted by intestinal mucosal cells

A

Aminopeptidase

57
Q

Enzymes in pancreatic juice and neutralizes acidic chyme

A

Trypsin,
Chymotrypsin, and
Carboxypeptidase

58
Q

Trypsin, Chymotrypsin, and Carboxypeptidase pH

A

7.0 and 8.0

59
Q

Activated form Trypsinogen

A

Trypsin

60
Q

Activated form Chymotrypsinogen

A

Chymotrypsin

61
Q

Activates Trypsinogen

A

[Enteropeptidase]

62
Q

Activates Chymotrypsinogen

A

[Trypsin]

63
Q

Enzymes: that continue to break down proteins into
peptides

A

Trypsin,
Chymotrypsin,
Elastase

64
Q

Enzymes: splits off the amino acid at the carboxyl end of a
peptide

A

Carboxypeptidase

65
Q

Enzymes: cleaves off the amino acid at the amino end of a
peptide

A

Aminopeptidase

66
Q

Enzymes: splits dipeptides into single AA

A

Dipeptidase

67
Q

Digest terminal peptide bonds to release amino acids

A

Exopeptidase

68
Q

Types of exopeptidase

A

Aminopeptidase
Carboxypeptidase

69
Q

digest internal peptide bonds

A

Endopeptidase

70
Q

Connects small intestine to the liver

A

Portal vein

71
Q

amino acid to liver cell through ATP

A

Active transport

72
Q

Involves only the shuffling of amino groups among the amino acids

A

Transamination

73
Q

Protein Degradation: Chemical reactions

A

Transamination
Oxidative Deamination

74
Q

Removal of the α-amino groups – 1st step in the catabolism of most L-amino acids (liver)

A

Protein Degradation

75
Q

Protein Degradation Mechanism:

A

transfer of an amino (NH2) group from an amino acid to a keto acid

76
Q

Protein Degradation Enzyme:

A

aminotransferases or transaminases

77
Q

Most amino acid product in transaminase

A

L-glutamate

78
Q

Protein Degradation Purpose:

A

to collect the amino groups from many different amino acids in the form of L-glutamate:

o functions as an amino group donor for biosynthetic pathways or for excretion pathways → elimination of nitrogenous waste products

o Cells contain different types of aminotransferases

79
Q

Intermediate carrier of amino groups at the active site of aminotransferases

A

Prosthetic group

80
Q

Coenzyme form of pyridoxine, or vitamin B6

A

Pyridoxal phosphate

81
Q

α-amino acid is converted → α - keto acid (used for a variety of reactions, including energy generation) with release of an ammonium ion

A

Oxidative Deamination

82
Q

Occurs primarily in liver (hepatocytes) and kidney mitochondria and 2nd step of amino acid degradation

A

Oxidative Deamination

83
Q

Oxidative Deamination Mechanism:

A

ammonium ion (NH4) is liberated from the glutamate formed by transamination

84
Q

Oxidative Deamination Enzyme:

A

L-glutamate dehydrogenase

85
Q

Oxidative Deamination Purpose:

A

amino group of L-glutamate molecules must be removed from glutamate to prepare them for excretion

86
Q

amino acids that can become glutamate

A

Arginine
Histidine
Proline
Glutamine

87
Q

Glutamate turn to ___________ by glutamate dehydrogenase

A

α - ketoglutarate

BIOCHEMISTRY LEC (6 decks)

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