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Biochem 2.0 > Protein Metabolism PPT > Flashcards

Protein Metabolism PPT Flashcards

1
Q

Not stored in the human body, they are constantly broken down into their constituent amino acids and then reused for protein synthesis.

A

Protein

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2
Q

Excess of this are not stored! but rapidly degraded for the synthesis of glucose (glycolosis) and lipids. Degradation of excess this causes an excess of nitrogen.

A

Degradation (Catabolism of AA)

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3
Q

Nitrogen excess is transformed into urea (80%) and ammonium (NH4 +) in order to be thrown away in the urine. (Liver and Blood)

A

Waste

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4
Q

Protein breakdown begins in the _______

A

stomach

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5
Q

No protein hydrolyzing enzymes are found in _______

A

saliva

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6
Q

Hydrolysis (10% of peptide bonds) & denaturization by _____ & ____ produce short chain polypeptides in the stomach.

A

pepsin enzyme & HCl acid

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7
Q

enzymes from pancreatic juices

A

Trypsin, chymotrypsin, & carboxypeptidase

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8
Q

also an from Pancreatic juices, it is from cells in the small intestine Brush Zone create “free” amino acids.

A

Aminopeptidase

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9
Q

Chemical digestion: it is produced in the pancreas

A

Pancreatic juice

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10
Q

2 pancreatic enzymes

A

Trypsin and Chymotrypsin

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11
Q

The total supply of free amino acids available is called

A

Amino Acid Pool

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12
Q

3 sources of “free” amino acids

A

Dietary protein breakdown
Biosynthesis of amino acids in the Liver
Protein turnover

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13
Q

is the breakdown & re-synthesis of body protein:
Old tissues
Damage
Recycling enzymes & hormones

A

Protein turnover

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14
Q

It’s in the mouth, it has no effect on digestion

A

Saliva

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15
Q

In the stomach, which denatures protein

A

HCl

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16
Q

It hydrolyzes peptide bonds

A

Pepsin

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17
Q

From large polypeptides to

A

oligopeptides

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18
Q

Amino acids in the small intestine

A

Trypsin, Chymotrypsin, Carboxypeptidase, Aminopeptidase

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19
Q

Dietary protein entering the stomach effects the release of the hormone _______ by stomach mucosa cells

A

gastrin

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20
Q

its antiseptic properties kill most bacteria

A

Hydrochloric acid

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21
Q

its denaturing action “unwinds” globular proteins, making peptide bonds more accessible to digestive enzymes

A

Hydrochloric acid

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22
Q

its acidity leads to the activation of pepsinogen, which is the inactive form of the digestive enzyme pepsin

A

Hydrochloric acid

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23
Q

Passage, in small batches, of the stomach’s acidic protein contents into the small intestine stimulates production of the hormone ________, which in turn stimulates pancreatic production of bicarbonate ion, HCO3, whose function is neutralization of gastric hydrochloric acid

A

secretin

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24
Q

secreted by intestinal mucosal cells, also attacks peptide bonds

A

Aminopeptidase

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25
Q

Pepsin, trypsin, chymotrypsin, carboxypeptidase, and aminopeptidase are all examples of

A

proteolytic enzymes

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26
Q

Two steps in degrading amino acids

A

1) remove α-amino group
2) breakdown & process carbon skeleton

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27
Q

Release of an amino group is also two steps:

A

1) Transamination
2) Oxidative deamination

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28
Q

Four amino acids of central role of glutamate:

A

glutamate, aspartate, alanine and glutamine

29
Q

present in mammalian cells at much higher concentrations than the other 16

A

glutamate, aspartate, alanine and glutamine

30
Q

function as excitatory neurotransmitters in the central nervous system, and glutamate is partly responsible for the flavour of food. (It is the mono sodium glutamate listed on processed food labels.)

A

Glutamate and aspartate

31
Q

occupies a special position in amino acid breakdown, and most of the nitrogen from dietary protein is ultimately excreted from the body via the glutamate pool.

A

glutamate

32
Q

present in higher concentrations in mammalian cells. Have metabolic functions as well as roles in proteins.

A

Glutamate, aspartate, alanine & glutamine

33
Q

Escapes in large amounts from dead or dying liver tissue. Measured in blood samples for diagnostic purposes

A

alanine aminotransferase

34
Q

Very active enzyme, exists in mitochondrial and cytosolic variants. The detailed iso-enzyme pattern is tissue-specific.

A

Glutamate: pyruvate transaminase [GPT]

35
Q

is the principal amino acid released from muscle tissue during starvation. It is an important substrate for hepatic gluconeogenesis

A

Alanine

36
Q

required for the proper maintenance of fasting blood glucose concentrations.

A

Alanine transamination

37
Q

very active enzyme inside heart cells. Also escapes in large amounts from dead or dying heart tissues & enters bloodstream. Measured in blood for diagnosing myocardial infarction.

A

aspartate aminotransferase

38
Q

It exists in mitochondrial and cytosolic variants, and the detailed iso enzyme pattern is tissue-specific. It escapes in large amounts from dead or dying tissues and enters the bloodstream, so it is often measured in blood samples for medical diagnostic purposes. The metabolic importance of this enzyme is that it brings about a free exchange of amino groups between glutamate (which is the most common amino acid) and aspartate which is a second major amino acid pool.

A

Glutamate: oxaloacetate transaminase [GOT]

39
Q

_______ and _______ are each required for separate but essential steps in the urea cycle, which is responsible for ammonia detoxication and nitrogen excretion.

A

Glutamate and aspartate

40
Q

Most transaminases share a common substrate and product (oxoglutarate and glutamate) with the enzyme __________

A

glutamate dehydrogenase

41
Q

has a central role in the overall control of nitrogen metabolism.

A

Glutamate

42
Q

The glutamate produced from the transamination step is then deaminated by __________ using the enzyme glutamate dehydrogenase

A

oxidative deamination

43
Q

Recycles back to a ketodiacid & releases ammonia

A

Oxidative Deamination

44
Q

will reversibly convert glutamate to α-ketoglutarate and α-ketoglutarate to glutamate.

A

Glutamate dehydrogenase [GluDH]

45
Q

Deamination reaction uses

A

NAD+

46
Q

reverse reaction uses

A

NADPH

47
Q

converting glutamate to α-ketoglutarate is an easily shifted equilibrium reaction.

A

Oxidative deamination

48
Q

building up favors the synthesis of excessive amounts of glutamate, decreasing the Krebs cycle intermediate α-ketoglutarate.

A

Ammonium ions

49
Q

What are the inputs to the urea cycle

A

NH3, CO2, and aspartic acid and fumaric acid

50
Q

__________ from the urea cycle enters the Krebs cycle

A

Fumarate

51
Q

________ produced from oxaloacetate of the Krebs cycle enters the urea cycle.

A

Aspartate

52
Q

takes off amine groups from amino acids and forms glutamate (ionized glutamic acid)

A

Transamination

53
Q

Amine groups form ________ when removed in deamination

A

ammonia

54
Q

Spiders excrete _______, 5 nitrogen atoms in a small molecule.

A

guanine

55
Q

Reptiles & birds excrete ______ – very insoluble purine compound – forms supersaturated solutions.

A

uric acid

56
Q

Transamination or Oxidative deamination both produce _________

A

α-keto acids

57
Q

Amino acid C skeletons that degrade to form a Krebs cycle intermediate can then be used to make glucose via gluconeogenesis. These are called:

A

Glucogenic Amino Acids

58
Q

Amino acid C skeletons that degrade to form acetyl CoA or Acetoacetyl CoA can form fatty acids or ketone bodies. These are called

A

Ketogenic Amino Acids.

59
Q

Use glycolysis intermediates:

A

3-phosphoglycerate & pyruvate

60
Q

Krebs cycle intermediates:

A

Oxaloacetate & α-ketoglutarate

61
Q

Defective phenylalanine hydroxylase – phenylalanine accumulates in body. Phenylalanine is transaminated to phenylpyruvate.

A

Phenylketonuria (PKU)

62
Q

Iron atom stored in a protein

A

ferritin

63
Q

degraded to bile pigments

A

Tetrapyrrole

64
Q

Central methylene bridge of Biliverdin is reduced creating _______.
It is found to be the major antioxidant in blood

A

Bilirubin

65
Q

_______ transported to liver. Becomes more water soluble with attachment of glucoronide sugars to propionate side chains

A

Bilirubin

66
Q

Intestinal bacteria help change Bilirubin into ______ and _______ for excretion.

A

Stercobilin and urobilin

67
Q

Changing color of a bruise shows dominant degradation product of heme: either _____ or _____

A

biliverdin or bilirubin

68
Q

when bilirubin accumulates in the blood. Spleen is degrading heme, but liver isn’t removing the product

A

Jaundice

69
Q

the Brain uses ______or _______bodies for fuel.

A

Glucose or Ketone

Biochem 2.0 (10 decks)

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