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Biochem > Leys > Flashcards

Leys Flashcards

1
Q

Two major complex carbohydrates

A

glycoproteins and proteoglycans.

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2
Q

proteins that contain short glycan (or sugar) chains.

A

Glycoproteins

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3
Q

usually about 3 to 15 sugars long and often highy branched. They do not have a repeating unit and usually contain about 10-15% carbohydrate by weight.

A

Glycan chains in glycoproteins

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4
Q

Found on the cell surface proteins, the ER and the golgi or they are secreted.

A

Glycoproteins

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5
Q
  1. assist in protein folding to the correct conformation,
  2. enhance protein solubility,
  3. stabilize the protein against denaturation,
  4. protect the protein from proteolytic degradation,
  5. target the protein to specific subcellular locations,
  6. serve as recognition signals for carbohydrate binding proteins (lectins).
A

Carbohydrates on glycoproteins

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6
Q

Major sugars found on proteins

A

Amino sugars, neutral sugars and acidic sugars

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7
Q

N-acetylglucosamine and N-acetlygalactosamine

A

Amino sugars

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8
Q

galactose, mannose and fucose

A

Neutral sugars

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9
Q

sialic acid (N-acetylneuraminic acid)

A

Acidic sugars

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10
Q

Contain as much as 50-60% sugars

A

Proteoglycans

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11
Q

long unbranched polymers than can contain hundreds of monosaccharides usually having a repeating disaccharide unit

A

Sugarchains

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12
Q

Two types of linakages of carbohydrates to proteins

A

N- linked & O- linked

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13
Q

linked where the sugar is attached to an asparagine

A

N

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14
Q

inked where the sugar is attached to a serine, threonine or hydroxylysine.

A

O

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15
Q

How many complex carbohydrates have been identified

A

More than 100

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16
Q

Core of complex carbohydrates

A

2 N-acetylglucosamines and 3 mannose residues

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17
Q

Do proteins have both N-linked and O-linked structures?

A

Yes

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18
Q

What do O link proteins attach

A

Serine, threonine, and hydroxylysine

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19
Q

What do cells use to make all other sugars

A

Glucose (NO non essential sugars)

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20
Q

Recognize carbohydrate signals on leukocytes.

A

Lectins on the surface of endothelial cells

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21
Q

Found on the surface of bacteria

A

Complex carbohydrates

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22
Q

Have a thick layer of peptidoglycan on their surface

A

Gram positive

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23
Q

Have a thin layer of peptidoglycan between two lipid bilayers.

A

Gram negative

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24
Q

Made up of the alternating co-polymers or N-acetylglucosamine (NAG) and N-acetylmuramic acid (NAM).

A

Carbohydrate portion of peptidoglycan

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25
Q

Synthesis and deposition of peptidoglycan

A

Target of several antibiotics (penicillin)

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26
Q

What surrounds some bacteria?

A

thick polysaccharide capsule

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27
Q

help bacteria stick to each other to form plaque on the surface of teeth.

A

Glugans of S. Mutans

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28
Q

Synthesis of biological compounds

A

Anabolism

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29
Q

Breakdown of compouds

A

catabolism

30
Q

Main source of amino acids

A

Dietary protein

31
Q

Storage form of amino acids

A

There is none

32
Q

Where do mammals acquire most of their energy

A

Carbohydrates, fats and proteins

33
Q

Most efficient but yields the lowest amount of energy

A

Carbohydrate breakdown

34
Q

intermediate amount of energy, however nitrogen containing byproduct must be eliminated.

A

Protein

35
Q

Synthesizes nonessential amino acids, removes and breaks down excess amino acids, removes ammonia from the blood and converts it to urea and makes other nitrogen-containing compounds.

A

Liver

36
Q

Where do amino acids feed into other pathways

A

pyruvate, acetyl CoA, and TCA intermediates

37
Q

Difference between amino acids and fatty acids

A

Amino acids are converted to pyruvate and then glucose. While fatty acids cannot

38
Q

The first step in converting amino acids into glucose or other intermediates

A

Deamination

39
Q

The most common mechanism for deamination

A

Transamination

40
Q

Exchanges the amino group with the keto group on alpha- keto glutarate resulting in glutamic acid.

A

Transamination

41
Q

Key intermediate in amino acid metabolism

A

Glutamate

42
Q

Can be deaminated to give free ammonia

A

Glutamate

43
Q

There is no net loss of nitrogen or ammonia during

A

transamination

44
Q

Required amino acids in diet

A

Essential

45
Q

Purpose of removing the amino group

A

Synthesize new nitrogen compounds or excreted as urea

46
Q

Amino acid catabolism

A

removes amino group which incorporates carbon atoms for TCA cycle

47
Q

Nitric oxide, hormones, neurotransmitters, nicotinamide, heme, creatin phosphate and nucleotides.

A

Major compounds that derive nitrogen from aa

48
Q

Transaminase reactions are..

A

Reversible

49
Q

Allows the inter-conversion between amino acids keeping their concentrations balanced.

A

Reversible reaction of transaminase

50
Q

highly toxic to living organisms and must be eliminated safely

A

Ammonia

51
Q

Where does conversion of ammonia to urea take place

A

Liver

52
Q

Converts one molecule of free ammonia (from glutamic acid) and one amino group from aspartate into urea and fumarate.

A

Urea cycle

53
Q

What is the connection between the urea cycle and the TCA cycle

A

Product of fumarate during the urea cycle

54
Q

Used to transport nitrogen from peripheral tissues to the liver

A

Alanine

55
Q

Converted to pyruvate with the nitrogen incorporated into urea.

A

Alanine

56
Q

Facilitates that conversion of amino acids into glucose

A

The glucose-alanine cycle

57
Q

Account for about 50% of amino acids released by muscle into the blood.

A

Alanine and glutamine

58
Q

Where does the conversion of ammonia into carbamoyl phosphate occur

A

Mitochondria

59
Q

What is the effect of lack of urea cycle activity

A

Death

60
Q

Use of compound that react with amino groups and remove them from the body.

A

Treatment for urea cycle genetic defects

61
Q

Can be metabolized into 3 carbon molecules that can be used to synthesize glucose

A

Glucogenic amino acids

62
Q

Metabolized into 2 or 4 carbon structures.

A

Ketogenic amino acids

63
Q

Disease causes by defects in amino acid metabolism

A

Maple syrup urine disease (MSUD), Phenylketouria, Albinism, Alkaptonuria

64
Q

Inability to metabolize branch chain amino acids.

A

Maple syrup urine disease (MSUD)

65
Q

Deficiency of phenylalanine hydroxylase that converts phenylalanine to tyrosine.

A

Phenylketonuria

66
Q

Caused by other defects in aromatic amino acid metabolism.

A

Alkaptonuria (black urine disease) and Albinism

67
Q

Black urine disese

A

Alkaptonuria

68
Q

Decarboxylation of ornithine to make putrescine.

A

First step in polyamine syntheis

69
Q

Rate-limiting step in polyamine synthesis and has been the target for a number of cancer drugs.

A

Ornithine decarboxylase (ODC)

70
Q

Carbohydrate binding proteins that recognize and bind to specific glycans in a non-catalytic and reversible manner

A

Lectins

71
Q

Rate limiting step for glycolysis

A

phosphofructokinase

72
Q

Which enzyme catalyses the conversion of pyruvate to oxaloacetate?

A

Pyruvate carboxylase

Biochem (2 decks)

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