Leys Flashcards

(72 cards)

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
Synthesis and deposition of peptidoglycan
Target of several antibiotics (penicillin)
26
What surrounds some bacteria?
thick polysaccharide capsule
27
help bacteria stick to each other to form plaque on the surface of teeth.
Glugans of S. Mutans
28
Synthesis of biological compounds
Anabolism
29
Breakdown of compouds
catabolism
30
Main source of amino acids
Dietary protein
31
Storage form of amino acids
There is none
32
Where do mammals acquire most of their energy
Carbohydrates, fats and proteins
33
Most efficient but yields the lowest amount of energy
Carbohydrate breakdown
34
intermediate amount of energy, however nitrogen containing byproduct must be eliminated.
Protein
35
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.
Liver
36
Where do amino acids feed into other pathways
pyruvate, acetyl CoA, and TCA intermediates
37
Difference between amino acids and fatty acids
Amino acids are converted to pyruvate and then glucose. While fatty acids cannot
38
The first step in converting amino acids into glucose or other intermediates
Deamination
39
The most common mechanism for deamination
Transamination
40
Exchanges the amino group with the keto group on alpha- keto glutarate resulting in glutamic acid.
Transamination
41
Key intermediate in amino acid metabolism
Glutamate
42
Can be deaminated to give free ammonia
Glutamate
43
There is no net loss of nitrogen or ammonia during
transamination
44
Required amino acids in diet
Essential
45
Purpose of removing the amino group
Synthesize new nitrogen compounds or excreted as urea
46
Amino acid catabolism
removes amino group which incorporates carbon atoms for TCA cycle
47
Nitric oxide, hormones, neurotransmitters, nicotinamide, heme, creatin phosphate and nucleotides.
Major compounds that derive nitrogen from aa
48
Transaminase reactions are..
Reversible
49
Allows the inter-conversion between amino acids keeping their concentrations balanced.
Reversible reaction of transaminase
50
highly toxic to living organisms and must be eliminated safely
Ammonia
51
Where does conversion of ammonia to urea take place
Liver
52
Converts one molecule of free ammonia (from glutamic acid) and one amino group from aspartate into urea and fumarate.
Urea cycle
53
What is the connection between the urea cycle and the TCA cycle
Product of fumarate during the urea cycle
54
Used to transport nitrogen from peripheral tissues to the liver
Alanine
55
Converted to pyruvate with the nitrogen incorporated into urea.
Alanine
56
Facilitates that conversion of amino acids into glucose
The glucose-alanine cycle
57
Account for about 50% of amino acids released by muscle into the blood.
Alanine and glutamine
58
Where does the conversion of ammonia into carbamoyl phosphate occur
Mitochondria
59
What is the effect of lack of urea cycle activity
Death
60
Use of compound that react with amino groups and remove them from the body.
Treatment for urea cycle genetic defects
61
Can be metabolized into 3 carbon molecules that can be used to synthesize glucose
Glucogenic amino acids
62
Metabolized into 2 or 4 carbon structures.
Ketogenic amino acids
63
Disease causes by defects in amino acid metabolism
Maple syrup urine disease (MSUD), Phenylketouria, Albinism, Alkaptonuria
64
Inability to metabolize branch chain amino acids.
Maple syrup urine disease (MSUD)
65
Deficiency of phenylalanine hydroxylase that converts phenylalanine to tyrosine.
Phenylketonuria
66
Caused by other defects in aromatic amino acid metabolism.
Alkaptonuria (black urine disease) and Albinism
67
Black urine disese
Alkaptonuria
68
Decarboxylation of ornithine to make putrescine.
First step in polyamine syntheis
69
Rate-limiting step in polyamine synthesis and has been the target for a number of cancer drugs.
Ornithine decarboxylase (ODC)
70
Carbohydrate binding proteins that recognize and bind to specific glycans in a non-catalytic and reversible manner
Lectins
71
Rate limiting step for glycolysis
phosphofructokinase
72
Which enzyme catalyses the conversion of pyruvate to oxaloacetate?
Pyruvate carboxylase