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Biochem > problem set 9 > Flashcards

problem set 9 Flashcards

1
Q

anticoagulant

A
  1. aspirin
  2. large doses of vitamin E
  3. Coumadin
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2
Q

what is the anticoagulant found in small quantities in the blood

A

heparin

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3
Q

what is the formation of a clot within a blood vessel

A

thrombsis

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4
Q

what is it called if the clot breaks loose and moves elsewhere

A

embolism

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5
Q

Prothrombin, fibrinogen, and pepsinogen are examples of

A

zymogen

proenzyme

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6
Q

it is an anti-coagulant because it complexes Ca2+, which is needed for blood clotting

A

oxalate

citrate

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7
Q

what is the inactive enzyme that is the precursor to the peptidase found in the stomach

A

pepsinogen

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8
Q

any metal that is required for enzyme activity is called

A

cofactor

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9
Q

specific area on the enzyme where the chemical reaction takes place

A

catalytic site

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10
Q

specific area on the enzyme where the substrate binds

A

contact site

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11
Q

what is the cofactors plus the protein part called

A

holoenzyme

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12
Q

what is the cofactor that is organic but not a protein called

A

coenzyme

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13
Q

what peptidase has an optimum pH range near 2

A

pepsin

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14
Q

what peptidase is found in the small intestine

A

trypsin

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15
Q

what is the inactive protein part (without cofactors) of an enzyme called

A

Apoenzyme

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16
Q

what is the largest protein found in blood plasma, its function is blood coagulation

A

fibrinogen

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17
Q

different forms of an enzyme that catalyze the same reaction in different organs and tissues of the body is called

A

isoenzyme

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18
Q

what vitamin is needed for the synthesis of collagen

A

vitamin C

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19
Q

if a blood test taken in the emergency room indicates a high level of LDH and CK enzymes, what could be the cause

A

heart attack

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20
Q

Thiamine: coenzyme

A

TPP

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21
Q

Riboflavin: coenzyme

A

FAD

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22
Q

Niacin: coenzyme

A

NAD

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23
Q

Folic Acid: coenzyme

A

THF

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24
Q

Pantothenic acid:coenzyme

A

Coenzyme

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25
Q

TRUE about general zymogens

A
  1. they usually have their catalytic site blocked by several amino acids
  2. several blood clotting enzymes are synthesized as zymogens
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26
Q

FALSE about general zymogens

A
  1. catalytic activity
  2. usually smaller than active enzyme
  3. important for the enzymes needed for carbohydrate metabolism
  4. they are sometimes called apoenzymes
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27
Q

TRUE plasma proteins

A
  1. they are mainly made in the liver

2. serum albumins help maintain osmotic pressure

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28
Q

FALSE plasma proteins

A
  1. in times of protein deprivation they will be metabolized before muscle protein
  2. there are only four plasma proteins
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29
Q

enzymes are held together by…

A
  1. hydrogen bonds

2. salt bridges

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30
Q

what happens to the rate of an enzyme catalyzed reaction as substrate concentration is raised beyond the saturation point
(enzyme concentration remains constant)

A

remains the same

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31
Q

NOT peptidases

a. pepsin
b. plasmin
c. amylase
d. trypsin
e. thrombin

A

c. amylase

e. thrombin

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32
Q

TRUE concerning trypsinogen and trypsin

a. trypsin is a protein while trypsinogen is not
b. trypsin is larger protein than trypsinogen
c. trypsin has catalytic ability while trypsinogen does not
d. both have catalytic ability but not for the same substrate

A

c. trypsin has catalytic ability while trypsinogen does not

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33
Q

if an enzyme’s turn over rate is very high, it is

A

very efficient

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34
Q

which is found in blood plasma but not in blood serum

A

fibrinogen

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35
Q

calcium ions are needed for __ to be converted into ___

A

prothrombin –> thrombin

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36
Q

what compound causes the conversion of fibrinogen to fibrin

A

thrombin

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37
Q

what is the actual blood clot

A

fibrin

38
Q

what destroys the blood clot after it is no longer needed

A

plasmin

39
Q

what is the inactive precursor of thrombin

A

prothrombin

40
Q

what two things are necessary for the precursor (prothrombin) to be converted to thrombin

A
  1. calcium ions

2. thromboplastin

41
Q

enzyme (given to patient after a heart attack) which is used to convert plasminogen to plasmin

A

streptokinase

42
Q

where would you find covalent bonding

A
  1. disulfide bonds
  2. irreversible inhibition
  3. peptide bond
  4. amide bond
43
Q

why can enzymes be used in diagnostic medicine

A
  1. normally, blood plasma contains very small amounts of enzymes
  2. the same enzyme might have slight structural differences depending upon what type of tissue it is in
  3. tissue damage can cause enzymes to leak into the blood
  4. computerized assay procedures can measure very small quantities of enzymes
44
Q

TRUE concerning enzymes vs. hormones

A
  1. all enzymes are proteins, while some hormones are proteins
  2. low concentrations of either can have a dramatic effect
  3. hormones can be made in a gland and travel through the blood stream
  4. enzymes are used in the cells where they are made
45
Q

factors affecting the activity of all enzymes

A
  1. pH
  2. temperature
  3. substrate saturation
  4. genetic control to increase the concentration of the enzyme
46
Q

catalytically active

A

holoenzyme

47
Q

TRUE pepsin and pepsinogen

A

pepsin has catalytic ability while pepsinogen does not

48
Q

part of the enzyme most likely to be deactivated by temperature

A

apoenzyme

49
Q

what compounds react with hyrolase enzymes in the body

A
  1. fat
  2. polysaccharides
  3. corn oils
  4. tetrapeptide
  5. ethyl acetate
50
Q

true of noncompetitive inhibitors

A

a. Mercury poisoning is an example
b. inhibitor has a different binding site than the substrate
c. binding the inhibitor alters the 3-D shape of the enzyme
d. allosteric enzymes inhibitors are examples

51
Q

lactose

A

substrate

52
Q

maltase

A

enzyme

53
Q

maleate isomerase

A

enzyme

54
Q

alanine

A

substrate

55
Q

urease

A

enzyme

56
Q

tyrosine synthetase

A

enzyme

57
Q

glutamic acid

A

substrate

58
Q

Allosteric enzymes TRUE

A

a. they are affected by regulator molecules, which can be inhibitors or activators
b. usually 2 or more subunits, with one unit having the active site, and the other having a regulatory site
c. can be reversed by adding more substrate
d. some allosteric enzymes have several different sites for different regulator molecules

59
Q

false allosteric enzymes

A
  1. allosteric enzymes can cause build up of metabolic products
60
Q

true competitive inhibitors

A

a. inhibitors resembles the substrate
b. can be reversed by adding more substrate
c. an example is ethanol as an antidote for methanol poisoning
d. sulfa drugs are an example

61
Q

false competitive inhibitors

A
  1. binds at different site than the substrate

2. allosteric enzyme inhibitors are an example

62
Q

what type of enzyme would be synthezied first as a zymogen

A
  1. protein digesting enzymes

2. blood clotting enzymes

63
Q

what causes permanent enzyme denaturing

A

a. very high temperatures

b. large pH changes

64
Q

TRUE acetylcholine

A
  1. contains ester linkage
  2. deficiency in the brain is involved in Alzheimer
  3. it is a neurotransmitter
  4. a molecule that blocks its receptor site can be used as a muscle relaxant
65
Q

TRUE nerve gas

A
  1. it forms a permanent covalent bond with an amino acid at the active site
  2. it can cause convulsions and death
  3. it affects the enzyme acetylcholine esterase
66
Q

can be reversed by adding an excess of the substrate

A

competitive

67
Q

which usually forms covalent bonds with the enzyme

A

irreversible

68
Q

inhibitors look like the substrate

A

competitive

69
Q

lead poisoning destroys the salt bridges of many enzymes, but it can be removed with EDTA
–lead poisoning is what kind of inhibitor

A

non-competitive

70
Q

inhibitor binds to enzyme at different site than substrate, but it can be removed

A

non-competitive

71
Q

nerve gas permanently binds to serine in the active sites

A

irreversible

72
Q

antifreeze (ethylene glycol) is oxidized in the liver to oxalic acid, which is toxic. The treatment of antifreeze poisoning is intravenous solution of ethanol. what kind of inhibitor is ethanol to the liver enzyme

A

competitive

73
Q

olive oil to glycerol & 3 fatty acids

A

hydrolases

74
Q

cis 2-pentene to trans 2-pentene

A

isomerases

75
Q

glucose-6-phosphate & ADP to glucose & ATP

A

transferases

76
Q

isocitrate dehydrogenase

A

oxidoreductases

77
Q

petidases

A

hydrolases

78
Q

phosphoglucomutase

A

isomerases

79
Q

glucose-6-phosphate to fructose-6-phosphate

A

isomerases

80
Q

oxaloacetate & acetyl-CoA to citric acid

A

ligases

81
Q

transfers an amino group from aspartic acid

A

transferases

82
Q

hydrolyzes sucrose

A

hydrolases

83
Q

removes CO2 from pyruvic acid

A

lyases

84
Q

citric acid sythetase

A

ligases

85
Q

oxidizes succinic acid

A

oxidoreductases

86
Q

phosphoglycerate kinase

A

transferases

87
Q

glutamic-pyruvic transaminase

A

transferases

88
Q

lactose to glucose and galactose

A

hydrolases

89
Q

pyruvate decarboxylase

A

lyases

90
Q

amylose to glucose

A

hydrolases

91
Q

removes 2H from an alcohol

A

oxidoreductases

Biochem (27 decks)

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