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bmsc 200 > enzymes > Flashcards

enzymes Flashcards

1
Q

Enzyme associating inorganic ion (metals) to function

A

Cofactor

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2
Q

Enzyme associating complex organic molecules like vitamins to function

A

Coenzyme

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3
Q

Tightly associated cofactor or coenzyme

A

Prosthetic group

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4
Q

belief that living things are fundamentally different
from non-living things because the contain some non-physical element
or are governed by different principles that inanimate objects.

A

Vitalism

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5
Q

meaning “in yeast”, these are proteins that catalyze reactions

A

enzymes

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6
Q

used to pre-digest proteins during manufacture of baby food, used together with lipase in bio detergents to break down stains

A

protease

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7
Q

bio detergents to digest stains

A

lipase

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8
Q

50% drug research on this type of enzyme, for treatment of cancer and such

A

kinase (inhibitors)

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9
Q

protein portion of an anzyme, inactive by itself

A

apoenzyme

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10
Q

apoenzyme+coenzyme/factor=

A

holoenzyme

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11
Q

lower threshold energy needed for rxn to happen–>doesn’t change equilibrium, recycled

A

catalysts

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12
Q

can catalyze 1 million substrate to product per second

A

carbonic anhydrase

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13
Q

amost instantaneous conversion to product, highly stereospecific and doesn’t cause many side rxns/byproducts, function at physiological conditions, responsive to organism’s dynamic needs (allosteric regulation)

A

enzymatic catalysis

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14
Q

often require extreme temp/pressure/pH, not as fast, specific or regulated reactions

A

chemical catalysis

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15
Q

able to catalyze rxn faster by diffusion control limits–enzyme draws substrate towards itself to shorten rate determining step

A

Circe effect

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16
Q

molecule acted on by enzyme

A

substrate

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17
Q

what is produced by enzyme

A

product

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18
Q

part of enzyme responsible for binding substrate to make enzyme substrate complex: 3D cleft, small, exclude water (unique microenviro), quite flexible (induced fit/comformation selection), bind substrate by weak noncovalent interactions

A

active site

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19
Q

hand in glove: need specificity but also catalytic power

so substrate not exactly same as each other, enzyme select for subpopulation of substrate that is good

A

induced fit

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20
Q

the
relationship between the rate of a
reaction and the activation energy is
___ and ____

A

inverse; exponential

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21
Q

physical interactions between enzyme and substrate, including substrate binding and transition state stabilization–>enables substrate specificity and catalytic power

A

binding effects

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22
Q

more obvious to see, involve acid/base catalysis, covalent catalysis; after substrate binding, enzyme act upon substrate to promote product form (polar ionizable a.a.)

A

chemical effects

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23
Q

enzymes act as matchmakers, promote rxn by reduce entropy, strip away water, induce fit, distort substrate

A

substrate binding

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24
Q

enzymes bind substrate much tighter in this state

A

transition state stabilization

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25
Q

stable comps that resemble unstable transition states, bound to enzyme w/ higher affinity than natural substrate–>competitive inhibitors, used in drugs

A

transition state analogs

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26
Q

antibodies generated against transition state analog

A

catalytic antibodies/abzymes

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27
Q

reaction acceleration achieved by catalytic transfer of proton; often involve histidine

A

acid base catalysis

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28
Q

two step process, first form covalent linkage with enzyme, second regenerate free enzyme

A

covalent catalysis

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29
Q

study of rates at which rxns occur; initial reaction velocity vs. [S]

A

kinetics

30
Q

delta [P] / delta time

A

velocity (rate of reaction)

31
Q

rate of reaction in relationship to [E] is ___

A

linear relationship

32
Q

velocity at beginning of enzyme catalyzed reaction before product accumulation

A

initial velocity/pre-equilibrium velocity

33
Q

initial velocity = concentration of enzyme substrate complex x rate constant of formation of product from ES

A

Vo = [ES]k2

34
Q

what did Michaelis and Menton have to assume to derive their equation?

A

Steady state: rate of formation of ES = to rate of its breakdown

35
Q

what is the M-M equation?

A

Vo = Vmax [S] / Km + [S]

36
Q

the [S] required to reach half of Vmax

A

Km

37
Q

velocity becomes independent of substrate concentration at this point

A

Vmax

38
Q

if [S] is

A

enzymes are highly sensitive to changes in [S] but have very little activity

39
Q

if [S] is > Km then…

A

enzymes high activity but insensitive to [S] changes

40
Q

if [S] is = km then…

A

enzyme has significant activity and is responsive to [S] changes

41
Q

double reciprocal plot more precise than M-M, used to determine Vmax/Km: 1/Vo=Km/Vmax[S]+1/Vmax

A

Lineweaver-Burke

42
Q

the enzyme turnover number that looks at population of enzymes and takes average. Is # of cules of substrate converted to product per unit time under saturating conditions; calculated by Vmax/[Et]

A

kcat

43
Q

compound that binds to enzyme to infere w/ activity either prevent ES from form or prevent breakdown to E and P–>bind to enzyme by noncovalent interactions

A

reversible enzyme inhibition

44
Q

usually resembling the substrate, these inhibitors bind only to free enzyme and not ES. Vmax is same but apparent Km is ^

A

competitive inhibition

45
Q

bind only to ES, decreases Vmax and apparent Km (double reciprocal plot lines are parallel)

A

uncompetitive inhibition

46
Q

bind both E and ES, Vmax decreases with no change in Km

A

noncompetitive inhibition

47
Q

tend to be manmade, permanently inactivate enzyme, form highly stable interactions/covalent bonds with enzymes–>includes transition-state analogs

A

irreversible inhibitors

48
Q

specific type of irreversible enzyme inhibition, also called biochem trojan horses or mechanism based inactivators–>initially unreactive but converted to reactive species that inactivates enzyme (effective drugs)

A

suicidal inactivator

49
Q

digestive enzymes including trypsin, chymotrypsin, elastase that cleave peptide bonds in protein substrate; also function in mediating turnover of self proteins; synth and stored in pancreas as inactive zymogens

A

serine proteases

50
Q

stored in pancreas, inactive form of serine proteases, activated at proper time by selective proteolysis

A

zymogens

51
Q

serine protease that cleaves by Lys and Arg because it has deep pocket and negative charged end

A

trypsin

52
Q

serine protease that cleaves by Phe and Tyr

because it has a deep hydrophobic pocket

A

chymotrypsin

53
Q

serine protease that cuts all peptide bonds

A

papain

54
Q

serine protease that cuts by Gly and Ala because it has a shallow hydrophobic pocket

A

elastase

55
Q

serine proteases have a conserved catalytic mechanism based on Asp, His, and Ser. What is this referred to as?

A

Catalytic triad

56
Q

This residue removes H from Ser’s OH to make it a strong nucleophile and activates a water cule to regenerate the free enzyme in acid base catalysis

A

Histidine

57
Q

This residue stabilizes the + charged His to facilitate serine ionization

A

Aspartate

58
Q

This residue acts as the nucleophile attacking the carbonyl group of polypeptide substrate in covalent catalysis–>usually in 2 steps: gen intermediate, then generate product

A

Serine

59
Q

how can you regulate the activity of enzymes over the long term?

A

by controlling enzyme availability: location, amounts, rates of synth/degrade

60
Q

how can you regulate the activity of an enzyme over the short term?

A

covalent (phosphorylation) and noncovalent modification (allosteric)

61
Q

this is important in aa with OH groups; posttranslational modifications; each protein has about 4 diff events of this, and about 16 diff permutations; critical for regulating function and activity

A

phosphorylation

62
Q

enzymatic pathways self-regulate, in response to bodily needs; shuts down first unique committed step in respects to branching points

A

negative feedback regulation

63
Q

interact w/ metabolic intermediates that bind noncovalently at sites distinct from active site, usually quaternary structure; often slow; sigmoidal curve, not follow M-M (cooperative activation)

A

allosteric enzymes

64
Q

below a certain substrate [] there is little enzyme activity; after threshold has been reached the enzyme activity ^ rapidly

A

threshold effect

65
Q

What is PFK1?

A

catalyzer of early step in glycolysis

66
Q

What is the allosteric inhibitor of PFK1?

A

PEP

67
Q

what is an allosteric activator of PFK1?

A

ADP

68
Q

Phosphoryl groups are added by ____ and removed by _____

A

kinases; phosphatases

69
Q

production of glycogen from glucose is catalyzed by ___ and broken down into glucose by ____

A

glycogen synthase’ glycogen phosphorylase

70
Q

which hormones in a hungry state cause phosphorylation, which activates catabolic enzymes and inactivates anabolic enzymes, breaking glycogen into glucose?

A

glucagon and epinephrine

71
Q

which hormone in a fed state cause both enzymes to be unphosphorylated, which activates anabolic enzyme and inactivates catabolic E, storing glucose as glycogen?

A

insulin

bmsc 200 (7 decks)

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