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BMSC 200 > Chapter 6 > Flashcards

Chapter 6 Flashcards

1
Q

vitalism

A

belief that living things are different from non-living

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2
Q

protease

A

pre-digest proteins

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3
Q

lipase

A

together with protease, break down substances into smaller water soluble substances

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4
Q

carbohydrase

A

convert starch syrup to sugar syrup

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5
Q

isomerase

A

convert glucose to fructose (sweeter)

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6
Q

co-factors

A

inorganic ions required by some enzymes for activity

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7
Q

co-enzymes

A

vitamins required by some enzymes for activity

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8
Q

prosthetic group

A

tightly associated with enzyme (like glued)

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9
Q

apoenzyme

A

lack of extra factor

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10
Q

holoenzyme

A

apoenzyme with extra factor

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11
Q

6 classifications of enzymes

A
  • oxidoreductases
  • transferases
  • hydrolases
  • lyases
  • isomerases
  • ligases
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12
Q

chemical catalysts…

A

require extremes of temp, pressure, pH

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13
Q

enzymes function at…

A

physiological conditions

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14
Q

enzymes have a ________.

A

high degree of specificity

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15
Q

Active sites can change…

A

pKa

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16
Q

Substrates are bound to enzymes by…

A

weak interactions (H bonding, electrostatic, hydrophobic, vdW)

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17
Q

specificity of substrate depends on….

A

arrangement of atoms in the active site

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18
Q

substrate binding can cause…

A

induced fit or conformation selection

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19
Q

hand

A

substrate

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20
Q

glove

A

enzyme

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21
Q

P < S

A

spontaneous

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22
Q

binding effects

A

interaction between enzyme and substrate

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23
Q

chemical effects

A

accepting/donating protons; forming covalent linkages

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24
Q

Induced fit during E+S causes…

A

active site to become more complimentary toward transition state

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25
Substrate binding promotes reaction by...
- reducing entropy - removal of water molecules to expose reactive groups - alignment of reactive functional groups of enzyme with substrate - distortion of substrates - induced fit as a response
26
Increased interactions of enzyme and substrate occurs in....
transition state
27
enzymes have higher affinity for ....
transition state than substrates
28
transition state analogs
stable compounds whose structures resemble unstable transition states
29
catalytic antibodies
- abzymes - generated against a transition state analog may bind to substrate, catalyzing rex by promoting formation of transition state
30
What participates in enzymatic catalysis?
- polar, ionizable residues (Asp, Glu, His, Cys, Tyr, Lys, Arg, Ser) - anions and cations of certain amino acids
31
two commonly observed mechanisms of catalysis
- acid/base | - covalent
32
for most enzymes, greatest activity at...
physiological pH 7.4 and 37 degrees
33
steady state equation
rate of formation of ES complex is equal ti rate of its breakdown
34
Km
amount of substrate required for enzyme to function at half maximal velocity
35
[S] < Km
enzymes are highly sensitive to change in substrate conc., but have very little activity
36
[S] > Km
enzymes have high activity but are insensitive to changes in substrate concentration.
37
[S] = Km
enzyme has significant activity and is responsive to changes in substrate concentration
38
kcat
-enzyme turnover number | the number of molecules of substrate converted to product per unit time by a single enzyme
39
how to calculate kcat
Vmax/[E]t
40
reversible enzyme inhibitors
bind to enzyme by non-covalent interactions - competitive - uncompetitive - non-competitive
41
competitive inhibitors
resemble substrate - binds only to enzyme - increase Km
42
uncompetitive
- bind to ES | - decrease Vmax and Km
43
non-competitive
- bind to E and ES | - decrease Vmax
44
irreversible enzyme inhibitors
- highly stable covalent bonds with enzymes | - permanently inactivates enzyme
45
what are serine protease
- digestive enzyme - mediate turnover of self proteins - in pancreas as inactive zymogens - both covalent and acid/base catalysis
46
zymogens
prevent damage to cellular proteins, activated by selective proteolysis
47
trypsin cleaves
Lys and Arg
48
chymotrypsin cleaves
Phe, Tyr
49
Elastase cleaves
Gly, Ala
50
papain
cuts all peptide bonds
51
catalytic triad
His, Asp, Ser
52
catalytic triad - His
removes H from Ser hydroxyl to make it a strong nucleophile and donate electrons and activating a water molecule to regenerate the free enzyme – acid/case catalysis
53
catalytic triad - Asp
stabilize the positively-charged His to facilitate serine ionization
54
catalytic triad - Ser
acts as nucleophile (tendency to donate e-) attaching the carbonyl grouop of the polypeptide substrate – covalent catalysis
55
enzyme can be regulated by:
- controlling amount present (long term) | - adjusting activity of a constant quantity (short term)
56
enzymatic pathways often controlled through
negative feedback by final product
57
final product often inhibits...
first step; conserving material and energy and prevent accumulation of intermediates
58
negative feedback is...
a branched pathway
59
allosteric enzymes do not....
obey michaelis-mentin kinetics and have signoidal curves
60
allosteric enzyme binding of substrate disrupts R to T equilibrium in favour of...
R
61
cooperatively/threshold effect
Allosteric enzymes transition from a less active state to a more active state within a narrow range of substrate concentration. They are sensitive near the Km than M-M enzymes of the same Vmax. Below this sensitivity there is little zctivity, after the threshold, the enzyme activity rapidly increases.
62
PEP is an ____________ of PFK-1
allosteric inhibitor
63
ADP is an _________ of PFK-1
allosteric activator
64
When ration of [PEP]/[ADP] is low....
PFK is activated and glycolysis produces more ATP
65
glycogen synthase
-anabolic, catalyzes production of glycogen from glucose
66
glycogen phosphorylase
-catabolic, catalyze breakdown of glycogen into glucose
67
phosphorylation favours....
breakdown of glycogen into glucose in response to glucagon and epinephrine (anabolic inactive)
68
dephospho rylation favours....
storage of glucose as glycogen in response to insulin (catabolic inactive)

BMSC 200 (11 decks)

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