Enzymes 1 & 2 Flashcards

1
Q

what is activation energy?

A

the energy required to go from reactants to products

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2
Q

stabilizing transition states makes it more favorable and reduces ___________

A

delta G

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3
Q

definition of an enzyme

A

increases the rate or velocity of a chemical reaction without changing itself in the process

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4
Q

classic enzyme nomenclature

A

substrate +action+ase

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5
Q

systematic enzyme nomenclature

A

substrate(s) + enzyme type

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6
Q

oxidoreductase function

A

catalyze oxidation-reduction reactions
ex. lactate to pyruvate

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7
Q

transferase function

A

catalyze transfer of C N or P containing groups
ex. serine to glycine

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8
Q

hydrolase function

A

catalyze cleavage of bonds by addition of water
ex. urea

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9
Q

Renin

A

role in regulation of blood pressure

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10
Q

pepsin

A

digestive enzyme

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11
Q

how do enzymes accelerate reactions?

A

-create an alternate reaction pathway in which the transition state has lower free energy
-decreases free energy of activation and lowers the activation barrier of delta G
-increase the concentration of substrate in the transition state and thus increases the rate of the reaction

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12
Q

describe the active site of an enzyme

A

-small 3D cleft or crevice formed by different parts of amino acid sequence
-complementarity of substrate for site
-noncovalent interactions

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13
Q

Lyases

A

catalyzes cleave of C-C, C-S, and C-N bonds
ex. pyruvate to acetylaldehyde

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14
Q

Isomerases

A

catalyze racemization of optical or geometric isomers
ex, methylmalonyl CoA to Succinyl CoA

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15
Q

ligases

A

catalyze formation of bonds between carbon and S, O, N coupled to hydrolysis of high energy phosphates
ex. pyruvate to oxaloacetate

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16
Q

what are the noncovalent interactions that hold enzyme and substrate complexes together

A

-H bonding
-ionic
-van der waals
-hydrophobic

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17
Q

what happens at Vmax

A

all of the enzyme present in the system is saturated

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18
Q

what is km

A

km is the amount of substrate is takes to reach half Vmax
Vmax/2

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19
Q

what is kcat

A

how many substrate molecules are transformed into products per unit time by a single enzyme

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20
Q

how to calculate enzyme efficiency

21
Q

at high concentrations of substrate, the velocity of the reaction is ___________________, constant and independent of substrate concentration

A

zero order

22
Q

at low concentrations of substrate, the velocity of the reaction is ___________, proportional to substrate concentration

A

first order

23
Q

large Km=

A

low affinity of enzyme for substrate

24
Q

small Km=

A

high affinity of enzyme for substrate

25
competitive inhibition
-inhibitor binds to active site -Km increases and Vmax stays the same
26
how can competitive inhibition be overcome?
flooding the reaction with substrate
27
noncompetitive inhibition
-binds to allosteric site -Km stays the same and Vmax decreases graph makes a v shape
28
uncompetitive inhibition
-binds to enzyme-substrate complex -Km decreases and Vmax decreases lines run parallel
29
modifies transpeptidase and prevents bacterial cell wall synthesis
penecillin
30
modifies cyclooxygenase (1&2) & reduces inflammatory signals
Aspirin
31
cooperative binding
binding at one site enhances binding at another
32
Aspartate transcarbamyolase (ATCase)
first committed step of nucleotide biosynthesis -CTP is end product and feeds back to inhibit the enzyme
33
what amino acids can be phosphorylated
serine, threonine, tryosine histidine in bacteria
34
enzymes that add phosphates
kinases
35
regulatory proteins involved in muscle contractility
Troponins T and I
36
released in the plasma in response to cardiac damage -gold standard in diagnosing MI
Cardiac specific isoforms (cTn)
37
cleaves all accessible peptide bonds (serine protease)
subtilisin
38
cleaves after all accessible Lys or Arg (serine protease)
trypsin
39
cleaves only after Arg in a specific sequence
thrombin
40
statins block the 1st committed step in cholesterol synthesis because they are.....
competitive inhibitors in Hydroxymethylglutaryl (HMG) CoA reductase
41
serious side affects of statins
-reduced testosterone -memory loss -transiant global amnesia -muscle pain
42
formulas for delta G
ΔG=ΔH-TΔS ΔG=ΔG0'+1.36log products/reactants
43
formula for standard state ΔG
ΔG0'= -1.36(logKeq)
44
how can unfavorable biosynthetic reactions proceed?
can be accomplished by coupling reaction to a favorable reaction
45
the overall ΔG of a reaction its the sum of....
free energy changes of the individual steps
46
many unfavorable biosynthetic reactions are coupled to ________________
ATP hydrolysis (strong phosphate bonds)
47
hexokinase couples reaction by ......
transferring phosphate directly from ATP to glucose----aided by proximity of both reactants binding to adjacent sites on the enzyme
48