Lec 7 Kinetics Flashcards

1
Q

k is the blank

A

rate constant

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2
Q

enzymes speed up attainment of equilibrium by influencing blank

A

k

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3
Q

linear portion of equilibrium curve is what we use to determine blank

A

rate

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4
Q

enzyme assay when product yield is measured throughout entire reaction

A

continuous assay

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5
Q

assay where individual time points are taken

A

sampled assays

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6
Q

assay where two metabolic reactions that share a common intermediate … product of first is substrate of the second

A

coupled assay

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7
Q

these can enhance sensitivity, and facilitate data collection during assay

A

synthetic substrate

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8
Q

enzyme is saturated with substrate at blank

A

Vmax

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9
Q

study of how enzymes influence the rates of change

A

enzyme kinetics

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10
Q

Km =

A

[S] at 1/2 Vmax (Affinity of enzyme for substrate)

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11
Q

Km and Vmax are part of this model

A

Michaelis menten

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12
Q

michaelis menten model is a blank

A

square hyperbola

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13
Q

Km does not equal

A

Vmax / 2 because it is the substrate concentration at 1/2 Vmax

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14
Q

an enzyme does not have to obey michaelis menten and can have a blank

A

Km

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15
Q

an enzyme that acts on more than one substrate it will usually have a different blank for each

A

Km

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16
Q

low Km means blank affinity of E for S

A

high

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17
Q

high Km means blank affinity of the E for S

A

low

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18
Q

a good way to tell isozymes apart is to look at each of their….

A

Km’s

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19
Q

low affinity (high Km) may mean that the enzyme isnt even ….

A

catalyzing the reaction

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20
Q

hexokinase and glucokinase are blank

21
Q

glucokinase is found mostly in the blank and blank

A

liver/beta cells of pancreas

22
Q

hexokinase as a blank affinity for glucose than glucokinase

23
Q

hexokinase is present in blank

A

most tissues including liver

24
Q

glucokinase responds when the levels of glucose are blank

25
hexokinase functions more during blank levels of glucose
normal
26
inhibitors work in a variety of ways and differ in terms of their blank
specificity
27
general inhibitors like heavy metals inactivate enzymes blank and blank
irreversibly, non specifically
28
specific enzyme inhibitors are useful in medicine because they can mimic the blank to target enzyme
substrate
29
these bind at the active center and rom a permanent covalent bond to the enzyme
irreverisble inhibitors
30
two types of reversible inhibitors
competitive, non competitive
31
competitive inhibitors bind to the blank center by non covalent bonds
active
32
noncompetitive inhibitors do not bind to blank
active site
33
competitive inhibitors are influenced by amount of blank but blank are not
substrate, noncompetitive
34
competitive inhibitor blank Vmax and blank Km
does not change, increases
35
noncompetitive inhibitor blank Vmax and blank Km
decreases, doesnt change
36
converting hyperbolic function of michaelis menten model into linear
lineweaver burk
37
competitive makes a blank lineweaver burk plot
x intercept change
38
noncompetitive lineweaver burk plot changes blank
y intercept
39
an enzyme who's activity is influenced by multiple variables
allosteric
40
hemoglobin is not an enzyme but has blank properties
allosteric
41
enzymes regulated by allosteric effects always have more than one subunit and more than one center....aka
quaternary structure
42
enzyme that adds phosphate onto a side chain
kinase
43
enzyme that breaks off a phosphate group
phosphatase
44
adding a phosphate to something like serine or threonine would make it look more like blank because of negative charge
aspartic acid/glutamic acid
45
active digestive proteases cannot be synthesized inside cells because they would blank the cells that made them
damage
46
proteases are secreted as inactive precursors... aka
zymogens
47
zymogens are blank in the gut
activated
48
enteropeptidase is synthesized in cells lining the blank and secreted directly.... even though it is an active protease it is no danger to cells that secrete it because it has such a blank
duodenum, limited specificity
49
kinetic studies amount of product formed in amount of time formula
deltaP/deltaT = k[S]