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

A

isozymes

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

A

higher

23
Q

hexokinase is present in blank

A

most tissues including liver

24
Q

glucokinase responds when the levels of glucose are blank

A

high

25
Q

hexokinase functions more during blank levels of glucose

A

normal

26
Q

inhibitors work in a variety of ways and differ in terms of their blank

A

specificity

27
Q

general inhibitors like heavy metals inactivate enzymes blank and blank

A

irreversibly, non specifically

28
Q

specific enzyme inhibitors are useful in medicine because they can mimic the blank to target enzyme

A

substrate

29
Q

these bind at the active center and rom a permanent covalent bond to the enzyme

A

irreverisble inhibitors

30
Q

two types of reversible inhibitors

A

competitive, non competitive

31
Q

competitive inhibitors bind to the blank center by non covalent bonds

A

active

32
Q

noncompetitive inhibitors do not bind to blank

A

active site

33
Q

competitive inhibitors are influenced by amount of blank but blank are not

A

substrate, noncompetitive

34
Q

competitive inhibitor blank Vmax and blank Km

A

does not change, increases

35
Q

noncompetitive inhibitor blank Vmax and blank Km

A

decreases, doesnt change

36
Q

converting hyperbolic function of michaelis menten model into linear

A

lineweaver burk

37
Q

competitive makes a blank lineweaver burk plot

A

x intercept change

38
Q

noncompetitive lineweaver burk plot changes blank

A

y intercept

39
Q

an enzyme who’s activity is influenced by multiple variables

A

allosteric

40
Q

hemoglobin is not an enzyme but has blank properties

A

allosteric

41
Q

enzymes regulated by allosteric effects always have more than one subunit and more than one center….aka

A

quaternary structure

42
Q

enzyme that adds phosphate onto a side chain

A

kinase

43
Q

enzyme that breaks off a phosphate group

A

phosphatase

44
Q

adding a phosphate to something like serine or threonine would make it look more like blank because of negative charge

A

aspartic acid/glutamic acid

45
Q

active digestive proteases cannot be synthesized inside cells because they would blank the cells that made them

A

damage

46
Q

proteases are secreted as inactive precursors… aka

A

zymogens

47
Q

zymogens are blank in the gut

A

activated

48
Q

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

A

duodenum, limited specificity

49
Q

kinetic studies amount of product formed in amount of time formula

A

deltaP/deltaT = k[S]