Lecture 4 - Biochemistry Rules of Engagement Flashcards

(35 cards)

1
Q

steps to create products from the enzymes

A

1: substrate enters active site on enzyme
2: creates an enzyme/substrate complex
3: becomes a enzyme/product complex
4; products leave the active site of the enzyme

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2
Q

what are the 4 major things needed to help create biological reactions

A

enzymes, energy (ATP), the redox class of helpers (NADH,FADH2, and NADPH), and electric charge across membranes

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3
Q

the enzyme substrate E-S complex

A

when a substrate enters the enzyme active site

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4
Q

what reaction would be used to find the substrate concentrations of an enzyme

A

velocity reaction

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5
Q

how would you quantify a substrate in a velocity reaction

A

use an electric scale to weigh out starch and put in in known solution volumes to know starting concentration

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6
Q

how would you quantify a product in a velocity reaction

A

use a metabolite specific test to measure color and intensity with a spectrophotometer

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7
Q

how is the standard curve plotted in a velocity reaction

A

make up a range of sucrose concentrations from sugar and make up a range of standards

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8
Q

what is vmax/reaction velocity

A

looking at how much product an enzyme can make in a given time frame

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9
Q

how could an enzyme be inhibited

A

could be driven by having more substrate, product could reduce enzyme activity (like a backlog), toxins/metabolites could temporarily or permanently block enzyme sites

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10
Q

what is the easiest enzyme reaction curve

A

the Michaelis Menton Curve

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11
Q

what does the km of the Mechaelis Menten curve mean

A

is 1/2 of vmax, where vmax is the maximum velocity

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12
Q

at what conditions do enzyme operate (in regards to vmax, oxygen and pH)

A

enzymes operate below their vmax, at specific pH conditions, and under certain aerobic/anaerobic conditions

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13
Q

what are enzymes activated by

A

metabolites

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14
Q

classes of enzymes inhibition

A

Competitive and non-competitive inhibition

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15
Q

competitive inhibition

A

reversible. adding more of proper substrate can out-compete and flush out the inhibitor

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16
Q

non-competitive inhibition

A

where the inhibitor cannot be removed and you have to replace them enzyme with new enzyme

17
Q

where do inhibitors typically operate

A

the active site and at the allosteric site

18
Q

what can override or cancel inhibition at the allosteric site

19
Q

what is ATP regulated by

A

ATP synthase (ATPase)

20
Q

energy charge

A

the sum of ATP and 1/2 the ADP/ all the ATP +ADP+AMP

21
Q

what is the energy charge of ATP producing reactions

22
Q

what is the energy charge of ATP consuming reactions

23
Q

what is the energy charge in healthy cells

24
Q

what are the 3 kinds of ATP synthase

A

F, V, and P-ATPase

25
where is ATP synthase present
in the mitochondria, chloroplasts, and bacteria
26
F-ATPase
the regular H+ transporting type found in the mitochondria Fat type
27
V-ATPase
types found on the vacuole vacuole type
28
P-ATPase
stands for pumping types
29
T/F: ATPase can rotate
t
30
What is the other use for ATP synthase besides as a catalyst for the ATP reaction
used to move H+ ions and generate electric charge
31
what part of ATP synthase is the active site that makes ATP
the roof
32
membrane potential
an electric charge across a membrane
33
to hold a charge, you need a ________
membrane
34
what direction do electrons flow
to the area with less electrons
35
proton motive force
the gradient of H+ ions