enzymes Flashcards

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1
Q

contact residues

A

bind to substrate and determine enzyme specificity

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2
Q

catalytic residues

A

acts on bonds in substrate broken by enzyme action

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3
Q

catabolic

A

breaking down

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4
Q

anabolic

A

synthesis

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5
Q

why do enzymes need to be broken down?

A

to prevent simultaneous backward and forwards reactions from happening

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6
Q

why only a small number of enzymes needed?

A
  • can be re-used
  • catalyse reactions at a rapid rate
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7
Q

how do enzymes lower activation energy?

A
  • substrate strained by enzyme to help reach transition state
  • enzyme enclose substrate to create favourable environment e.g. acidic environment
  • enzymes orientate substrate molecules so reacting bonds are close to each other
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8
Q

what is temperature quotient Q10?

A

Q10 is the factor by which rate increases for a ten degree rise in temperature

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9
Q

what is the equation for Q10

A

rate at T + 10C / rate at T

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10
Q

how does cyanide act as a non competitive inhibitor

A

changes shape of cytochrome oxidase irreversibly and therefore prevents ATP production

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11
Q

state an example of a precursor enzyme

A

protease synthesised as inactive precursor to prevent damage to proteins in a cell = pepsinogen (inactive) but when HCl added, it is turned back into pepsin.

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12
Q

how can precursor enzymes be activated?

A

addition of co factor e.g. co-enzymes FAD and NAD

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13
Q

function of filter paper in chromatography

A

stops plate from drying out

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14
Q

if the sample moved higher up the chromatography paper…

A

it it less polar = more soluble in a solvent, and so less attracted to plate which is why it moves up.

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15
Q

higher polarity molecules will…

A

stick/absorb to surface more and therefore move slowly.

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16
Q

what is a similarity between non competitive and competitive inhibitors

A

they both decrease rate of reaction