9 - Energetics and Dynamics Flashcards

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1
Q

structure of an enzyme?

A

sachride interacting residue

catalytic residue

extended binding cleft

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2
Q

steps of an ezyme reaction?

A
enzyme + substrate [binding]
enzyme subtrate complex
[catalysis]
Enzyme-product complex
[release]
enzyme + product
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3
Q

understand an exergonic reaction and endergonic using Gibbs?

A

if G more than 0

  • EXERGONIC
  • energy is lost

if G less than 0

  • ENDERGONIC
  • energy not lost
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4
Q

coupling energonic and exergonic?

A

.

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5
Q

substrate factors that enzyme function depends on?

A
  • localisation of sub
  • orientation
  • binding energy
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6
Q

what step is the slowest step in a reaction?

A

K2
step from enzyme substrate –> enzyme + product

  • K2 = Kcat
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7
Q

what are the 3 assumptions of the michaelis-menten calc?

A
  1. Reverse reaction is neglible
  2. Only single Enzyme Substrate complex
  3. Assume subtrate is in much more excess than enzyme and [S] isn’t affected
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8
Q

understand initial rate and [S] graph?

A

.

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9
Q

what is the Vmax and the eq?

A

theoretical max where enzyme is fully saturated [limiting factor]

Vmax = Kcat [E]t

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10
Q

What is Vo

A

half the Vmax
cant be obtained as you don’t know the Vmax

so use m-m eq

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11
Q

michealis menten eq?

A

Vo = Vmax [S] / Km + [S]

(Vmax is also Kcat[E]t)

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12
Q

what is Km?

A

Michealis constant

[S] when reaction is 1/2 maximal

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13
Q

how to find Km?

A

line where Vo meets curve then down to [S]

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14
Q

what is Kcat?

A

Kcat is the slowest step so the K2 step

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15
Q

what does a

  • high Kcat value mean
  • small Km value mean
A

high Kcat
- rapid turnover

small Km
- high substrate affinity

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