Topic 5 Flashcards

1
Q

Nitrogen fixation

A

N2 + 3H2 > NH3

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2
Q

At what environments do industrial processes do N fix?

A

~200 atmospheres and 400 degrees Celcius

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3
Q

At what environments do bacteria fix N?1

A

Atmospheric pressure, ambient temperature

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4
Q

2 ways a reaction can be accelerated?

A

Adding heat

Adding catalyst

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5
Q

3 ways enzymes are proteins?

A
  • primary, secondary, tertiary, quaternary structure
  • typically globular
  • structure determined by same forces
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6
Q

3 ways enzymes are catalysts?

A
  • accelerate reaction rates
  • regenerate at the end of reaction
  • highly specific (no side reactions)
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7
Q

Enzyme Nomencclature

A

end in -ase

substrate (or product) chemical rxn

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8
Q

A reaction will only proceed if…

A

free E of products is less than free E of reactants

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9
Q

When G is negative

A

Reaction is exergonic, thermodynamically favourable, spontaneous

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10
Q

When G is positive

A

Reaction is endergonic, thermodynamically unfavourable, and non-spontaneous

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11
Q

how is the speed of a biochemical reaction determined?

A

activation energy barrier

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12
Q

At what point in the reaction is there highest free energy?

A

Transition state

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13
Q

T/F do enzymes affect G of reaction

A

FALSE, enzymes do not affect

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14
Q

How do enzymes reduce free energy? (4)

A
  1. remove substrates from aqueous solutions
  2. proximity and orientation
  3. taking part in reaction mechanism
  4. stabilizing transitions state
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15
Q

Active sites (4)

A
  • where catalysis occurs (small portion of protein)
  • key amino acids located in active site (binding and catalysis)
  • determines affinity, speciality and rate
  • complementary to substrate/transition state (shape, hydrophobic interactions, H bonds, ion pairs)
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16
Q

Where is the active site in a lysosome?

A

3D cleft/crevice

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17
Q

Lock and Key model

A

active site matches shape of substrate contributing to affinity and specificity

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18
Q

Desolvation

A

exclusion of water,

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19
Q

3 advantages of desolvation

A
  1. removal of water shell accelerates reactions
  2. enhances polar interactions
  3. prevents side reactions
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20
Q

Induced Fit Model

A

enzymes change shape when substrate binds
closes off active site
brings catalytic groups together

21
Q

orientation

A

chemical reactions only occur if substrates come together in right orientation

22
Q

proximity

A

active sites bind substrates close to each other

23
Q

3 types of catalysis

A

acid/base, covalent, metal ion

24
Q

how are catalysis reactions acheived

A

amino acids or cofactors

25
Q

Acid/Base catalysis

A

R groups of amino acids act as acids or bases depending on state of protonation

26
Q

Covalent catalysis

A

de-protonated R groups of amino acids act as nucleophiles

27
Q

Review classification of cofactors tree

A

and examples btw

28
Q

holoenzyme

A

prosthetic group and tertiary structure

29
Q

apoenzyme

A

tertiary structure without prosthetic group

30
Q

3 ways transition state is stabilized

A
  • binding TS lowers G
  • parts of protein interact with unstable transition state
  • enzyme active sites
31
Q

the more tightly an enzyme binds to TS ….

A

the greater the catalytic activity of the enzyme

32
Q

TS analogs are ____ inhibitors

A

potent

33
Q

potent inhibitors

A

binds to enzyme with higher affinity compared to substrate

rational basis for drug design

34
Q

Km gets ___ as affinity ____

A

smaller, increases

35
Q

Mechanisms that affect intrinsic activity of enzyme

A

competitive inhibition, allostery, reversible covalent modification, ionic signals

36
Q

Allostery (allosteric enzymes)

A

modify metabolic processes with allosteric effectors because enzyme activity may be cooperative

37
Q

Reversible covalent modification

A

modify proteins in tertiary amino acid residue, increase or decrease activity of target

38
Q

mechanisms that change amount of enzyme available,

A

regulation of gene expression, changes in sub cellular localization (regulate access of enzyme and substrate)

39
Q

competitive inhibitors

A

bind reversibly
resemble substrate or TS but DO NOT react
physically block = less active sites, lower reaction rate, increase in Km

40
Q

how to overcome inhibition

A

increase substrate concentration (no change in Vmax)

41
Q

Competitive inhibitors decrease _____ affinity (increase Km)

A

decrease

42
Q

T state

A

low activity, allosteric inhibitor favours

43
Q

R state

A

high activity, allosteric activators favours

44
Q

most common type of reversible modification

A

phosphorylation

45
Q

Phosphorylation

A

increases size, polarity, and charge

46
Q

____ catalyze phosphoryaltion

A

protein kinase

47
Q

______ catalyze dephosphorylation by ____

A

protein phosphatase, hydrolysis

48
Q

which amino acids are usually phosphorylated (ones with OH)

A

ser, tyr, thr