Brainscape's Knowledge GenomeTM

Browse over 1 million classes created by top students, professors, publishers, and experts.


See full index

BIOL1007 > Enzymes > Flashcards

Enzymes Flashcards

1
Q

define enzyme

A

one or more polypeptide chians forming a catalytic active site

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

define substrate

A

moleucle which binds to an active site and undergoes a chemical reaction

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

define product

A

the reuslt of an enzymes actions

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

Name 6 roles of enzymes and an example of an enzyme that completes that function

A
  1. digestion of food (pepsin)
  2. clotting of blood (thrombin)
  3. Blood pressure (ACE)
  4. Immune defence (lysozyme)
  5. Breakdown of drugs (cytochrome P450)
  6. routine cell processes
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

Name the types of reactions that enzymes catalyse

A
  1. anabolic (smaller –> larger)
  2. catabolic (larger–> smaller)
  3. interconversions (reaction can go in either direction without any energy cost)
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

What does the name of most enzymes end in?

A

-ase

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

Whats the enzymes commision number?

A

Class. Subclass. Sub-sub class. Serial number

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

Name 6 classes of enzymes and what the role is (the type of reactions that enzymes can do)

A
  1. Oxidoreductases- transfer of electrons (as H- or H)
  2. Transferases- transfer chemical groups e.g. methyl
  3. Hydrolases- breaks bonds with water
  4. lyases- reactions involving double bonds
  5. isomerases- trasfer of groups within a molecule
  6. ligases- formation of bonds uisng energy for ATP
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

Why are enzymes necessary?

A
  • Pace of life
  • conditions of life e.g. body temp, neutral pH
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

What do reaction rates of enzymes depend on?

A
  • the speed of 1 reaction (rate constant, K)
  • the number of reactions happening simultaneously
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

Enzymes can’t change the maximum speed of a reaction, so what do they do instead to help speed up reactions?

A

They make it possible for more reactions to happen by reducing the activation energy

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

Whats meant by enzyme potency?

A

How much it speeds up a reaction

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

Tell me 4 advantages of enzymes

A
  1. Reusable (saves resources)
  2. specific (only desired reaction)
  3. efficient (only desired reaction)
  4. Controllable (start/ stop reactions)
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

Whats the active site?

A
  • a small part of the whole enzyme
  • 3D arrangement of amino acids
  • contains binding and catalytic residues
  • source of substrate and reaction specificity
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

Name 2 hypothesis, and by who they were created by relating to substrate specificity

A
  1. lock and key model (Fischer)
  2. induced fit model (Koshland)
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

whats the lock and key hypothesis?

A
  • the enzyme is the lock
  • the substrate is the key
  • the two are complementary
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

Whats the induced fit hypothesis?

A
  • idea that active site changes shape slightly to allow a strong binding of substrate to enzyme
  • there are opposing charges of substrate and active site. so, when substrate binds to the site the attraction force pulls the protein around the substrate
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

give an example of an enzyme that follows the induced fit hypothesis?

A

Hexokinase

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

Whats stereo-specificity and what is the hypothesis of this?

A

Ogstron 3-point binding

  • arrangement of protein determines the substrate it could bind to due to the overall orientation of the molecule
  • the substrate’s may have the same chemical properties and mr
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

What is reaction specificity determined by?

A
  • the 3D arrangment of residues
  • chemical properties of residues
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

often how many amino acids are involved in the reaction and what is this known as?

A

often only 3 (carefully positioned) amino acids perform the actual catalysis. This is known as a catalytic triad

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
22
Q

sometimes amino acids aren’t enough for a reaction to occur. So what things may have to be used, give some examples for each

A
  • metal cofactors
    e. g. Mg2+, Zn2+. Metal ions provide a small and dense positive charge
  • coenzymes
    e. g. NAD, NADP
  • Prosthetic groups

​e.g. Flavins, haem (Hb and catalase)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
23
Q

What are coenzymes?

what can they act as?

A

organic moelcules which provide/ remove groups for reactions and are sometimes called co-substrates

e. g. NADH –> NAD+ (co-substrate provuded the H)
* can act as hydrogen shuffles in redox reactions

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
24
Q

Whats the definition of enzyme kinetics?

A

The characterisation of the rates and steps of catalysis

i.e. putting numbers to how quickly enzymes work in a reaction

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
25
Q

What is enzyme kinetics measuring?

A

How an enzyme reacts by measuring the change in [S] or [P] over time after addition of the enzyme

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
26
Q

What apparatus can be used to measure an enzyme reaction and what is it measuring?

A

A spectrophotometer is used to measure either the decrease in [S] or increase in [P] by absorbance change

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
27
Q

does [P] increase over time at a constant rate?

A

no

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
28
Q

Why does [P] not increase over time at a constant rate?

A

a straight line isn’t shown on a [P]-time graph as, as time progresses the [S] runs out which means the reaction slows down which results in a curved line

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
29
Q

What are the units of V= reaction velocity?

A

mol/min

OR

mol/s (katal)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
30
Q

What are the units of enzyme activity?

A

umol/min (I.U.)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
31
Q

Whats the eqaution for specific activity as an indication for purity?

A

enzyme activity/ total amount of protein = indication of purity

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
32
Q

What are the units for specific activity ?

A

umol/min/mg

OR

umol.min-1.mg-1

OR

I.U./mg

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
33
Q

What does this graph show?

A
  • Product appears as substrate disappears
  • not all [S] has been converted to [P]
  • no completion as concentration required is not enought for reversable reaction
  • rate appears to be zero at the end due to an equilibrium being established as the forwards and backwards reaction occurs at the same rate
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
34
Q

What does the overall rate of a reaction depend on?

A

the rate constants and concentration

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
35
Q

How is rate calculated?

A

rate constant x concentration

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
36
Q

usually…

Ks –> P > KP –> S

so this is known as Kforwards and Kreverse

at equliibrium, how can this relationship be written?

A

Ks –> P x [S] = KP –> S x [P]

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
37
Q

What must an enzyme provide and what does this help to do?

A

an enzyme must provide an alternative route from S–> P, which requires less energy

therefore…

more molecules have that energy so more go from S–> P per second and the equilibrium is reached sooner

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
38
Q

how can reactions be pushed ‘backwards’?

A

by increasing the [product]

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
39
Q

whats the equation for the equilibrium constant?

A

Keq= Kforward / Kreverse = [P] / [S]

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
40
Q

as [S] increases so does the rate in a linear relationship. What equation defines this?

A

V= Kforward x [S]

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
41
Q

When an enzyme is introduced, the relationship between [S] and V is no longer linear but a curved shape. What equation defines this?

A

V = Vmax x [S]/ Km + [S]

This is also known as the Michaelis-Menten equation

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
42
Q

What’s the equation for general enzyme reactions?

A

Enzyme + substrate –> Enzyme-substrate complex –> Enzyme + Product

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
43
Q

What model describes the shape of the saturation curve?

A

The Michaelis- Menten model

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
44
Q

The following reversable reaction can be split into 2 sections, what are these sections? and what are the constant(s) associated with those sections?

E + S ⇔ ES ⇔ E + P

A

E + S ⇔ ES

This is the binding section

constants K-1 and K1

ES ⇔ E + P

This is the catalysing section

contant Kcat

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
45
Q

Whats the equation for the dissociation contant, Kd?

A

K-1 / K1 = [E] x [S] / [ES] = Kd

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
46
Q

What does Kd show?

A

The affinity for a substrate

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
47
Q

Fill in the blanks…

____ Kd = ____ Affnity

____ Kd = _____ Affinity

A

Small Kd = High affinity

Large Kd = Small affinity

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
48
Q

Whats the equation for Michaelis’ contant, Km?

A

K-1 + Kcat / K1 = Km

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
49
Q

The steady-state kinetics model is the Briggs/ Haldane, what assumptions have to be made with this model?

A
  • [ES] is constant
  • [S] >> [E] so [S] is constant
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
50
Q

Whats the equation for the chemical reaction for rate?

A

V= Kforward x [S]

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
51
Q

Whats the equation for the enzyme reaction for rate?

A

V= Vmax x [S] / Km + [S]

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
52
Q

On the Michaelis- Menten curve, Vmax and Km can’t be found as the curve levels off before Vmax and 1/2Vmax is needed to find Km. So instead, what graph is used to find these two values?

A

The Lineweaver-Burk plot

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
53
Q

Whats the definition and equation for Vmax?

What can the equation be rearranged to find?

A

Vmax is the maximal possible rate (when all ES)

Vmax = Kcat x [E]

This equation can be used to find Kcat…

Kcat = Vmax / [E]

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
54
Q

Whats Km and what does a low Km suggest?

A

Km is [S] which gives half the maximum rate

Km is [S] at which half of the enzyme moelcules are ES

A low Km suggests a high affinity for the substrate

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
55
Q

With Vmax, low saturating [S] is unusual, whats the exception to this? and tell me about this?

A

Ethanol

Vmax of alcohol dehydrogenase (ADH) is 10g/rate

the body can’t break ethanol down any faster than this unless the body has been adapted to due to high volumes digested reguarly e.g. alcoholics

56
Q

What’s more biologically significant; Vmax or Km

A

Km

57
Q

Whats methanol posioning and whats used to treat it and why?

A

When Methanol has been drunk, ADH (alcohol dehydrogenase) converts it to formaldehyde. However this is toxic.

For the treatment, ethanol has to be drunk as it’s Km is lower than methanols so it binds more strongly to ADH reducing the amount or formaldehyde produced

Ethanol Km= 1mM

Methanol Km= 10mM

58
Q

What are isozymes?

A

Different enzymes but they target the same substrate

59
Q

What three ways can be used to compare enzymes?

A
  1. The turnover number
  2. efficiency
  3. Potency
60
Q

Whats an enzymes turnover number?

A

The catalytic rate contant Kcat

It is the number of reactions that enzyme catalyses per second

61
Q

Whats enzyme efficiency?

A

the catalytic speed versus binding affinity

Kcat / Km

62
Q

Whats ‘kinetic perfection’?

A

if Kcat / Km > -1x108 then V is limited by diffusion of the substrate to the enzyme, not the enzyme itsself

63
Q

Whats enzyme potency?

A

How many times faster a reaction is when an enzyme is present

it looks at the ‘time for reaction with enzyme’ and ‘time of reaction without enzyme’ in order to calculate the ‘rate enhancement’

64
Q

Tell me 4 ways in which enzyme activity is controlled?

A
  1. change in temperature
  2. change in chemical conditions e.g. pH
  3. increase and decrease in transcription or breakdown
  4. direct regulation of the enzyme molecules
65
Q

What does this graph show?

A

The effect of temperature on V

66
Q

What does this graph show?

A

The effect on pH on V

67
Q

What does this graph show?

A

The effect of [enzyme] on V

68
Q

What model is used to explain the effect of [enzyme] on V?

A

The Michaelis-Menten model

69
Q

What two main bonds are involved in enzyme regulation?

A
  1. Covalent
  2. non-covalent
70
Q

Tell me the two types of covalent enzyme regulation and the enzymes involved in the process?

A
  1. Cleavage of peptide chain is Zymogen (irreversable)
  • part of the structure of the enzyme blocks the active site
  • A protease enzyme removes the blockage making the enzyme active
  1. Phosphorylation (reversable)
  • kinase enzyme attaches a phosphate covalently to an enzyme which distorts the molecule and changes the shape of the active site
  • could be a temporary effect
  • phosphatase removes the phosphate in order to reverase the reaction
  • usually activated by hormones
71
Q

tell me about non-covalent bonds with an enzyme and the types of regulation this has on an enzyme?

A
  • reversable binding of molecules to specific sites
  • increase or decrease in activity (boosting or inhibiting effect)
  • the two types of regulation in the enzyme are: K type (effects binding) and V type (effects catalysis)
72
Q

What type of regulation is cooperativity?

A

K type regulation

73
Q

Tell me about cooperativity?

A
  • substrate binding to one site increases the affinity at another
  • [substrate] directly regulates the enzymes activity
  • subunits of the enzyme stay in weak form until the substrate binds
  • when the substrate binds, it effects both subunits not just one
74
Q

What type of curve is produce when cooperativity of an enzyme is present?

Explain/ describe this curve

A

A sigmoidal curve

  • ’s shaped’ curve
  • level of Vmax is unaffected
  • makes enzymes sensitive to chnages in substarte concentration
  • No Km on this curve, instead its known as K0.5, still gives 1/2Vmax but not same as Km as its shifted right
75
Q

What do sigmoidal kinetics suggest?

A

A multiple subunit enzyme with cooperative changes in substrate affinity between subunits

76
Q

Are allosteric enzymes K type or V type?

A

K type

77
Q

What are allosteric enzymes?

A

Their activity is changed by other molecules (but not substrates)

They have regulatory subunits

allo- other

steric- site or shape

78
Q

What can allosteric enzymes be?

A

Activators or inhibitors

79
Q

Explain this curve and the effects it has on the values…

Is it a K type or V type?

A
  • activators shift curve to left
  • inhibitors shift curve to right
  • K0.5 changes as the curve shifts
  • activator produce a ‘normal’ saturation curve
  • chnages affinity of enzyme to substrate
80
Q

Explain this curve and the effects it has on the values…

Is it a K type or V type?

A
  • changes the catalytic step (Vmax)
  • inhibitor shifts curve right and makes Vmax lower
  • activator shifts curve left and raises the Vmax (hard to do)
81
Q

Whats are enzyme inhibitors?

A

they reduce the enzyme activity irreversibly or reversibly

82
Q

Name some irreversible inhibitors and what this means?

A

Irreversible inhibitors are known as suicide substrates (bind to enzymes active site and stops completion of that reaction)

examples

  1. aspirin
  2. penicillin
83
Q

How does aspirin act as an irreversible inhibitor?

A
  • leads to permanent covalent alteration of the enzyme
  • stopping it making pain signals
  • only part of molecule stays in the enzymes active site
84
Q

How does penicillin act as a irreversible inhibitor?

A
  • leads to a permanent covalent alteration of enzyme
  • entire compound stays in active site
  • permanent effect
85
Q

can inhibitors target the same steps as allosteric regulators?

A

yes

86
Q

What are the two type of inhibitors?

A

Competitive and non-competitive

87
Q

What are competitive inhibitors?

A

They interfere with binding

binds to active site and stop the substrate binding

88
Q

What are non-competitive inhibitors?

A

They interfere with the catalytic step

binds to allosteric site which means that the substrate can bind to the active site it just stops the product moelcule from being made

89
Q

Explain these graphs for inhibitors with respect to Vmax, Km and [S] or [E] concentration

A

competitive:

  • Vmax is the same
  • Km seems to be larger
  • acts as if [S] was less

Non-competitive:

  • Vmax seems to be smalled
  • Km is the same
  • Acts as if [E] was less
90
Q

Tell me about the opposing effects that competitive and non-competitive inhibitors have on certain values?

A

Both types lower V, but affect Vmax and Km differently. Opposite effects on Vmax and Km

91
Q

Which one shows the competitive and non-competitive lineweaver-plot?

A

Left: competitive

Right: non-competitive

92
Q

whats the equation for the inhibition factor (IF)?

A

1 + [I] / Ki

93
Q

whats the rate eqation for competitive inhibitors which contains the inhibition factor?

A

V = Vmax x [S] / (Km x IF) + [S]

94
Q

whats the rate eqation for non-competitive inhibitors which contains the inhibition factor?

A

V= (Vmax / IF) x [S]/ Km + [S]

95
Q

Whats the enzyme reaction equation for competitive inhibitors?

A

E+S+I ⇔ ES ⇒ E+P

96
Q

Whats the enzyme reaction equation for non-competitive inhibitors?

A

E+S+I ⇔ES+I

97
Q

What does Ki tell you?

A

Tells you how strongly an inhibitor binds

98
Q

Whats the third type of inhibitor and tell me about it?

A

uncompetitive inhibitor

Only binds when the substrate has already bound to the enyme

99
Q

Whats the reate equation for uncompetitive inhbitors containing the inhibition factor?

A

V= Vmax x [S]/ Km + ([S] x IF)

100
Q

What does an uncompetitive inhibitors Lineweaver Burk plot always look like?

A

2 parellel lines

101
Q

Tell me what the following inhibitors bind to…

competitive

Uncompetitive

Non-competitive

Mixes

A

Competitive: binds to only free E

uncompetitive: binds only to ES

non-competitive: binds to either

Mixed: binds to either (E or ES), but with different affinity for E and ES

102
Q

What does a mixed Lineweaver Burk plot look like?

A

Dont cross on axis

103
Q

Tell me some health related uses for Competitive inhibitors…

A
  • Viagra (cGMP phosphodiesterase)
  • Ibuprofen (COX2)
  • Statins (HMG CoA-reductase)
  • ACE inhibitors e.g. captopril
104
Q

Tell me some health related uses for Non-competitive inhibitors…

A
  • Turmeric (phosphorylase)
  • Donepezil (acetylcholinesterase)
105
Q

Tell me a use for an uncompetitive inhibitor…

A
  • weed killed (EPSP synthase)
106
Q

Summary

M-M curve can become sigmoidal if >1 active site

Other molecules can ­¯ activity via allosteric sites

Binding is specific, but may not be absolute (inhibitors)

Environmental conditions and inhibitors can ¯ activity

A
107
Q

What are the two types of substrate/ product reactions?

A
  1. Sequential method
  2. Ping-pong method
108
Q

Whats the sequential method?

A
  • the substrates may be ordered or random (so either one substrate has to bind before the other, or it makes no difference in the order that they bind)
109
Q

Whats the Ping-pong method?

A
  • covalent bonds to the enzyme are formed during this process
  • the substrates never meet each other
  • E’ is in an active form allowing B to form a bond with it (covalent bond)
110
Q

Even through the sequential and ping pong methods are different, do they come out with the same outcome?

A

yes

111
Q

Draw and energy profile diagram for reactions that are catalysed and uncatalysed. include the transition states, when each part of the reaction is formed etc.

A
112
Q

What does binding of substrate to enzyme partially offset?

A

The activation energy

113
Q

What are the two enzyme strategies?

A
  1. General strategies
  2. specific chemical strategies
114
Q

What are the general enzyme strategies?

A
  • The position of the reactant correctly in order for interaction
  • distort the reactants which makes them less stable
  • stabilise transition state (TS)
  • change the environment to favour the reaction
115
Q

Whats the order of affinity for transition state, substrate and product?

A

Affinity: Transition> substrate> Product

116
Q

What may resemble a transition state?

A

An inhibitor drug

117
Q

What are the specific chemical enzyme strategies? Tell me what happens in each?

A
  • Covalent catalysis: a.s.r reacts with substrate
  • Acid/ base catalysis: a.s.r accepts/ donates H+ (basic AA, acidic AA, Cys, Ser, Tyr)
  • Metal ion catalysis: various types

a.s.r= active site residue

118
Q

What are the strategies a combination of?

A

A combination of non-covalent binding effects and covalent chemical interactions which lowers the overall AE

119
Q

Name an example of a chemical strategy?

A

Proteolysis

120
Q

What is proteolysis?

A

The breaking of peptide bonds

121
Q

How can peptide bonds be cleaved?

A

Hydrolysis by boiling in 6M HCl acid for 24 hours

122
Q

Are peptide bonds stable?

A

yes

123
Q

Give an example of what can be used for proteolysis?

A

serine proteases (break down proteins using serine)

124
Q

Give 4 examples of serine proteases and what they are used for?

A
  1. Trypsin
  2. Chymotrypsin
  3. Elastase
  4. Thrombin

Gene duplication and divergence

125
Q

Whats the same and also different with each serine protease?

A

They carry out the same reaction (cleavage of peptide bond via hydrolysis) but they use different substrates due to the binding specificity

126
Q

Why is the Chymotrypsin active site so specific?

A

Its lined by hydrophobic residues

127
Q

Why is the trypsin acitve site so specific ?

A

There is a negatively charged group in the active site, which means that only positive side chain groups can bind there

128
Q

Why is the elastase active site so specific?

A

It has 2 Valine amino acids attached on the inside of the pocket which means the active site is small. meaning that only small side chains can enter

129
Q

What is chymotrypsin made of and what are the bonds present?

A

Its made of 3 chains joined by disulphide bridges

130
Q

How is the nucleophile in chymotrypsin formed?

A

By the catalytic traid of (D/H/S. the AA side chains form the triad)

131
Q

What are the steps to the chymotrypsin reaction mechanism?

A
  1. Nucleophilic attack on polypeptide carbonyl (to make the OH group more reactive)
  2. Covalent intermediate (entire polypeptide attached to Ser)
  3. Cleavage and loss of C-terminal fragment
  4. Nucleophilic attack on polypeptide carbonyl by water (hydrolysis): His removes H from water [acid/base catalysis] to make an OH- nucleophile)
  5. Different covalent intermediate formed
  6. Cleavage and loss of N-terminal fragment

Look at lecture 18 for diagrams of mechanism

132
Q

What can be used to test for the presence of serine proteases and why?

A

DIPF and TPCK

DIPF reacts with ONLY Ser195 (not other Ser)

TPCK reacts with ONLY His57 (but not other His)

133
Q

What the reason for the presence of an oxyanion hole?

A

To help stabilise the transition state

134
Q

What are the two forms the oxyanion hole come in and what does each form do?

A
  1. Planar: destabilising the substrate
  2. Tetrahedral: stabilising of transition state
135
Q

Name some other proteases which also cause a nucleophilic attack on peptide bonds?

A
  1. Aspartyl proteases e.g. pepsin
  2. cysteine proteases
  3. Metalloproteases

BIOL1007 (8 decks)

Brainscape helps you reach your goals faster, through stronger study habits.
© 2024 Bold Learning Solutions. Terms and Conditions