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DS1101 - S1 Y1 > Week 4 - Enzymes > Flashcards

Week 4 - Enzymes Flashcards

1
Q

What are enzymes

A

Enzymes are biological catalysts (protein)
- nearly all enzymes are globular proteins

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2
Q

What is the function of enzymes

A
  • increase the rate of a reaction
  • some catalyze the reaction of only one compound e.g. urease
  • some catalyze reactions of specific types of compounds or bonds
  • some change a particular functional group into another functional group

they stabilise the transition state for the reaction, lowering activation energy and increasing the rate of reaction.

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3
Q

Example of enzymes in dentistry

A

Pellicle Proteins:
- a-amylase lysozyme - protect enamel surfaces

Saliva Proteins:
- carbonic anhydrase VI isoenzyme - regulates pH in oral environment
- a-Amylase
- lysozyme
- lipase

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4
Q

What are cofactors

A

Only some enzymes require them but they are any non protein component of an enzyme which are either
coenzymes such as Coenzyme A (CoA) or
Metal ions such as Zn 2+, Mg2+ (or metal complexes

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5
Q

What are coenzymes

A

cofactors made from organic molecules
e.g. Coenzyme A (CoA)

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6
Q

What are apoenzymes

A

The protein component of an enzyme that requires a cofactor

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7
Q

What are holoenzymes

A

The combination of the apoenzyme (protein part) and cofactor (non protein part)

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8
Q

What is a substrate

A

the reactant that is going to be catalysed
e.g. phosphoenol pyruvate, ADP substrates for pyruvate kinase

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9
Q

What is an active site

A

A molecular crevice on the surface of the enzyme where the substrate (reactant to be catalysed) will fit during the reaction

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10
Q

What is a transition state

A

The intermediate stage of a reaction where the substance is neither the reactant or product

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11
Q

Describe the lock and key models

A

When the substrate (key) fits the active site (lock) catalysis can occur

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12
Q

Describe the induced fit model

A

the substrate approaches the enzyme, the enzyme senses the incoming substrate, and it adapts the active site to achieve a perfect fit with the substrate to the active site. So it’s not an inflexible lock, it creates an induced fit, which optimises the interaction with the active site upon bonding to form.

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13
Q

How do substrates bind to the active sight

A

intermolecular forces (h-bonds, salt-bridges) to AA side chains of the active site (enzymes are proteins)

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14
Q

What are the 6 major enzyme classification classes

A
  • Oxidoreductases
  • Transferases
  • Hydrolases
  • Lyases
  • Ligases
  • Isomerases

(Over The HILL)

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15
Q

What does a oxidoreductases do

A

oxidation - reduction reaction

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16
Q

What does a transferases do

A

group transfer reactions
they catalyse the transfer of functional groups from one molecule to another

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17
Q

What does a hydrolases do

A

hydrolysis reactions: that is the addition of a water molecule to a bond, resulting in bond breakage.

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18
Q

What do lyases do

A

addition of a group to a double bond or the removal of a group to form a double bond.

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19
Q

What do ligases do

A

Enzyme which uses ATP to form bonds

enzymes which catalyse a reaction in which a C-C, C-S, C-O or C-N bond is made or broken. This is accompanied by an ATP-ADP interconversion.
Joining of two substrates using ATP

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20
Q

What do Isomerases do

A

Isomerization reaction
Isomerases rearrange the functional groups within a molecule and catalyze the conversion of one isomer into another.

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21
Q

Example of a oxidoreductase enzyme

A

lactate dehydrogenase

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22
Q

Example of a transferases enzyme

A

pyruvate kinase
or Hexokinase (step 1 glycolysis) - transfers phosphate group

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23
Q

Example of a hydrolase enzyme

A

Lipase - hydrolysis of triglycerides into glycerol and FA

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24
Q

Example of a lyases enzyme

A

carbonic anhydrase
takes CO2 which has a double bond in it, adding water to it and turning it into carbonic acid

adolase (step 4 glycolysis) - breaks down F-6,1-P into DHAP and GAP

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25
Example of a ligases
DNA ligase (DNA rep step 6)
26
Example of a isomerases enzyme
GAP triose phosphate isomerase (glycolysis step 5) Phosphoglucoisomerase - step 2 glycolysis (G-6-P into F-6-P)
27
What is the enzyme catalyzed Reaction
28
What are Michaelis-Menten Kinetics
??
29
What are the main 5 amino acids which participate in the active sites in more than 65% of the enzymes
His > Cys > Asp > Arg > Glu - Histidine - Cysteine - Aspartate - Arginine - Glutamate 4 out 5 have either acidic or basic side chains
30
What are the active site functions? (3)
- brings the reacting atoms of the substrate (s) together - Moving reacting parts apart to stretch a bond to be broken - adding H+ to increase the speed of acid catalysed reaction
31
Explain pyruvate kinase as a enzyme
Pyruvate kinase catalyses the transfer of PO4 3- to ADP in glycolysis Coenzyme = ADP 2 cofactors = Mg2+ and K+ are found in the active site where catalysis occurs. Substrates = PEP (PhosphoEnolPyuvate) and ADP
32
What are the characteristics of the active site
- lot of acidic and basic side chains around the enzyme - Hydrophobic pockets - Both a specific shape and polarity to fit the substrate We are packing substrate/s and cofactors into the active site (so a very busy environment)
33
What are Isoenzyme/Isozymes
An enzyme that occurs in multiple forms, each catalyses the same reaction but in different environments
34
Example of an Isoenzyme/Isozyme
Lactate dehydrogenase (LDH) which catalyses the oxidation of lactate to pyruvate It has H4 isoform which is in the heart and a M4 isoform which is in the liver and skeletal muscle
35
What is the turn over number
The number of catalytic reaction events/s at the active site - the number of catalytic reaction events at the active site and the enzyme per second
36
What can the maximum speed of an enzyme be describe as
Maximum velocity which has the units of micro moles per litre of product per second Vmax REFERS TO PRODUCTS
37
What does enzyme activity mean
Catalytic ability to convert substrate to product expressed in catalytic units (U) 1U = 1 micro mole substrate/min REFERS TO REACTANTS
38
What is the activity of an enzyme-catalyzed reaction influenced by ( 5 factors)
- enzyme concentration - substrate concentration - temperature - pH - presence of cofactors
39
What does this graph represent
substrate concentration vs enzyme rate
40
What does this graph represent
Enzyme concentration vs enzyme rate
41
What does this graph represent
Temperature vs enzyme rate - peak = optimal temperature - low trough has no activity due to insufficient energy to reaction - second low trough, temperature is too high and the protein denatures, or enzyme is too flexible and the induced fit doesn't work well so the activity falls off
42
What does this graph represent
pH vs enzyme rate - peak = optimum pH
43
What are proenzymes (zymogens)
An inactive form of an enzyme that must have part of protein chain cleaved(removed) to become the active enzyme. e.g. trypsin
44
Example of a proenzyme (zymogen)
Trypsin (active enzyme), trypsinogen (proenzyme) A digestive protease is synthesized and stored as the proenzyme trypsinogen, which has no enzyme activity until its hydrolyzed from the N-terminal.
45
What is protein modification
A process of changing enzyme activity by covalently modifying it
46
Example of protein modification
Pyruvate kinase (PK) PK is the active form of the enzyme and when it is phosphorylated by protein kinase A (PKA) it forms PK-Pi which is an inactive enzyme. PK-Pi can then be activated by phosphatase.
47
What is activation in enzymes
Any process that initiates or increases the activity of an enzyme
48
What is inhibition in enzymes
Any process that makes an enzyme less active or inactive. Slows the rate of an enzyme catalyzed reaction.
49
What are the types of enzyme inhibition
- competitive inhibitor (reversible) - competitive inhibitor (irreversible) - non- competitive inhibitor (reversible) - Non-competitive inhibitor (irreversible)
50
What are competitive inhibitors (reversible)
Substance that binds to the active site of an enzyme thus preventing the substrate to bind to it. This substance can be removed
51
Example of a competitive inhibitor (reversible)
Methotrexate which inhibits the metabolism of dihydrofolate. Used in chemotherapy.
52
What is competitive inhibitor (irreversible)
A substance that binds to the active site and blocks substrate entry. Cannot be removed
53
Example of a competitive inhibitor (irreversible)
Penicillin An antibacterial drug which works as a transpeptidase inhibitor. It binds irreversible to the active site. Transpeptidase catalyzes the last step of cell wall synthesis for bacteria.
54
What are non competitive inhibitors
Substance that changes the shape of the active site but isn't attached to the active site.
55
Example of a non competitive inhibitor (reversible)
ATP inhibits citrate synthase (TCA S1)
56
Example of a non competitive inhibitor (irreversible)
- Propecia
57
What is allosteric control
The inhibition or activation of enzymes by a regulatory molecule which binds to a site other than the active site - regulating the activity of the enzyme A type of enzyme regulation based on an event occurring on the enzyme not at the active site which create change in the active site.
58
What is an allosteric enzyme
An enzyme which undergoes allosteric regulation, and they often have multiple polypeptide chains (quaternary structure)
59
What are the types of allosteric control
- negative modulation - positive modulation
60
What is negative modulation
Allosteric control which the active site is changed to inhibit an allosteric enzyme
61
What is positive modulation
Allosteric control where the active site is changed to activate an allosteric enzyme
62
What is a regulator (ligand)
The substance which binds to an allosteric enzyme which causes the change in the active site structure

DS1101 - S1 Y1 (63 decks)

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