C1.1 Enzymes Flashcards

1
Q

Metabolism

A

A complex network of interdependent and enzyme catalyzed chemical reactions occuring in living organisms

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2
Q

Anabolic reactions

A

Synthesis of polymers from smaller monomers

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2
Q

Anabolic & catabolic acronym

A

Anabolic = assemble, catabolic = cut down

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3
Q

Effect on active site in - Catabolic Reactions

A

Enzymes active site affects the bonds in the substrate so they are easier to break. to smaller molecules

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3
Q

Enzymes

A

Biological catalysts which speed up the rate of a reaction without being used up themselves

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4
Q

Enzyme Info

A
  • reduce activation energy of a reaction
  • can work intracellular and extracellular
  • globular proteins
  • tertiary structure
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5
Q

Enzyme Mechanism

A

specificity = enzyme substrate complex = enzyme product complex = release of product

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6
Q

Lock-and-key assumptions

A

assumes the active site of an enzyme is rigid in its shape

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6
Q

Induced fit

A

suggests the active site is flexible and only assumes catalytic conformation after the substrate molecules bind to the site

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7
Q

Enzyme immobilisation

A

Enzymes can be immobolised by being embeded in the membrane of cells

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7
Q

Denaturation

A

An irrevsersible change to a proteins active site

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7
Q

How enzymes operate in anabolic reactions

A
  1. enzymes hold substrates close together
  2. reduce repulsion
  3. bonds more easily
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8
Q

How enzymes operate in catabolic reactions

A
  1. enzymes active site puts strain on bonds
  2. fitting the substrate into active site puts strain on bonds
  3. easier to break
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9
Q

activation energy

A

energy needed to start a reaction

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10
Q

How PH affects enzyme activity

A
  • a change in pH from the optimum affects the charges of the enzyme proteins
  • alters 3e structure
  • denaturation
  • goes up and rapidly down
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11
Q

How substrate concentration affects enzymes rate of reaction

A
  • increased substrate concentration leads to increased reaction rate as more ESC are formed
  • until saturation point
  • increases sub. conc. will not increase rate of reaction anymore as all enzymes active sites are occupied
  • no more ESC
  • plateaus
12
Q

Metabolic pathway

A

Any chain or cycle of linked reactions catalysed by enzymes

13
Q

competitive inhibitor mechanism

A
  • similar shape to substrate
  • binds to active site
14
Q

non competitive inhibitor mechanism

A
  • binds to allosteric site
  • substrate no longer fits
15
Q

Type of non competitive inhibition

End Product Inhibition

A

In order to control metabolic pathways the end product of the pathway can sometimes inhibit the activity of the first enzyme in the pathway

(avoids excessive prodcution & build up)

16
Q

competitive inhibitor

A

A mechanism in which the inhibitor competes with the substrate to bond with the actuve site

17
Q

non competitive inhibitor

A

A mechanism in which the inhibitor to an allosteric site away from the enzymes active site

18
Q

Metabolic rate

A

Amount of energy needed by that organism in a given time period

19
Q

mechanism (suicide) based inhibition

A

inhibitor binds permanently to the active site

ex: anti cancer, anti HIV, antibiotic

20
Inactive precursors
types of enzyme that have an inhibitor on it, this it only works in certain coniditions
21
# Inactive precursor Protease
* an inactive precursor * means that it only works under acidic PH conditions * to prevent protein degration
22
Why when substrate conc. increase; rate increase?
More frequent collisions
23
competitive inhibitor - descripitive graph
* slows down rate of reaction as it competes for active site * has a similar shape to substrate * binding is reversible * as substrate conc. increases; more binds to active site than competitor = reaction rate increases * plateaus as all active sites will be at full capacity
24
catabolism
breaking down complex molecules into smaller monomers
25
Importsnce of enzymes in metabolism
* lower activation energy * increase rate of reaction * end product inhibition can control metabolic pathways * specific enzyme for each substrate
26
Outline Lock and Key model
* explains specificity of enzyme-substrate * the substrate (key) fits into enzymes active site (lock) * active site can only be changed through temperature & pH changes => substrate cannot bind
27
Outline induced fit model
* as ESC is formed; active site changes to allow substrate to bind * substrate induces active site to change * bonds weakend in the substrate (easier to break) * easier to break bonds = lowers activation energy * opportunities for wider substrate specificity
28
How do bacteria develop resistance to penicillin?
* modifying the structure of their transpeptidase enzymes * prevents the irreversible binding of penicillin to the active site.