C1.1 Enzymes and Metabolism Flashcards

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1
Q

enzyme

A

mainly proteins that function as biological catalysts

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2
Q

catalyst

A

a substance that speeds up the rate of a chemical reaction

effective in small amounts and remain unchanged at the end of the reaction

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3
Q

what are enzymes

A

globular proteins

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4
Q

features of a globular protein

A

rounded and spherical
functional - catalysts
mostly soluble
irregular amino acid sequence

ex. haemoglobin, insulin, catalase

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5
Q

what is the shape of an enzyme determined by

A

folding of protein
amino acids in the primary structure of protein
DNA genetic code

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6
Q

metabolism

A

chemical reactions in the body

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7
Q

role of enzyme in metabolism

A

if there are no enzymes - reactions at slow rate
enzyme speeds up reactions

wrong collisions would occur

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8
Q

what is the point of enzyme specificity

A

metabolic processes can be closely controlled

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9
Q

how are enzyme specificty classified

A

according to the type of reaction they catalyse and names according to substrate

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10
Q

collision in enzyme action

A

parts are in continual random molecular motion
by chance collisions will occur

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11
Q

catalysis in enzyme action

A

substrates bind to the enzymes active site which undergoes induced fit to achieve the proper alignment and enable the enzyme to perform its catalytic function

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12
Q

release in enzyme action

A

products leave active site
enzymes left unchanged - can be reused

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13
Q

anabolism

A

synthesis of complex molecules from simpler molecules including the formation of macromolecules from monomers

building up

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14
Q

examples of anabolism

A

synthesis of proteins from amino acids
synthesis of polysaccharides from sugars
photosynthesis

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15
Q

endergonic

A

energy requiring reactions - anabolism

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16
Q

catabolism

A

breakdown of complex molecules into simpler molecules including the hydrolysis of macromolecules into monomers

breaking down

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17
Q

examples of catabolism

A

hydrolysis of macromolecules into monomers in digestion

18
Q

exergonic

A

energy releasing reactions - catabolism

19
Q

active site

A

the binding point where the substrate binds with enzyme to produce product

20
Q

enzyme substrate complex

A

temporary structure formed when a substance binds to the active site of an enzyme

21
Q

properties needed in active site

A
  • binding to substrate molecule
  • holding on to it during chemical reactions
  • lowering energy of transition state
22
Q

induced fit

A

binding of the substrates causing slight change in the shape of the enzyme to enhance catalytic activity

23
Q

lock and key model

A

enzyme is the lock and substrate is the key

shape of the key must match lock and one key opens one lock

24
Q

hand in glove OR induced fit model

A

in induced fit model because the active site change to fit substrate to ensure optimal fit

most enzymes follow this

25
Q

why is movement needed in enzymic reactions

A

needed for a substrate molecule and an active site to come together

greater the kinetic energy greater the chance of collisions

26
Q

immobilised enzymes

A

enzymes attached to an inert, insoluble material, enabling recovery, reuse and improved enzyme stability

27
Q

features of immobilised enzymes

A
  • more stable
  • provide better environment for enzyme activity
28
Q

how do enzymes get immobilised so they dont go away

A

enzyme may be entrapped between fibres or covalently bonded to a matrix

enzymes prevented from being washed away

29
Q

example of immobilised enzymes in job

A

widely used method in food processing, pharmaceuticals and waste water treatment

30
Q

enzyme immobilisation techniques

A

entrapment
absorption
covalent bonding
cross linking
affinity

31
Q

advantages of enzyme immobilisation

A
  • permits reuse of enzyme preparation
  • product is enzyme free
  • more stable and long lasting due to protection
32
Q

denaturation in enzymes

A

occurs when weak intramolecular (hydrogen bonds) interactions within enzyme formed between different amino acids break

changes 3D shape of active site so enzyme substrate complex can’t form

33
Q

effect of temperature in enzyme reactions

A

raising temperature speeds up a reaction
more kinetic energy means particles move faster and are more likely to collide

34
Q

what can extremely high temperature do

A

cause bonds of enzyme and active site to break that maintain structure

it will loose its shape and stop workinge

35
Q

effect of PH in enzymes

A

bonds are vulnerable to pH
each enzyme has an optimum pH for optimum rate
pH change causes change in shape of active site
activity of enzyme is reduced and rate of reaction slows

36
Q

activation energy

A

initial energy input in the reaction

36
Q

effect of substrate concentration in enzymes

A

increase causes rate of reaction to a certain point as there is more opportunity for collisions between enzyme and substrate

once all enzymes have bound a substrate any more substrate increase will have no effect on rate of reaction

37
Q

transition state

A

point where there is maximum value of energy

38
Q

effect of enzymes on activation energy

A

all chemical reactions require energy
- reactants need to have bonds weakened or broken
- molecules need to be reorientated
- new bonds need to be formed

39
Q

importance of bonds

A

store energy because theyre made of energyen

40
Q

how do enzymes catalyse chemical reactions by lowering activation energy

A
  • wearing or breaking bonds in the substrates
  • reorienting atoms in the substrates
  • forming new bonds