enzymes Flashcards

1
Q

enzyme features

A
  • globular proteins (have a tertiary structure)
  • act as biological catalysts
  • alter rate without bring permanently changed or used up
  • able to be reused
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2
Q

how are enzymes biological catalysts

A

they speed up many metabolic reactions in living organisms

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3
Q

what is the turnover number

A

the number of reactions an enzyme can catalyse per second

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4
Q

how are enzymes (biological catalysts) different to chemical catalysts

A
  • chemical catalysts usually need high temps, increased pressures and an extreme ph
    —> however biological catalysts can speed reactions up to 10^12 times at lower temps, normal pressure and a neutral ph
  • enzymes are more specific
  • enzymes dont produce unwanted products
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5
Q

how do enzymes help if 2 substrates need to be joined

A

being attached to the enzyme holds them close together and reduces any repulsion so they can bond easily

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6
Q

how does an enzyme help break a stubstrate down

A

when the substrate fits into the active site, a strain is put onto the bonds in it, making it break down easier into smaller molecules

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7
Q

how do enzymes get their structure

A
  • they’re chains of AAs, therefore theyre coded for by the dna of the organism
  • the instructions for making enzymes are encoded in genes
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8
Q

what happens to the enzyme if a gene has a mutation on

A
  • it will alter the sequence of AAs
  • this may alter the enzymes tertiary structure and prevent it from functioning
  • this can then lead to problems with metabolic functions from; digestion, or the formation of blood vessel walls, joints and connective tissues
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9
Q

what is the active site

A
  • a specific indentation or cleft on the surface of an enzyme, it consists of about 6-10 AA
  • shape is complementary to the shape of the substrate
  • shape can be altered by temp or ph changes
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10
Q

where do enzymes work

A

they can catalyse both intracellular and extracellular reactions inside and outside of the cell

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11
Q

what are intracellular enzymes

A
  • work WITHIN cells and organelles
  • often over 1000 reactions occur simultaneously, each being catalysed by a different enzyme
    —> some of these are part of a metabolic pathway
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12
Q

what is a metabolic pathway

A

a series of connected chemical reactions that feed one another, each step catalysed by a different enzyme

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13
Q

what are metabolites

A

the intermediate products of metabolic reactions

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14
Q

what are the two types of metabolic pathways

A

anabolic - E is used to synthesise smaller molecules into larger ones
catabolic - large molecules are broken down into smaller ones, releasing E

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15
Q

what is catalase

A
  • a type of intracellular enzyme which identifies found in nearly all living organisms exposed to O
  • fastest acting enzyme - turnover number is 6mil per second
  • optimum pH in humans is ph7
  • optimum temp in humans is 45 degrees
  • found in vesicles - peroxisomes
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16
Q

what does catalase do

A
  • protects cells from damage by breaking down hydrogen peroxide into water and oxygen
  • used by WBCs to kill invading microbes when WBCs try to ingest pathogens
17
Q

catalase structure

A
  • 4 polypeptide chains and a haem group with iron
18
Q

what are extracellular enzymes

A

enzymes that have been secreted from cells and act on substrates outside of cells

19
Q

how is fungi use extracellular enzymes

A

it releases extracellular hydrolytic enzymes onto food (such as bread) which digest carbs, proteins and lipids, and then the products of digestion are absorbed into the fungal hyphae for growth and respiration

20
Q

what are cofactors

A

non -protein molecules that attach to enzymes and help them catalyse reactions, especially redox reactions

21
Q

what are prosthetic groups

A

they’re cofactors which are permanently bound, by covalent bonds, to an enzyme

22
Q

what is the prosthetic group on carbonic anhydrase

A

a zinc ion

23
Q

what is the equation for carbonic anhydrase and what does it do

A

carbon dioxide and water <—> carbonic acid <—> bicarbonate and H ion

  • the reaction enables CO2 to be carried in the blood from respiring tissues to the lungs
24
Q

what is an enzyme substrate complex

A

it forms when the substrate and enzyme molecules temporarily bind together

25
Q

what do other cofactors do

A
  • some aren’t permanently bound, and instead they temporary associate with either the substrate or the enzyme during reactions to increase rate
  • some change the charge or distribution of charge on the surface of the substrate or enzyme to make the ESC easier to form
  • some are cosubstrates and coenzymes
26
Q

what are cosubstrates

A

cosubstrates and the substrate together form the correct shape to bind to the active site

27
Q

what are coenzymes

A

small, organic non-protein molecules that temporarily bind to the active site just before, or at the same time as, the subtrate binds
—> they’re chemically changed during reactions and need to be recycled to their original state

28
Q

where are many coenzymes derived from

A

water -soluble vitamins