enzyme action Flashcards

1
Q

what are enzymes

A

biological catalysts that speed up metabolic reactions in living organisms by raising activation energy
catalysts remain unchanged at the end of the reaction
small amount can catalyse conversion of large no of substrates into product

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2
Q

turnover number

A

the number of reactions that an enzyme molecule can catalyse per second

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3
Q

what type of protein is an enzyme

A

globular protein
soluble in water bc of hydrophilic nature of R groups in their aa

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4
Q

why are enzymes important

A

to sustain life, chemical reactions must occur rapidly with the aid of enzymes

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5
Q

what is the role of enzymes in anabolic reactions

A

build up/synthesise large polymers
e.g. cellulose/long protein molecules
catalyses reaction

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6
Q

what is the role of enzymes in catabolic reactions

A

break down large organic molecules
e.g. disgestion of large organic molecule starch into monomer, release of energy during respiration
catalyses reaction

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7
Q

how does enzyme function

A

both intra/extraceullarly

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8
Q

example of an intracellular process

A

dna replication
dna polymerase, ligase
catalse, protects cell from damage by breaking down hydrogen peroxide to water and oxygen
4 polypeptide chains and a haem group, highest turnover number

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9
Q

example of an extracellular process

A

digestion
amylase, produce in salivary glands, digest starch to maltose

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10
Q

what is a metabolic pathway

A

series of consecutive reactions with each step being catalysed by a different enzyme, specific to substrate produced
cam be anabolic/catabolic
e.g. respiration, photosyntesis

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11
Q

what happens when one enzyme cannot function

A

whole metabolic pathway cannot run

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12
Q

what are metabolites

A

reactants, intermediaries, products

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13
Q

what are oxidoreductases

A

enzymes that catalyses the transfer of electron during oxidation and reduction reactions

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14
Q

transferases

A

the transfer of functional group from one molecule to another

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15
Q

hydrolases

A

catalyses hydrolysis

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16
Q

lyases

A

splitting of bonds

17
Q

isomerases

A

rearranging of molecule

18
Q

ligases

A

joining two molecules by forming covalent bonds

19
Q

general equation for enzyme-controlled reaction

A

enzyme + substrate –> enzyme-substrate complex –> enzyme product complex –> enzyme
+ product

20
Q

activation energy

A

energy to start the reaction

21
Q

how do enzymes increase the rate of a reaction

A

activation energy is transferred to break the bonds of reactants
enzyme lowers activation energy by creating a transition state between the enzyme and substrate that is more stable
if 2 substrate molecules need to be joined, attaching to enzyme holds them close together so they can bond more easily
if enzyme is catalysing a breakdown, fitting into active site puts a strain on the bonds in the substrate allowing molecule to break more easily

22
Q

what maintains the shape of the enzyme and active site

A

amino acids

23
Q

how does enzyme form

A

folding of sequence of amino acids

24
Q

lock and key hypothesis

A

substrate fits exactly into active site just like a key fitting a lock
held there with various bonds to form enzyme-substrate complex
1. substrate molecule is split into two or more products
2. more substrate molecules are joined together
complex only exists for a fraction of a second until the products are formed
products leave the active site and enzyme is free to take part in another reaction

25
induced fit hypothesis
active site initially not an exact fit for the substrate substrate moves into active site, forces between the two molecules, distort enzyme and active site enzyme substrate complex forms formation of complex lowers activation energy to form products products leave the active site and enzyme return to shape
26
cofactors
a small non-protein molecule attached to enzymes
27
two types of cofactors
activators and coenzyme
28
activators
inorganic groups that permanently bound to the enzyme and prosthetic group iron zinc copper
29
coenzymes
large organic molecules that bind temporarily to the enzyme transferring chemical groups that is necessary for reaction to occur nad vitamin b3, c atp
30
amylase as an example of cofactor
only digest starch if Cl- is present
31
precursor activation
inactive enzymes important bc some enzymes causes damage in their activated form undergo a change in shape to be activated, by addition of a cofactor precursor protein, apoenzyme before activation holoenzyme after activation