Enzymes and coenzymes Flashcards

1
Q

what is an enzyme?

A

biological catalysts which speed up rate of reaction - without altering the final eqm between reactants and products
they are not used up and are regenerated

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2
Q

are enzymes efficient?

A

extremely - catalase catalyses break down of H2O2 to water 10^4 times faster than the uncatalyzed reaction at 30C

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3
Q

how do enzymes catalyse reactions?

A

they provide an alternative pathway for the reaction with a lower activation energy

  • binding energy decreases overall energy by stabilising the transition state, orienting the substrates correctly and distorting reactants to a reactive state
  • it is reversible reaction
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4
Q

what is an isoenzyme?

A

enzymes that catalyse the same reaction but are different gene products

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5
Q

what does enzyme specificity mean

A

enzymes will only catalyse one reaction with specific substrate(s), including differences in stereoisomers

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6
Q

what is specificity determined by?

A

the shape of the active site where only the correct shaped and charged substrate can fit

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7
Q

what are the consequences of enzyme specificity?

A

group of enzymes present together in one compartment of a cell e.g. cytoplasm of muscle cells, can give rise to a complex and co-ordinated metabolic pathway

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8
Q

what are the 6 main classes of enzyme?

A
oxidoreductase
transferase
lyase
hydrolase
isomerase
ligase
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9
Q

what does oxidoreductase enzyme do?

A

catalyse transfer of H atoms and electrons (redox reactions)

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10
Q

what does transferase enzyme do?

A

catalyse transfer of functional groups from donors to acceptors

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11
Q

what does lyase enzyme do?

A

catalyse cleavage of C-C, C-O, C-N bonds (addition of groups to double bonds or formation of double bonds by removal of groups)

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12
Q

what does hydrolase enzyme do?

A

catalyse cleavage of bonds by addition of water (hydrolysis)

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13
Q

what does isomerase enzyme do?

A

catalyse transfer of functional group within the same molecule

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14
Q

what does ligase enzyme do?

A

use ATP to catalyse formation of new covalent bonds

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15
Q

what are the other three enzymes and what do they do?

A

phosphorylase - addition of inorganic P group
kinase - addition of P from ATP
phosphatase - removal of P group

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16
Q

what is the structure of an enzyme?

A

tertiary proteins - folded into complex 3D structures

stabilised by many weak bonds

17
Q

what bonds stabilise enzymes?

A

H bonds, ionic bonds, hydrophobic interactions

18
Q

what are the weak bonds in enzymes affected by?

A

easily broken
affected by temp and pH
generally sensitive to their environment

19
Q

what determines the shape of the active site?

A

amino acid side chains
- they are involved in the formation of ESCs
other parts if aa are used to channel the enzyme to the active site as part of the catalysis process

20
Q

what are the two models that allow binding of substrate to AS?

A

lock and key

induced fit

21
Q

how does lock and key work?

A

substrate fits directly into active site

22
Q

how does induced fit work?

A

conformation of the enzyme

  • substrate binds in closed configuration
  • active site forms around the substrate
23
Q

how does temp affect enzymes?

A
  • ROR inc up until the optimum temperature

- rate then dec as weak bonds in tertiary structure are broken so enzyme denatures and loses active site

24
Q

hoe does pH affect enzymes?

A

pH affects the weak bonds and so ROR will be fastest at optimum pH
-pH changes cause reversible changes to the enzyme as they will accept/donate a proton depending on the environment

25
Q

what is a co factor?

A

any substance that is required for an enzyme to be catalytically active

26
Q

what are coenzymes?

A

organic cofactors e.g. NAD

27
Q

what do co substrates do?

A

transfer groups from one enzyme to another

28
Q

what are prosthetic groups and their function?

A

co factors that are tightly bound to the enzyme and remain attached to it when catalysing the reaction; remain unchanged at the end of the reaction cycle