Enzyme Mechanisms Flashcards

1
Q

enzyme

A

biological catalyst that speed up rates of reaction that would otherwise be too slow to support life

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2
Q

catalyst

A

a chemical agent that changes the rate of reaction without being consumed by the reaction

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3
Q

substrate

A

reactant that enzyme acts on

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4
Q

active site

A

a pocket where the substrate binds - catalytic center where substrate is converted to product

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5
Q

where do enzymes act on substrates?

A

at their active site

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6
Q

what are enzymes composed of?

A

proteins (except 1) - ribozyme

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7
Q

how many reactions can an enzyme catalyze?

A

JUST ONE they are reaction specific

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8
Q

metabollic enzymes work in which direction?

A

most work both BOTH - forward and reverse

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9
Q

what does it mean to be substrate specific?

A

an enzyme can recognize one specific set of substrates related to the reaction it catalyzes

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10
Q

An enzyme can only act on one substrate but substrates can have multiple enzymes that react on it

A
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11
Q

what are the main types of enzymes?

A

simple, complex

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12
Q

what are the states of complex enzymes?

A

apoenzyme, holoenzyme

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13
Q

simple enzyme

A

composed only of protein component

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14
Q

complex enzyme

A

an enzyme that requires a cofactor to function in addition to its protein component

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15
Q

apoenzyme

A

inactive form of the enzyme because it is missing the cofactor

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16
Q

holoenzyme

A

active form of the enzyme with the cofactor

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17
Q

types of cofactors

A

inorganic, organic

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18
Q

examples of inorganic cofactors

A

metal ions, zinc, iron, copper

19
Q

examples of organic cofactors

A

usually from vitamins of their derivatives

20
Q

prosthetic group organic cofactor

A

covalently/permanently bonded to an apoenzyme

21
Q

coenzyme organic cofactor

A

non-covenlently/reversibly bound to an apoenzyme

22
Q

function of oxidereductase

A

shuffling electrons

23
Q

function of transferase

A

moving chemical groups

24
Q

function of hydrolase

A

breaking molecules with water

25
functions of lyase
breaking molecules without water
26
function of isomerase
changine molecular shapre (keeps the same atoms)
27
function of ligase
forming bonds between molecules
28
enzyme name ending
ase
29
what is the induced fit model?
as the substrate binds, the enzyme changes shape leading to a tighter fit bringing chemical groups in position to catalyze the reaction binding of a substrate induces a favourable change in the shape o the active site
30
exergonic reaction
exothermic - a reaction that releases energy
31
activation energy
amount of energy needed to push the reactants over an energy barrier
32
how do enzymes speed up a reaction?
lower the activation energy
33
what are the mechanisms for lowering activation energy?
1. proximity 2. bond strain 3. microenvironment 4. covalent catalysis
34
proximity & orientation description
active site brings reactants closer together and in the correct orientation
35
bond strain description
active site bends bonds in substrate making it easier to break
36
microenvironment description
creates a favourable environment for the reaction
37
covalent catalysis description
enzymes may bind covalently to substrates in an intermediate step before returning to normal
38
how does covalent catalysis increase reactionr rate
properly orienting the susbtrate, changing the chemistry at the active site
39
limitations to enzyme activity
substrate concentration temperature pH availability of cofactors
40
what is the correlation between substrate concentration and rate
direct, increase in concentration, increase speed of binding to active sites, increased reaction rate
41
what happens with enzyme saturation
active sites on all enzymes are engaged only way to increase productivity is to increase number of enzymes
42
increased temperature effects on enzyme activity
increased temp, increases speef of molecules, incrases collisions between substrate and active site
43