Enzyme Flashcards

(37 cards)

1
Q

globular proteins that catalyse chemical reactions in living organisms

A

enzyme

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2
Q

specific, increase rate of reaction, unchanged at the end of reaction

A

properties of enzymes

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3
Q

metabolic reactions must reach this point to form products

A

activation energy En

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4
Q

build molecules

A

anabolic reactions

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5
Q

break down molecules

A

catabolic reactions

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6
Q

lower the amount of activation energy needed, speeding up reactions, not used up or altered

A

how do enzymes work

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7
Q

releases heat, gibbs free energy is negative

A

exergonic

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8
Q

requires input of energy, gibbs free energy is positive

A

endergonic

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9
Q

reactant for a specific enzyme

A

substrate

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10
Q

interact with the substrate, causing physical stress in order to break bonds and create products, reducing activation energy

A

amino acid side groups

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11
Q

depression in the surface of the globular protein where substrate binds

A

active site

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12
Q

original model, goes straight from substrate + enzyme to enzyme substrate complex and enzyme + products

A

lock and key model

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13
Q

active site is caused by folding, enzyme adjusts its shape to allow substrate to fit exactly into active site

A

induced fit model

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14
Q

substrate and enzyme interacting, held together by hydrogen bonds and weak ionic interactions

A

enzyme substrate complex/transition state

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15
Q

minimum amount of energy required to start the reaction

A

activation energy

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16
Q

reduce the height of the energy barrier, lowering the activation energy required to start the reaction, increasing the rate of reaction

A

effect of enzyme on reaction

17
Q

factors that affect enzyme activity

A

temperature, pH, substrate concentration, enzyme concentration

18
Q

reaction rate increases as temperature increases within a temperature range towards optimal temperature

19
Q

enzyme denatures, loss of enzyme activity

A

above optimal temperature range

20
Q

enzyme is inactive

A

below optimal temperature range

21
Q

enzymes function best at an optimal pH, usually in the range of pH 6-8

22
Q

if amount of enzyme is kept constant and substrate concentration is increased, reaction rate increases until it reaches max

A

substrate concentration

23
Q

when adding substrate has no effect because all enzymes are part of an enzyme substrate complex

A

substrate saturation

24
Q

if amt of substrate is kept constant and enzyme concentration is increased, reaction rate increases until it reaches a maximum

A

enzyme concentration

25
when adding amount of enzyme has no effect on reaction rate because all substrate is bound
enzyme saturation
26
receptor site that is close to but not directly on the active site of the enzyme
allosteric site
27
shapes of enzymes (active/inactive) that enzymes will oscillate between
conformations
28
chemicals that bind to specific enzymes and inhibit enzyme activity, important as enzyme activity must be controlled to coordinate cellular activities
enzyme inhibitors
29
similar in shape to substrate and competes directly with substrate, binds to active site and inhibits enzyme function, can be overcome by increasing concentration of substrate
competitive inhibitor
30
binds to allosteric site and inhibits enzyme activity by altering enzyme conformation, causing active site to change shape, preventing substrate binding shutting off enzyme activity
allosteric inhibitor
31
chemicals that bind to active site/allosteric site and turn on/enhance/stimulate enzyme activity, allowing cellular activity coordination
activators
32
binds to allosteric site of enzyme, altering conformation of the enzyme, causing active site to change shape, stabilizing conformation for the substrate, turning on/enhancing enzyme activity
allosteric activator
33
substrate is activator and binds to active site, stabilizing conformation of the enzyme, allows additional active sites to bind more easily with substrate, turning on/enhancing enzyme activity
substrate activator
34
inorganic ions (copper, zinc, iron) located in active site, attracting electrons from substrate, increasing binding ability between enzyme and substrate
cofactors
35
organic non-protein molecules that are cofactors
coenzymes
36
more permanent cofactors/coenzymes, bound more tightly, sometimes with a covalent bond to active site
prosthetic groups
37
method of metabolic control where product formed later in sequence of reactions will allosterically inhibit an enzyme that catalyzes a reaction occurring earlier in the metabolic process
feedback inhibition