Enzyme Flashcards

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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

A

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

A

pH

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
Q

when adding amount of enzyme has no effect on reaction rate because all substrate is bound

A

enzyme saturation

26
Q

receptor site that is close to but not directly on the active site of the enzyme

A

allosteric site

27
Q

shapes of enzymes (active/inactive) that enzymes will oscillate between

A

conformations

28
Q

chemicals that bind to specific enzymes and inhibit enzyme activity, important as enzyme activity must be controlled to coordinate cellular activities

A

enzyme inhibitors

29
Q

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

A

competitive inhibitor

30
Q

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

A

allosteric inhibitor

31
Q

chemicals that bind to active site/allosteric site and turn on/enhance/stimulate enzyme activity, allowing cellular activity coordination

A

activators

32
Q

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

A

allosteric activator

33
Q

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

A

substrate activator

34
Q

inorganic ions (copper, zinc, iron) located in active site, attracting electrons from substrate, increasing binding ability between enzyme and substrate

A

cofactors

35
Q

organic non-protein molecules that are cofactors

A

coenzymes

36
Q

more permanent cofactors/coenzymes, bound more tightly, sometimes with a covalent bond to active site

A

prosthetic groups

37
Q

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

A

feedback inhibition