Ch 3 - Enzymes Flashcards

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1
Q

substances that speed up reactions without being permanently altered

A

catalysts

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2
Q

energy input required to initiate a chemical reaction

A

activation energy

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3
Q

reactants in an enzyme-catalyzed reaction

A

substrates

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4
Q

particular binding site on an enzyme

A

active site

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5
Q

typical suffix in the names of enzymes

A

“-ase”

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6
Q

model that describes how the active site of an enzyme changes shape to tightly bind the substrate molecule

A

“induced fit” model

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7
Q

enzyme that breaks down sucrose

A

sucrase

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8
Q

enzyme that breaks down proteins

A

proteases

there are many specialized proteases - may also be called peptidase

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9
Q

enzymes that break down lipids

A

lipase

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10
Q

enzymes that build nucleic acid molecules by adding nucleotides to nucleic acid strands

A

polymerase

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11
Q

How does enzyme concentration affect reaction rate?

A

As enzyme concentration increases reaction rate increases

more enzymes, more frequent collisions between enzymes and substrates

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12
Q

How does substrate concentration affect reaction rate?

A

As substrate concentration increases reaction rate increases

more substrates, more frequent collisions between enzymes and substrates

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13
Q

How does temperature affect enzyme function?

A

Optimum temp: greatest number of collisions.
Heat: speeds up molecular movement - but too much will “denature” the enzyme shape
Cold: molecules move slower - thus decreasing collisions
(all enzymes have an optimal temp)

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14
Q

How does pH affect enzyme function?

A

changes in pH (H+ concentration) will disrupt bonding between enzymes and substrates.
changes in pH can also change the shape of the enzyme itself (thus changing the very specific shape of the active site)
(all enzymes have an optimal pH)

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15
Q

Inorganic compounds that help enzymes function

A

cofactors

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16
Q

Organic compounds that help enzymes function

A

coenzymes

17
Q

Compounds that reduce enzyme activity by blocking the enzyme’s active site

A

competitive inhibitor
(this is “competitive inhibition”)
compounds “compete” for active site so substrate cannot bind

18
Q

Compounds that reduce enzyme activity by binding to the enzyme (at allosteric site - other than active site) and change the enzyme’s shape

A

non-competitive inhibitor
(“non-competitive inhibition”)
this causes the active site to no longer be functional

19
Q

Inhibition in which the inhibitor permanently binds to enzyme by covalent bonding

A
Irreversible inhibition
(competitor=binds at active site)
(allosteric=binds to other "allosteric" site)
20
Q

Inhibition in which the final product of the pathway inhibits one of the earlier steps in the pathway

A

Feedback Inhibition

21
Q

An overall chemical reaction that is divided up into many small steps (a series of chemical reactions)

A

metabolic pathway
(this is the normal organization of the complex chemical reactions that drive live processes - each step typically involves its own specific enzymes)