Chapter 6 Flashcards

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1
Q

Oxidoreductases

A

oxidation-reduction reactions

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2
Q

Transferases

A

transfer functional groups from one molecule to another

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3
Q

Hydrolases

A

hydrolysis reactions - using water to break one molecule into two

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4
Q

Lyases

A

remove a group from one molecule and rearrange the electrons

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5
Q

Isomerases

A

convert two molecules with the same formula into different structures

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6
Q

Ligases

A

join two molecules together

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7
Q

What is the catalytic cycle of an enzyme?

A
  1. substrate binding
  2. substrate activation
  3. catalytic event
  4. product release
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8
Q

Name the 6 classes for enzyme nomenclature

A

oxidoreductases, transferases, hydrolases, lyases, isomerases, ligases

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9
Q

How does a catalyst increase the rate of a reaction?

A

by lowering the activation energy requirement

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10
Q

Activation Energy

A

how much energy required to get to a state to turn substrate into product

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11
Q

Active Site

A

where substrate binds to enzyme

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12
Q

Prostetic groups

A

small organic groups or metal ions on an enzyme that function as electron acceptors

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13
Q

Lock and Key Model

A

early model that explained enzyme specificity but not catalytic event

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14
Q

Induced Fit Model

A

when enzyme binds to substrate, both change shape

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15
Q

What is initial binding of substrate and enzyme caused by

A

RANDOM COLLISION!

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16
Q

Km

A

michaelis constant

specific substrate concentration at which the reaction proceeds at half it’s max speed

17
Q

Vmax

A

upper limit of reaction rate

only way to speed up is to get more enzymes

18
Q

Enzyme Regulation

A

mechanisms that adjust the rate of enzyme catalyzed reactions

19
Q

5 types of enzyme regulation

A
alter temp or pH, 
allosteric regulation,
 covalent modification, 
competitive inhibition, 
and substrate level regulation
20
Q

Competitive Inhibition

A

molecule binds to the active site so that substrates can’t bind

21
Q

what are substrate analogs

A

pretend substrates used in competitive inhibition

22
Q

Allosteric Regulation

A

binding of regulatory molecules at allosteric site that can turn molecule on or off

23
Q

Feedback Inhibition

A

when cell has made enough of the product, the product binds to the allosteric site and inhibits the enzyme that made it

24
Q

Covalent Modification

A

enzyme activity affected by addition or removal of chemical groups via covalent bonding

25
Q

Types of covalent modification

A

proteolytic cleavage and phosphorylation/dephosphorylation

26
Q

proteolytic cleavage

A

one-time irreversible removal of a portion of the polypeptide chain

27
Q

Ribozymes

A

RNA molecules that act as catalysts