Enzymes Flashcards

(52 cards)

1
Q

Macromolecules that catalyze chemical reactions in the body and increase the rate of chemical reactions without themselves being changed in the overall
process

A

Enzymes

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2
Q

Majority of all known enzymes are what type of protein shape?

A

Globular

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3
Q

Are all enzymes proteins? True or false

A

False

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3
Q

Enzymes made of ribonucleic acids

A

Ribozymes

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3
Q

Most enzymes are very specific. True or false

A

True

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4
Q

inhibits the enzyme that forms cell walls of bacteria, destroying the bacterium

A

Penicillin

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4
Q

causes blood vessels to narrow, increasing blood pressure.

A

ACE (angiotensin-converting enzyme)

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4
Q

given to those with high blood pressure to prevent ACE’s synthesis from it’s zymogen

A

ACE inhibitors

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5
Q

allows the virus to make copies of itself

A

HIV protease

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6
Q

interfere with this copying,
decreasing the virus population in the patient

A

HIV protease inhibitors

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7
Q

These are enzymes consisting of only amino acid units

A

Simple enzymes

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8
Q

These are enzymes that consist of a protein part and a non-protein part

A

Conjugated enzymes

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9
Q

The protein part of an enzyme

A

Apoenzyme

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10
Q

When an enzyme or apoenzyme is inactive, it is called..?

A

Proenzyme

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11
Q

The non-protein inorganic part of an enzyme (ex. iron, zinc, copper)

A

Cofactor

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12
Q

The non-protein organic part of an enzyme (ex. B vitamins, NAD)

A

Coenzyme

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13
Q

A functioning enzyme that consists of both the protein and nonprotein parts is called..?

A

Holoenzyme

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14
Q

a model states that the active site is
a rigid cavity; to react, the substrate must exactly match the shape of the active site.

A

Lock and key model

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14
Q

involved when oxygen acts as an acceptor of hydrogen or electrons.

A

Oxidases

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15
Q

the substance acted on by an enzyme

A

Substrate

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15
Q

The substrate binds to a specific portion of the enzyme during the reaction, called..?

15
Q

a model that assumes that the substrate plays a role in
determining the final shape of the enzyme and that the enzyme is partially flexible.

A

Induced fit model

16
Q

Enzymes that catalyze the oxidation-reduction
between two substrates

A

Oxidoreductase

17
Q

oxidize a substrate by transferring hydrogen to an acceptor that is either NAD+/NADP+ or a flavin enzyme

A

Dehydrogenases

18
catalyzes the reduction of hydrogen peroxide (H2O2)
Peroxidases
19
add hydroxyl groups (OH) to its substrates
Hydroxylases
20
incorporate oxygen from molecular oxygen into organic substrates
Oxygenases
21
catalyze reductions, in most cases reductases can act like an oxidases
Reductases
22
Enzymes that catalyze the transfer of a functional group between two substrates
Transferase
23
an enzyme that catalyzes the transfer of a phosphate group from ATP to a specified molecule
Kinase
24
catalyzes the addition of a phosphate group from an inorganic phosphate (HPO4) to a substrate
Phosphorylases
25
Enzymes that catalyze the hydrolysis of esters, carbohydrates, and proteins (polypeptides)
Hydrolase
26
Enzymes that catalyze the removal of groups from substrates by mechanisms other than hydrolysis
Lyase
27
Enzymes that catalyze the interconversion of stereoisomers and structural isomers
Isomerase
28
Enzymes that catalyze the linking of two compounds by breaking a phosphate anhydride bond in ATP
Ligase
29
Organic compounds required by many enzymes for catalytic activity
Coenzymes
30
organic compounds that are loosely bound to an enzyme and dissociates in an altered form as part of the catalytic cycle
Cosubstrates
31
coenzymes that are tightly (or covalently) and permanently bond to a protein
Prosthetic group
32
Any process that initiates or increases the action of an enzyme
Activation
33
Any process that makes an active enzyme less active or inactive
Inhibition
34
has a shape and structure similar to the substrate, so it competes with the substrate for binding to the active site
Competitive inhibitor
35
It is a lipase inhibitor that prevents the breakdown of fat
Orlistat
36
Binds to some other portion of the enzyme surface and sufficiently alter the tertiary structure of the enzyme so that its catalytic effectiveness is eliminated
Non-competitive inhibitor
37
The amount factor that affects enzyme activity
Enzyme and substrate concentration
38
The hotness and coldness that affects enzyme activity
Temperature
38
The factor in which, if it is too far from the optimum level, the enzyme will not function
pH
38
An interaction takes place at a position other than the active site but affects the active site
Allosterism
38
Inactive enzymes and are activated by the cleavage of one or a few peptide bonds
Zymogens or proenzymes
38
The activation or inhibition of the first reaction in a sequence is controlled by a product in the reaction sequence
Feedback control
39
the binding substance
Regulator
39
the site where the binding substance attaches
Regulatory site
40
Enzymes that differ in amino acid sequence but catalyze the same chemical reaction
Isozymes