Enzymes Flashcards

(32 cards)

1
Q

a substance that slows down or stops the
normal catalytic function of an enzyme by binding to it.

A

Enzyme Inhibitor:

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2
Q

Compete with the substrate for
the same active site

A

Competitive Inhibitors

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3
Q

Binds to the enzyme at a location other than active site

A

Noncompetitive Inhibitors

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4
Q

A noncompetitive enzyme inhibitor decreases enzyme activity by binding to a site on an enzyme other than the active site (T/F)

A

True

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5
Q

An irreversible enzyme inhibitor inactivates enzymes by forming a strong covalent bond with the enzyme’s active site. (T/F)

A

True

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6
Q

A process in which activation or inhibition of the first reaction in a reaction sequence is controlled by a product of the reaction sequence.

A

Feedback Control:

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7
Q

An enzyme that catalyzes the transfer of a
functional group from one molecule to another

A

Transferase

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8
Q

catalyze transfer of an amino group to a
substrate

A

Transaminases

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9
Q

catalyze transfer of a phosphate group from
adenosine triphosphate (ATP) to a substrate

A

Kinases

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10
Q

an enzyme that catalyzes a hydrolysis
reaction

A

Hydrolase

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11
Q

an enzyme that catalyzes the addition of a group to a double bond or the removal of a group to form a double bond in a manner that does not involve hydrolysis or oxidation

A

Lyase

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12
Q

It effects the removal of the components of
water from a double bond

A

Dehydratase

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13
Q

It effects the addition of the components of
water to a double bonds

A

Hydratase:

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14
Q

an enzyme that catalyzes the
isomerization (rearrangement of atoms) reactions.

A

Isomerase

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15
Q

enzyme that catalyzes the formation of a
bond between two molecules involving ATP hydrolysis:

A

enzyme that catalyzes the formation of a
bond between two molecules involving ATP hydrolysis:

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16
Q

Most enzymes have optimal activity in the pH range of 7.0 - 7.5 (T/F)

17
Q

Pepsin optimum pH

18
Q

Trypsin optimum pH

19
Q

Number of substrate molecules converted to
product per second per enzyme molecule under conditions of optimum temperature and pH

A

Turnover Number

20
Q

Enzyme has a pre-determined shape for the active site

A

Lock-and-Key model

21
Q

Lock-and-Key model has only substrate of specific shape can bind with active site (T/F)

22
Q

Substrate contact with enzyme will change the shape of the active site

A

Induced Fit Model

23
Q

Specificity: with an enzyme will catalyze a particular reaction for only one substrate

A

Absolute Specificity

24
Q

Absolute Specificity is most restrictive of all specificities (T/F)

25
Specificity with enzyme can distinguish between stereoisomers.
Stereochemical Specificity
26
Small organic molecules or Inorganic ions that are important for the chemically reactive enzymes
Cofactors
27
Enzyme that is composed only of protein (amino acid chains)
Simple enzyme
28
Enzyme that has a nonprotein part in addition to a protein part.
Conjugated enzyme
29
They are catalysts and are not consumed in the reactions
Enzymes
30
The human body has 1000s of enzymes (T/F)
True
31
Enzyme activity is dramatically affected by (3)
Alterations in pH Temperature Other protein denaturants
32
Most enzymes are globular proteins (T/F)
True