BIOCHEM: ENZYME Flashcards

1
Q

Catalysts for biochemical reactions

A

Enzymes

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2
Q

the substance on which an enzyme acts

A

Substrate

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3
Q

–substance produced by the action of enzyme on substrate

A

Product

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4
Q

– region or domain where the substrate binds

A

Active site

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5
Q

– nonprotein component that assists in catalysis

A
  • Cofactor
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6
Q

composed entirely of protein (AA chains)

A

Simple enzyme

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7
Q

– protein + nonprotein part

A

Conjugated enzyme

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8
Q

– biochemically active conjugated enzyme

A

Holoenzyme

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9
Q

provide additional chemically reactive functional groups
* May be permanently or temporarily bonded to the apoenzyme

A

Cofactors

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10
Q

– small organic molecules ← Vitamins

A

Coenzymes

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11
Q

– Zn2+, Mg2+, Fe2+, Fe3+, Cu+, Cu2+ ← Minerals

A

Metal ions

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12
Q
  • small portion that actually participates in the
    interaction with a substrate
A

Active Site

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13
Q

Intermediate reaction species that is formed
when the substrate binds to the active site

A

Enzyme-Substrate complex

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14
Q

The enzyme has enough
flexibility to allow for small
changes in its shape or geometry

A

Induced Fit Model

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15
Q

The active site has a fixed, rigid
geometrical conformation

A

Lock and Key Model

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16
Q

– enzyme catalyzes only one reaction;
e.g. catalase

A

Absolute specificity

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17
Q

enzyme acts only on molecules with a specific
functional group

A

Group specificity

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18
Q

– enzyme acts only on a specific chemical bond
e.g. phosphatase

A

Linkage specificity

19
Q

– enzyme acts only on a particular
stereoisomer

A

Stereochemical specificity

20
Q

Catalyzes an oxidation-reduction (redox) reaction

A

Oxidoreductase

21
Q

Catalyzes transfer of a functional group from one molecule to another

A

Transferase

22
Q

– catalyzes the transfer of an amino group

A

Transaminases

23
Q

catalyzes the transfer of a phosphate group

24
Q

Catalyzes a hydrolysis reaction

25
Catalyzes rearrangement of atoms (isomerization) of a substrate in a reaction, converting it into a molecule isomeric with itself
Isomerase
25
Catalyzes the addition of a group to a double bond OR removal of a group to form a double bond in a manner that DOES NOT involve hydrolysis or oxidation
Lyase
26
Catalyzes the bonding together of two molecules into one with the use of ATP
Ligase
27
Measure of kinetic energy of molecules
Temperature
28
– temperature at which an enzyme exhibits maximum activity
Optimum temperature
29
Can lead to changes on the charge of acidic and basic amino acids located on the active site
pH
30
Enzyme concentration is constant + Substrate concentration is increased → faster reaction rate until it reaches the maximum reaction rate (velocity)
Substrate Concentration
31
the number of substrate molecules transformed per minute by one molecule of enzyme under optimum conditions
Turnover number
32
molecule that sufficiently resembles the substrate in shape and charge distribution that it competes with the substrate for occupancy of the active site
Competitive inhibitor
33
as substrate concentration increases and enzymes become fully occupied
SATURATION
34
molecule that decreases enzyme activity by binding to a site other than the active site
Noncompetitive inhibitor
35
molecule that inactivates enzymes by forming strong covalent bonds to an amino acid side chain at the active site
Irreversible inhibitor
36
Process in which activation or inhibition of the first reaction in a sequence is controlled by a product of the reaction sequence
Feedback Control
37
inactive precursor of proteolytic enzymes
Zymogen (proenzyme)
38
adding or removing a group from enzyme by forming or breaking a covalent bond
Covalent modification
39
addition of a phosphate group ← kinases
Phosphorylation –
40
– removal of a phosphate group ← phosphatases
Dephosphorylation
41
Certain enzymes are not normally found in the blood and produced only in certain types of cells
Diagnosis
42
43