Enzymes Flashcards

(53 cards)

1
Q

catalytic proteins that increase the rate of
biological reactions within the cells of the body.

A

Enzymes

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2
Q

T/F. enzymes lower the activation energy for a chemical reaction

A

T

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3
Q

T/F. More energy is required to convert reactant molecules to products, which increases the rate of a biochemical reaction compared to the rate of an uncatalyzed reaction.

A

F

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4
Q

are proteins capable of catalyzing covalent bond cleavage & formation

A

Enzymes

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5
Q

endow cells with the capacity to exert kinetic control over thermodynamic potentiality

A

Enzymes

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6
Q

are the agents of metabolic function

A

Enzymes

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7
Q

*key attributes of enzymes
- enormous acceleration of rate of chemical transformations

A

– catalytic power —

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8
Q

*key attributes of enzymes
— can selectively bind and process substrates over closely-related molecular species

A

– specificity

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9
Q

— functional in aqueous environments at low
temperatures (as found in cells)

A

– reactivity conditions

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10
Q

– consist only of a polypeptide chain; it is the tertiary protein structure of the simple enzyme that makes it biologically active.

A

Simple proteins

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11
Q

protein portion is inactive without a cofactor; the cofactor is the nonprotein portion of an enzyme, such as a metal ion that is necessary for enzyme activity; if the cofactor is an organic compound, usually a vitamin, it is called a coenzyme.

A

Conjugated proteins -

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12
Q

protein portion of the enzyme, inactive

A

apoenzyme

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13
Q

apoenzyme + cofactor, active enzyme

A

holoenzyme

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14
Q

organic compounds derived from B vitamins (coenzymes) –inorganic metal ions

A

cofactors

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15
Q

An organic molecule bound to the enzyme by weak interactions / Hydrogen bonds

A

coenzyme

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16
Q

important for the chemically reactive
enzymes

A

Cofactors

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17
Q

small organic molecules or Inorganic ions

A

Cofactors:

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18
Q

Transfer of electrons (hydride ions or H atoms)

A

Oxidoreductase

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19
Q

Group transfer reactions

A

Transferas

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20
Q

Reaction where in it transfers functional groups to water

A

Hydrolases

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21
Q

Addition of groups to double bonds, or formation of double bonds by removal of groups

A

Lyases

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22
Q

Transfer of groups within molecules to yield isomeric forms

23
Q

Formation of C-C, C-S, C-O, and C-N bonds by condensation reactions coupled to ATP cleavage

24
Q

oxidation of substrate

25
reduction of substrate
reductases
26
introduction of a double bond by the removal of hydrogen from substrate
dehydrogenase
27
transfer phosphate group
kinases
28
– transfer amino group
transaminase
29
hydrolysis of peptide linkages in protein
protease
30
hydrolysis of glycosidic bonds in carbohydrates
carbohydrase
31
hydrolysis of ester linkages in lipids
lipases
32
hydrolysis of sugar-phosphate ester bonds in nucleic acids
nucleases
33
hydrolysis of phosphate ester bonds
phosphatases
34
removal/addition of water from substrate
dehydratases/hydratase
35
removal of carbon dioxide
decarboxylases
36
removal of ammonia
deaminases
37
conversion of D to L or vice versa
racemases
38
transfer of functional grp w/in a molecule
mutases
39
conversion of a sugar epimer into another
epimerases
40
formation of new bond w/ ATP
synthetases
41
formation of new bond w/ ATP & CO2
carboxylases
42
speeds a reaction by lowering the activation energy, changing the reaction pathway
enzyme
43
Pockets or clefts in the surface of the enzyme
active site
44
The part of the enzyme combining with the substrate
active site
45
The enzyme and substrate are made to fit exactly
Lock and Key Enzyme Model
46
This model fails to take into account protein conformational changes to accommodate a substrate molecule
Lock and Key Enzyme Model
47
enzyme action assumes that the enzyme an active site is more a flexible pocket whose conformation changes to accommodate the substrate molecule
Induced Fit Enzyme Model
48
the ability of an enzyme to bind only one, or a very few, substrates and thus catalyze only a single reaction.
Enzyme specificity
49
catalyze a particular reaction for one particular substrate only and will have no catalytic effect on substrates that are closely related
Absolute Enzyme Specificity
50
the enzyme catalyzes reactions involving any molecules with the same functional group
Group Enzyme Specificity
51
the enzyme catalyzes the formation or breaks up of only certain categories or type of bond
Linkage Enzyme Specificity
52
the enzyme recognizes only one of two enantiomers
Stereochemical:
53
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