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Biochemistry > Enzymes > Flashcards

Enzymes Flashcards

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

A

Isomerases

23
Q

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

A

Ligases

24
Q

oxidation of substrate

A

oxidases

25
Q

reduction of substrate

A

reductases

26
Q

introduction of a double bond by the removal of hydrogen from substrate

A

dehydrogenase

27
Q

transfer phosphate group

A

kinases

28
Q

– transfer amino group

A

transaminase

29
Q

hydrolysis of peptide linkages in protein

A

protease

30
Q

hydrolysis of glycosidic bonds in carbohydrates

A

carbohydrase

31
Q

hydrolysis of ester linkages in lipids

A

lipases

32
Q

hydrolysis of sugar-phosphate ester bonds in nucleic acids

A

nucleases

33
Q

hydrolysis of phosphate ester bonds

A

phosphatases

34
Q

removal/addition of water from substrate

A

dehydratases/hydratase

35
Q

removal of carbon dioxide

A

decarboxylases

36
Q

removal of ammonia

A

deaminases

37
Q

conversion of D to L or vice versa

A

racemases

38
Q

transfer of functional grp w/in a molecule

A

mutases

39
Q

conversion of a sugar epimer into another

A

epimerases

40
Q

formation of new bond w/ ATP

A

synthetases

41
Q

formation of new bond w/ ATP & CO2

A

carboxylases

42
Q

speeds a reaction by lowering the activation energy, changing the reaction pathway

A

enzyme

43
Q

Pockets or clefts in the surface of the enzyme

A

active site

44
Q

The part of the enzyme combining with the substrate

A

active site

45
Q

The enzyme and substrate are made to fit exactly

A

Lock and Key Enzyme Model

46
Q

This model fails to take into account protein conformational changes to accommodate a substrate molecule

A

Lock and Key Enzyme Model

47
Q

enzyme action assumes that the enzyme
an active site is more a flexible pocket whose conformation changes to
accommodate the substrate molecule

A

Induced Fit Enzyme Model

48
Q

the ability of an enzyme to bind only one, or a very few, substrates and thus catalyze only a single reaction.

A

Enzyme specificity

49
Q

catalyze a particular reaction for one particular substrate only and will have no catalytic effect on substrates that are closely related

A

Absolute Enzyme Specificity

50
Q

the enzyme catalyzes reactions involving any molecules with the same functional group

A

Group Enzyme Specificity

51
Q

the enzyme catalyzes the formation or breaks up of only certain categories or type of bond

A

Linkage Enzyme Specificity

52
Q

the enzyme recognizes only one of two enantiomers

A

Stereochemical:

53
Q

v

A

Biochemistry (10 decks)

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