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Biochemistry > Enzymes > Flashcards

Enzymes Flashcards

1
Q

are complex biological molecules,
primarily or entirely protein, that behave as
biological catalysts.

A

Enzymes

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2
Q

Some enzymes consist entirely of proteins, whereas others have nonprotein portions known

A

Cofactors

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3
Q

This may be a metal ion, such as magnesium, or an organic substance.

A

Cofactor

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4
Q

This may be a metal ion, such as magnesium, or an organic substance.

A

Cofactor

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5
Q

An organic cofactor is called a

A

Coenzyme

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6
Q

An enzyme lacking its cofactor is an

A

Apoenzyme

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7
Q

The combination of an apoenzyme and its cofactor is a

A

Holoenzyme

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8
Q

This contains an apoenzyme and a metal ion cofactor

A

Metalloenzyme

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9
Q

A tightly bound coenzyme is a

A

Prosthetic group

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10
Q

The enzyme in an inactive form is called

A

Proenzyme or zymogen

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11
Q

One of the enzymes present in the
stomach that’s responsible for the digestion of
proteins.

A

Trypsin

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12
Q

the molecule upon which an enzyme
acts

A

Substrate

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13
Q

is foundational to enzyme kinetics, describing the rate of enzyme reactions as a function of substrate concentration

A

Michaelis-Menten model

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14
Q

The isomerization of molecules

A

Isomerases

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15
Q

The joining of two molecules

A

Ligases or synthetases

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16
Q

Additions to a double bond, or the formation of a double bond

A

Lyases

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17
Q

catalyze a simultaneous oxidation and a reduction

A

Oxidoreductases

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18
Q

is to catalyze the transfer of a group from one molecule to another

A

Tranferase

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19
Q

The term that transfers an amino group

A

Aminotransferase

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20
Q

The term that transfers a phosphoryl group

A

Photranferase

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21
Q

catalyze the cleavage of a bond through the insertion of a water molecule

A

Hydrolases

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22
Q

catalyzes the hydro- lysis of a monophosphate ester

A

Phosphatase

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23
Q

catalyzes the hydrolysis of a peptide bond

A

Peptidase

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24
Q

catalyze the removal of a group

A

Lyases

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25
Q

enzymes catalyze the conversion of one isomer to another

A

Isomerase

26
Q

catalyzes the racemization of enantiomers

A

Racemase

27
Q

catalyzes the change of one epimer to another

A

Epimerase

28
Q

enzymes catalyze reactions leading to the joining of two molecules in which a covalent bond forms between the molecules

A

Ligases

29
Q

catalyzes the formation of a C-C bond

A

Pyruvate carboxylase

30
Q

Catalyzes the formation of a C-S bond

A

Acetyl-CoA synthetase

31
Q

is an experiment to determine an enzyme’s catalytic activity

A

Enzyme assays

32
Q

In this, you simply measure the amount of reaction in a fixed amount of time

A

Fixed-time assay

33
Q

In this, you monitor the progress of a reaction continuously

A

Kinetic assay

34
Q

is where all the enzyme molecules are part of an enzyme-substrate complex

A

Saturation point

35
Q

Michaelis-Menten equation

A

V= Vmax [S] / [S] + KM

36
Q

the chemists that were able to propose a model that explains the kinetics of many different enzymes

A

Leonor Michaelis and Maud Menten

37
Q

also known as a double-reciprocal plot

A

Lineweaver-Burk plot

38
Q

The basis of Lineweaver-Burk plot comes from the manipulation of the Michaelis-Menten equation to the form

A

l/v = Km/Vmax x l/[S] + l/Vmax

39
Q

It is the most widely used graphical technique for the determination of KM and Vmax

A

Lineweaver-Burk plot

40
Q

are substances that decrease an enzyme’s activity

A

Inhibitors

41
Q

Type of inhibitors that enters the active site of an enzyme and, thus, prevents the substrate from entering

A

Competitive inhibitors

42
Q

Type of inhibitors that don’t enter the active site but instead bind to some other region of the enzyme

A

Noncompetitive inhibitors

43
Q

Some enzymes have multiple forms known as

A

Isozymes or isoenzymes

44
Q

Used as a digestive aid for precooked food

A

Amylase

45
Q

Converts starch to dextrose

A

Amyloglucosidase

46
Q

Prevents the crystallization of lactose in ice cream

A

Lactase

47
Q

Used in the production of fructose from cornstarch

A

Glucose isomerase

48
Q

Used in the conversion of sawdust to sugar and the production of liquid coffee concentrates

A

Cellulase and hemicellulase

49
Q

Removes glucose from egg solids

A

Glucose oxidase

50
Q

Stabilizes sugars in soft-centered candy

A

Invertase

51
Q

Clarifies wine and fruit juice

A

Pectinase

52
Q

Removes H2O2 used in the “cold pasteurization” of milk

A

Catalase

53
Q

Added to detergents for removal of protein stains

A

Alcalase

54
Q

Tenderizes meat

A

Bromelain

55
Q

Produces flavor in cheese

A

Lipase

56
Q

Whitens bread

A

Lipoxygenase

57
Q

Tenderizes meat and stabilizes beer

A

Papain

58
Q

Used as a digestive aid for precooked food under proteases

A

Pepsin

59
Q

Used in cheese making

A

Rennin

60
Q

In this form of regulation, an inactive form of an enzyme — a proenzyme or a zymogen — undergoes irreversible conver- sion to the active form, often through the hydrolysis of one or more peptide bonds.

A

Proteolytic activation

Biochemistry (6 decks)

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