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BIO 024: Biochemistry > Enzymes PPT based > Flashcards

Enzymes PPT based Flashcards

1
Q

is a compound or biological polymer, usually a protein, that acts as a catalyst for a biochemical reaction.

A

ENZYMES

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2
Q

Biological catalyst for chemical reaction in biological system

A

Enzymes

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3
Q

is an enzyme composed only of protein (amino acids) not bound to any nonproteins

A

simple enzyme

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4
Q

is an enzyme that has a nonprotein part in addition to a protein part

A

conjugated enzyme

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5
Q

is the protein part of a conjugated enzyme or holoenzyme

A

apoenzyme

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6
Q

enzyme lacking an essential cofactor

A

apoenzyme

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7
Q

serve functions similar to those of prosthetic groups but bind in a transient, dissociable manner either to the enzyme or to a substrate such as ATP

A

cofactor

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8
Q

Tightly bound cofactor to the apoenzyme

A

prosthetic group

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9
Q

is the biochemically active conjugated enzyme produced from an apoenzyme and a cofactor

A

holoenzyme

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10
Q

Intact and functional enzyme containing all cofactors/ coenzyme

A

holoenzyme

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11
Q

is a small organic molecule that serves as a cofactor in a conjugated enzyme

A

Coenzyme or cosubstrate

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12
Q

the inorganic cofactor

A

Coenzyme or cosubstrate

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13
Q

is the reactant in an enzyme-catalyzed reaction

A

Substrate (S)

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14
Q

biomolecule that enzymes react with

A

Substrate (S)

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15
Q

the biomolecules formed by enzyme mediated reactions

A

Product (P)

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16
Q

Enzymes that require a metal ion cofactor

A

metal-activated enzymes

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17
Q

enzymes that contain tightly bound metal ions

A

metalloenzymes

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18
Q

are distinguished by their tight, stable incorporation into a protein’s structure by covalent or noncovalent forces.

A

Prosthetic groups

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19
Q

______ are the most common prosthetic groups

A

Metals

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20
Q

The roughly one-third of all enzymes that contain tightly bound metal ions are termed ______

A

metalloenzymes

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21
Q

serve functions similar to those of prosthetic groups but bind in a transient, dissociable manner either to the enzyme or to a substrate such as ATP.

A

Cofactors

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22
Q

Unlike the stably associated prosthetic groups, _____ therefore must be present in the medium surrounding the enzyme for catalysis to occur.

A

cofactors

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23
Q

Metalloenzyme:

Destroy superoxide anion

A

Superoxide dismutase

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24
Q

Metalloenzyme:

They oxidize a range of aliphatic and aromatic alcohols to their corresponding aldehydes and ketones using NAD+ as a coenzyme

A

Alcohol dehydrogenase

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25
Q

Metalloenzyme:

Synthesize DNA

A

DNA polymerase

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26
Q

Metalloenzyme:

is a protease enzyme that hydrolyzes (cleaves) a peptide bond at the carboxy terminal (C-terminal) end of a protein or peptide

A

Carboxypeptidase A

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27
Q

Metalloenzyme:

Synthesize oxaloacetate

A

Pyruvate carboxylase

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28
Q

Metalloenzyme:

Synthesize Urea

A

Arginase

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29
Q

Metalloenzyme:

transports oxygen from the lungs to the capillaries of the tissue

A

Hemoglobins

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30
Q

Metalloenzyme:

carry electrons between two segments of the electron-transport chain.

A

Cytochromes

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31
Q

Metalloenzyme:

hydrolyzes peptide bonds of C-terminal residues with aromatic or aliphatic side-chains

A

Cytochrome Oxidase

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32
Q

the suffix “______” is added to the name of the substrate

A

“ase”

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33
Q

CLASSIFICATION OF ENZYME:

acts on starch

A

amylase

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34
Q

CLASSIFICATION OF ENZYME:

acts on maltose

A

maltase

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35
Q

CLASSIFICATION OF ENZYME:

act on urea

A

cellulase

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36
Q

CLASSIFICATION OF ENZYME:

acts on fats

A

lipase

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37
Q

CLASSIFICATION OF ENZYME (except for):

in gastric juice (stomach

A

Pepsin

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38
Q

CLASSIFICATION OF ENZYME (except for):

in pancreatic juice (small intestine)

A

Trypsin

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39
Q

CLASSIFICATION OF ENZYME (except for):

in saliva

A

Ptyalin

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40
Q

CLASSIFICATION OF ENZYME (except for):

the milk curding enzyme

A

Rennin

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41
Q

NOMENCLATURE and CLASSIFICATION OF ENZYME:

oxidation reaction

42
Q

NOMENCLATURE and CLASSIFICATION OF ENZYME:

decarboxylation

A

decarboxylase

43
Q

NOMENCLATURE and CLASSIFICATION OF ENZYME:

transamination

A

transaminase

44
Q

NOMENCLATURE and CLASSIFICATION OF ENZYME:

hydrolysis

45
Q

NOMENCLATURE and CLASSIFICATION OF ENZYME:

reversible addition or removal of water

A

hydrase or dehydrase

46
Q

is an enzyme that catalyzes an oxidation–reduction reaction.

A

OXIDOREDUCTASE

47
Q

an oxidation that increases the number of C-O bonds and/or decreases the number of C-H bonds

A

ORGANIC OXIDATION rxn

48
Q

a reduction that decreases the number of C-O bonds and/or increases the number of C-H bonds

A

ORGANIC REDUCTION rxn

49
Q

“browning reaction” caused by _______ (or polyphenoloxidase), a conjugated enzyme in which copper is present:

50
Q

is an enzyme that catalyzes the transfer of a functional group other than hydrogen (ex. methyl, acyl, amino or phosphate groups) from one molecule to another

A

TRANSFERASES

51
Q

Example of Oxidoreductase

A

Lactate dehydrogenase

52
Q

Example of Transferases

A

transaminases and kinases

53
Q

is an enzyme that catalyzes a hydrolysis reaction in which the addition of a water molecule to a bond causes the bond to break

54
Q

Hydrolysis reactions are central to the process of _______

55
Q

Example of Hyrdolase:

breaking of glycosidic bonds in oligo- and polysaccharides

A

Carbohydrases

56
Q

Example of Hyrdolase:

breaking of peptide linkages in proteins

57
Q

Example of Hyrdolase:

breaking of ester linkages in triacylglycerols.

58
Q

is 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.

59
Q

Example of Lyase:

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

A

Dehydratase

60
Q

Example of Lyase:

effects the addition of the components of water to a double bond

61
Q

an enzyme that catalyzes the isomerization (rearrangement of atoms or interconversion of optical, geometric, or positional isomers of a substrate in a reaction, converting it into a molecule isomeric with itself. There is only one reactant and one product in reactions where isomerases are operative

62
Q

an enzyme that catalyzes the bonding together of two molecules into one with the participation of ATP

A

LIGASE or SYNTHETASE

63
Q

Main Classes and Subclasses of Enzymes:

oxidation of a substrate

A

OXIDOREDUCTASES, oxidases

64
Q

Main Classes and Subclasses of Enzymes:

reduction of a substrate

A

OXIDOREDUCTASES, reductases

65
Q

Main Classes and Subclasses of Enzymes:

introduction of double bond (oxidation) by formal removal of two H atoms from substrate, the H being accepted by a coenzyme

A

OXIDOREDUCTASES, dehydrogenases

66
Q

Main Classes and Subclasses of Enzymes:

transfer of an amino group between substrates

A

TRANSFERASES, Transaminases

67
Q

Main Classes and Subclasses of Enzymes:

transfer of a phosphate group between substrates

A

TRANSFERASES, Kinases

68
Q

Main Classes and Subclasses of Enzymes:

hydrolysis of ester linkages in lipids

A

HYDROLASES, Lipases

69
Q

Main Classes and Subclasses of Enzymes:

hydrolysis of amide linkages in proteins

A

HYDROLASES, Proteases

70
Q

Main Classes and Subclasses of Enzymes:

hydrolysis of sugar–phosphate ester bonds in nucleic acid

A

HYDROLASES, Nucleases

71
Q

Main Classes and Subclasses of Enzymes:

hydrolysis of glycosidic bonds in carbohydrates

A

HYDROLASES, Carbohydrases

72
Q

Main Classes and Subclasses of Enzymes:

hydrolysis of phosphate–ester bonds

A

HYDROLASES, phosphatases

73
Q

Main Classes and Subclasses of Enzymes:

removal of H2O from a substrate

A

LYASES, dehydratases

74
Q

Main Classes and Subclasses of Enzymes:

removal of CO2 from a substrate

A

LYASES, decarboxylases

75
Q

Main Classes and Subclasses of Enzymes:

removal of NH3 from a substrate

A

LYASES, deaminases

76
Q

Main Classes and Subclasses of Enzymes:

addition of H2O to a substrate

A

LYASES, hydratases

77
Q

Main Classes and Subclasses of Enzymes:

conversion of D isomer to L isomer,or vice versa

A

ISOMERASES, Racemases

78
Q

Main Classes and Subclasses of Enzymes:

transfer of a functional group from one position to another in the same molecule

A

ISOMERASES, Mutases

79
Q

Main Classes and Subclasses of Enzymes:

formation of new bond between two substrates, with participation of ATP

A

LIGASES, Synthetases

80
Q

Main Classes and Subclasses of Enzymes:

formation of new bond between a substrate and CO2, with participation of ATP

A

LIGASES, Carboxylases

81
Q

the relatively small part of an enzyme’s structure that is involved in catalysis. Usually a “crevicelike” location the enzyme.

A

Enzyme Active Site

82
Q

the intermediate reaction species that is formed when the substrate bind to the active site of an enzyme.

A

Enzyme-Substrate Complex

83
Q

only a substrate whose shape and chemical nature are complementary to those of the active site can interact with the enzyme.

A

Lock-and-Key Model

84
Q
  • is a result of the enzyme’s flexibility
  • the enzyme active site, although not exactly complementary in shape to that of the substrate, is flexible enough that it can adapt to the shape of the substrate.
A

Induced-Fit Model

85
Q

the extent to which an enzyme’s activity is restricted to a specific substrate, a specific group of substrates, a specific type of chemical bond, or a specific type of chemical reaction

A

Enzyme specificity

86
Q

FACTORS THAT AFFECT THE RATE OF ENZYME ACTIVITY:

Reaction rate increases with _____ until the point at which the protein is denatured and activity drops sharply.

A

Temperature

87
Q

FACTORS THAT AFFECT THE RATE OF ENZYME ACTIVITY:

Maximum enzymatic activity is possible only within a narrow ____ range; outside this ___ range, the protein is denatured and activity drops sharply.

88
Q

FACTORS THAT AFFECT THE RATE OF ENZYME ACTIVITY:

Reaction rate increases with _______ until full saturation occurs; then the rate levels off.

A

Concentration of Substrate/Substrate Concentration

89
Q

FACTORS THAT AFFECT THE RATE OF ENZYME ACTIVITY:

Reaction rate increases with increasing ______, assuming enzyme concentration is much lower than that of substrate.

A

Concentration of Enzyme/Enzyme Concentration

90
Q

is a microorganism that thrives in extreme environments, environments in which humans and most other forms of life could not survive.

A

Extremophile

91
Q

is a microbial enzyme active at conditions that would inactivate human enzymes as well as enzymes present in other types of higher organisms.

A

EXTREMOZYME

92
Q

Uses of this include:

  • detergent formulations
  • the petroleum industry during oil well drilling operations
A

EXTREMOZYME

93
Q

Extremophile:

optimal growth at pH levels of 3.0 or below

A

acidophiles

94
Q

Extremophile:

optimal growth at pH levels of 9.0 or above

A

alkaliphiles

95
Q

Extremophile:

a salinity that exceeds 0.2 M NaCl needed for growth

A

halophiles

96
Q

Extremophile:

a temperature between 80°C and 122°C needed to thrive

A

Hypothermophiles

97
Q

Extremophile:

a temperature of 15°C or lower needed for growth

A

cryophiles

98
Q

Extremophile:

a high hydrostatic pressure needed for growth

A

piezophiles

99
Q

commonly called H. pylori, is a bacterium that can function in them highly acidic environment of the stomach
* causes more than 90% of duodenal ulcers and up to 80% of gastric ulcers.

A

Helicobacter pylori

100
Q

a molecule closely resembling the substrate. Binds to the active site and temporarily prevents substrates form occupying

A

Competitive Enzyme Inhibitor

101
Q

a molecule that binds to a site on an enzyme that is not the active site. The normal substrate still occupies the active site

A

Noncompetitive Enzyme Inhibitor

102
Q

a molecule that forms a covalent bond to a part of the active site, permanently preventing substrate from occupying.

A

Irreversible Enzyme Inhibitor

BIO 024: Biochemistry (16 decks)

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