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Biochemical Principles > Lecture 8: Enzymes > Flashcards

Lecture 8: Enzymes Flashcards

1
Q

An ____________ is a protein + cofactor complex designed to catalyze biological reactions

A

enzyme

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2
Q

____________, _____________ & __________________ within the molecule are 3 basic ways that enzymes work on biological molecules.

A

Catabolism, Anabolism and rearranging atoms/molecules

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3
Q

Enzymes catalyze biological reactions in two ways: by _____________ and __________ _______

A

specificity and reaction rate

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4
Q

_____________ work to lower the ACTIVATION ENERGY of chemical reactions.

A

Catalysts

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5
Q

Without enzymes, most reaction rates would be at or near ______.

A

zero

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6
Q

Enzymatic reaction rate is between _______ to _______ times as fast if molecules were left alone to react.

A

100,000 to 1,000,000,000

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7
Q

Enzymes have a discriminatory ability to work on or select the exact molecule or atoms they’re designed for called ___________

A

specificity

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8
Q

_____________ is the generic name for a molecule that will be worked on by an enzyme; eg starch is the ___________ of amylase enzymes.

A

Substrate; substrate

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9
Q

Many drugs and herbs “_________” the specificity of enzymes. This is often caused by ______________ _____________ of the active site.

A

fool; competitive inhibition

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10
Q

There are both __________ & __________ consequences in artificially interfering with the active site & specificity of an enzyme.

A

positive and negative

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11
Q

Enzymes are made of protein but also incorporate cofactors like ____________, ___________, _____________ & mineral ions to facilitate their functioning

A

coenzymes, vitamins, porphyrins & mineral ions

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12
Q

The ____________ structure of an enzyme includes at least one _______ ______ where molecules fit & are transformed thru biochem reactions.

A

tertiary structure; one active site

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13
Q

_______ is a coenzyme and is utilized by many enzymes to facilitate the breaking and fusing of bonds in affected substrates.

A

ATP

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14
Q

Enzymes are also found as huge _____________ structures, with concatenated tertiary subunit proteins.

A

quaternary

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15
Q

Other enzymes, because they rearrange molecules in orientation, will _________ a change without using _____

A

catalyze; ATP

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16
Q

Enzyme activity is affected by many _________ _________

A

external factors

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17
Q

Name a few external factors that affect enzyme activity…

A
  1. Presence or absence of substrates, 2. pH changes or other iconic factors, 3. temp range, 4. availability of nutrients - ATP, cofactors, coenzymes & ions, 5. functionality of enzyme & 6. molecules form drugs, herbs, toxins or organisms
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18
Q

Synthase is known as a _____________

A

transferase

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19
Q

Amylase molecules from human saliva need ________ & ________ ions to be most effective

A

calcium & chloride ions

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20
Q

Enzymes are typically classified by the _________ ___________ of the reactions they catalyze

A

chemical reactions

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21
Q

__________________ remove molecules or atoms from substrates

A

Oxidoreductases

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22
Q

___________ - transfer functional groups from one molecule to another, such as moving a phosphate group

A

Transferases

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23
Q

______________ add water to substrates

A

Hydrolases

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24
Q

_________ work with double bonds

A

Lyases

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25
Q

_____________ change the isomeric status of a molecule

A

Isomerases

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26
Q

___________ join or release carbon bonds and requires ATP

A

Ligases

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27
Q

Enzymes are also named for the _____________ upon which they work

A

substrate

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28
Q

Examples of enzymes named after substrates they work on are __________ (work on urea molecule) & _______________ (remove water from molecule)

A

Urease & Dehydrogenase

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29
Q

Two digestive enzymes that retained their old names are __________ & ___________. They are both proteases.

A

Trypsin & Pepsin

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30
Q

A __________ ____________ goes from substrate enzyme entering active site to substrate complex to product complex to product leaving active site of enzyme

A

Catabolic pathway

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31
Q

An ________ __________ goes from entering enzyme product active site to product complex to substrate complex product being absorbed into active site of enzyme substrate

A

Anabolic pathway

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32
Q

A common way that drugs or other molecules stop enzyme function is via _________ __________

A

competitive inhibition

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33
Q

The term _________ _________ is commonly used to signify that a number of enzymes work on substrates in a specific order

A

enzyme cascade

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34
Q

____________ is known as an enzyme cascade

A

Glycolysis

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35
Q

Many enzymes are dependent for proper function on several non-protein molecules called _________

A

cofactors

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36
Q

When an enzyme doesn’t have its cofactors present, it is called an __________ and is not functional.

A

apoenzyme

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37
Q

An enzyme with cofactors and fully functioning is a _____________.

A

holoenzyme

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38
Q

Biochemists classify 2 types of cofactors - __________ ________ & ______________

A

Prosthetic groups & Coenzymes

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39
Q

Common prosthetic groups are ___________, ____________ groups & ___________ ______. These groups are often the limiting factor in nutrition & energy generation.

A

vitamins, porphyrin groups & metallic ions

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40
Q

Deficiency in vitamins and minerals slow metabolism and revert back to ___________ status

A

apoenzyme

41
Q

Ion in prosthetic groups provided for enzymes come from _________

A

metals

42
Q

_____________ is an ion prosthetic used by plants to produce sugars

A

Magnesium

43
Q

____________ is an ion prosthetic that helps with the antioxidant system of your body.

A

Selenium

44
Q

Whenever there is a Porphyrin with Iron, it’s called a _______

A

heme

45
Q

Vitamins have to come in via ______ _________

A

your diet

46
Q

Pyruvate dehydrogenase is a ___-________ ________ used to eventually make acetyl coenzyme A from pyruvic acid necessary for Krebbs Cycle.

A

six-domain enzyme

47
Q

______________ are called cosubstrates because they act to donate a part of themselves like a substrate to a reaction happening in an active site.

A

Coenzymes

48
Q

NAD/NADH and Acetyl coenzyme A are ____________ used repeatedly in production of _____ in mitochondrion

A

coenzymes; ATP

49
Q

NAD has one component - _________

A

Niacin/Vitamin B3

50
Q

Acetyl Coenzyme A has one component - _________ ______

A

Pantothenic acid/Vitamin B5

51
Q

_____ vitamins play a vital role in energy production and can be a limiting factor in nutrition

A

B vitamins

52
Q

ATP, Lipoamine, FAD/FADH, Ubiquinone (Coenzyme Q10) & S-adenyl methionine (Sam-e) are all important ___________

A

coenzymes

53
Q

ATP splits off a high energy bonded __________ ________ in the active sites of enzymes to propel reaction

A

phosphate group

54
Q

What regulates enzyme production?

A

Gene expression

55
Q

Genes coding for enzymes are either ________ or _________ by gene expression factors.

A

Induced or inhibited

56
Q

If the product produced by the enzyme reaches a plateau concentration, this turns off the enzyme.

A

Negative feedback loop or allosteric inhibition

57
Q

Some enzymes are regulated by _________ or __________ molecules that tell the enzyme to operate or not.

A

inhibitor or activator

58
Q

Enzymes can be modified by ________ or _______ of functional groups to make the enzyme active or not.

A

Addition or subtraction

59
Q

__________ of enzymes will turn on the breakdown of glycogen.

A

Phosphorylation

60
Q

(T/F) Placing an enzyme in a changed environment, as in pH change, can activate or deactivate the enzyme.

A

True - this is one of the regulations of enzyme activity by the cell.

61
Q

A pre-active enzyme.

A

Zymogen or proenzyme

62
Q

What are 3 coenzymes?

A

1) NAD/NADH+
2) Acetyl Coenzyme A
3) ATP - Adenosine Triphosphate

63
Q

Enzyme which reduces glutathione disulfide (GSSG) to the sulfhydryl form?

A

Glutathione reductase

64
Q

The most important cellular antioxidant.

A

Reduced glutathione (GSH)

65
Q

What antioxidant keeps one from getting chronic illness?

A

Reduced glutathione (GSH)

66
Q

What molecule is required to reduce GSSG to GSH? And how many of this molecule is required?

A

NADPH; 2

67
Q

What is the reduced, phosphorylated version of NAD+?

A

NADPH

68
Q

For every _________ and 2 ________ you gain 2 reduced GSH molecules that can again act as antioxidants scavenging reactive oxygen species (ROS) in the cell.

A

GSSG and NADPH

69
Q

The process of GSR reducing GSSG forming GSH is especially important in _____ _______ ______.

A

Red blood cells

70
Q

Oxygen with an extra electron: O2 -1

A

Superoxide

71
Q

(T/F) Reactive forms of oxygen that leak from mitochondrial respiration enzymes and wreak havoc on a cell.

A

True

72
Q

What enzyme detoxifies superoxide?

A

Superoxide dismutase (SOD)

73
Q

What special type of reaction, where 2 equal but opposite reactions occur on 2 separate molecules?

A

Dismutation

74
Q

SOD takes two molecules of ________, strips the extra electron off of one, and places it on the other.

A

superoxide

75
Q

The product of SOD creates a normal oxygen molecule and _________ __________, a toxic compound.

A

hydrogen peroxide

76
Q

What enzyme is used to detoxify the cell from hydrogen peroxide?

A

catalase

77
Q

What enzyme is the fastest enzyme and can convert hydrogen peroxide to water and O2 by the millions per second.

A

catalase

78
Q

SOD has recently gained notoriety for its connection with ________ _________ ________.

A

Amyotrophic Lateral Sclerosis (ALS)

79
Q

What is the common name for ALS?

A

Lou Gehrig’s disease

80
Q

What disease which is a degenerative disorder that leads to selective death of motor neurons in the brain and spinal chord, leading to gradually increasing paralysis over a few years?

A

Lou Gehrig’s disease

81
Q

What enzyme where a protein contains an iron porphyrin ring?

A

hemoprotein enzymes

82
Q

What enzyme is a common, large and diverse group of hemoprotein enzymes found in many types of life forms?

A

cytochrome P450 group

83
Q

Cytochrome P450 is found in mostly what life forms?

A

Eukaryotes

84
Q

Cytochrome P450 have 2 common functions:

A

1) oxygenate substrates

2) pass electrons in aerobic respiration

85
Q

Cytochrome P450 are unusual enzymes, b/c they can catalyze a plethora of substrates and so are _______.

A

nonspecific

86
Q

Where are cytochrome P450 found?

A

1) mitochondria - part of electron transport chain of oxidative phosphorylation
2) luman of ER in cells - detox functions

87
Q

What enzyme is one of 57 human cytochromes and is part of the electron transport chain in oxidative phosphorylation?

A

cytochrome c

88
Q

_________ are membrane-associated proteins, located either in the inner membrane (cristae) of mitochondria or in the ER of cells.

A

cytochromes

89
Q

(T/F) Cytochromes metabolize only a few of endogenous and exogenous compounds.

A

False - it metabolizes thousands

90
Q

Cytochrome P450 enzymes are present in all tissues of the body, and play important roles in 3 ways?

A

1) hormone synthesis and breakdown
2) cholesterol synthesis
3) vitamin D metabolism

91
Q

What organ does the cytochrome P450 perform as a detox function?

A

liver

92
Q

What is the most important cytochrome in cellular detoxification?

A

cytochrome P450 3A4

93
Q

Where does the cytochrome P450 3A4 reside?

A

ER of cells

94
Q

What organ detoxifies or metabolizes drugs and toxic compounds, all foods, as well as metabolic products?

A

liver

95
Q

What is a breakdown product of hemoglobin?

A

bilirubin

96
Q

Many drug side effects have to do with the overuse or inhibition of the cytochrome deoxification potential in liver __________.

A

hepatocytes

97
Q

What is the term used for reduced dosage of medications from too rapid metabolism?

A

induction

98
Q

What is the term used for slow breakdown of drugs, possibly causing an overdose?

A

inhibition

Biochemical Principles (11 decks)

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