Metabolism and enzymes Flashcards

1
Q

Catabolism is the

A

Breaking down nutrients into smaller molecules to produce energy
Energy is stored in bonds of ATP molecule and transported where it is needed

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2
Q

Anabolism is the

A

Stored energy is used to assemble new molecules from small components produced from catabolism

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3
Q

Energy for metabolic reaction is

A

Energy is supplied to cells by breakdown of nutrients
Storage forms of energy: ATP, NADH, FADH2
Energy is released when molecular bonds are broken

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4
Q

Stage one of catabolism occurs in

A

the gastrointestinal tract
Digestion in the lumen of the GI tract

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5
Q

Stage 2 of catabolism occurs in

A

Anaerobic respiration in the cell’s cytosol

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6
Q

Stage 3 of catabolism occurs in

A

Aerobic respiration in cell mitochondria

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7
Q

Catabolism stage 1 is the

A

Occurs in GI tract
Food is broken down in stomach and digested stomach contents pass to small intestine
Further broken down by enzymes
Hydrolysis
Carbohydrates broken down to monosaccharides
Fats broken down to fatty acids and glycerol
Proteins broken down to amino acids
Nutrient molecules are absorbed by cells that line small intestine
Nutrients pass to blood or lymph
Carried to organs and tissues
Many go to liver for further metabolism

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8
Q

Catabolic metabolism stage 2

A

Occurs in the cytosol
Process of anaerobic respiration catabolizes nutrients
Acetyl CoA is transported through cytoplasm to the mitochondria

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9
Q

Catabolic metabolism stage 3

A

Occurs in the mitochondria
Aerobic respiration involves the attachment of an inorganic PO4 to a molecule of ADP to form ATP
ATP used by the cell to carry energy
Catabolic pathways of proteins, carbohydrates and fats transfer energy stored in nutrients into ATP

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10
Q

Anabolic metabolism

A

A biosynthetic process

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11
Q

Dehydration synthesis

A

Important part of anabolism
Effect is opposite of hydrolysis
Monosaccharides are assembled to form chains of polysaccharide
1 monosaccharide + 1 monosaccharide = 1 disaccharide + water
Fat molecules are formed from the connection of glycerol and fatty acids
Proteins are created from chains of amino acids

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12
Q

Control of metabolic reactions

A

Metabolism is a multi-enzyme sequence of events
Reactions are highly specific
Cell relies on enzymes to initiate and control metabolism
Each enzyme reacts with one particular molecule (substrate) to produce a new molecule (product)
Product of one step is substrate of the next

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13
Q

Enzyme activity

A

Depends on molecular shape of the enzyme
Active site = region of enzyme that binds to the substrate
Enzymes not altered by the reactions
Enzyme names end in -ase
Enzymes often named for substrate it acts upon
Transferases are enzymes that move of part of a molecule to another molecule

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14
Q

Catalytic efficiency

A

Enzyme acts as catalyst
Speeds up reactions by lowering the activation energy
Increased rate of reaction is essential to life
Example: Carbon dioxide, a waste product of respiration, must be moved out of the body
To accomplish this carbonic anhydrase combines carbon dioxide with water to form carbonic acid (H2CO3) and bicarbonate ions (HCO3-)

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15
Q

Control of metabolic reactions

A

May need assistance of a nonprotein cofactor in order to complete a reaction
Completes the shape of a binding site
Examples: iron, zinc, copper, copper, potassium, calcium ions

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16
Q

Examples of coenzymes

A

nicotinamide adenine dinucleotide (NAD), acetyl-coenzyme A, flavin adenine dinucleotide (FAD)

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17
Q

Factors effecting enzyme activity

A

Enzyme concentration
Effect on rate is directly proportional
Substrate concentration
Rate increases until enzyme is saturated
Temperature
Rate increases until denaturation of enzyme
pH
Many enzymes have maximum activity at pH near 7
Most enzymes are denatured at pH extremes
Pepsin is an exception – optimum pH is 1.5

18
Q

Enzyme inhibition

A

Enzyme inhibitor – any substance that can decrease the rate of an enzyme-catalyzed reaction
Many poisons and some medicines inhibit enzymes
Some inhibitors provide internal regulation of cellular metabolism

19
Q

Two categories of enzyme inhibition

A

Irreversible and reversible

20
Q

Irreversible inhibition

A

Irreversible inhibitor - forms a covalent bond with a functional group of the enzyme
Renders enzyme inactive
Many poisons are irreversible inhibitors

21
Q

Cyanide ion are what type of inhibition

A

Irreversible inhibition
Interferes with cytochrome oxidase
Blocks mitochondrial electron transport chain
Stops aerobic cellular respiration
Death occurs in minutes
Antidote – sodium thiosulfate
converts cyanide ion to thiocyanate that does not bind cytochrome oxidase

22
Q

Heavy metals are what type of inhibition

A

Irreversible inhibition
Combine with sulfhydryl groups on enzymes
Can cause neurological damage
Treated with chelating agents
Substance combines with metal and holds it very tightly

23
Q

Antibiotics are

A

Irreversible inhibition
Penicillin
Inhibit enzymes essential to life processes of bacteria
Penicillin interferes with transpeptidase which is needed for bacterial cell wall construction

24
Q

Reversible inhibition is and have 2 types

A

Reversible inhibitor reversibly binds to an enzyme so can be removed
Two types:
Competitive
Non competitive

25
Q

Competitive inhibition

A

Competes with substrate for binding at the active site of enzyme
Have molecular structure similar to normal substrate of enzyme
Example: sulfa drugs
Folic acid needed by bacteria is synthesized from p-aminobenzoic acid, which resembles sulfanilamide
Sulfanilamide competes for active site
Synthesis of folic acid slowed or stopped
Bacteria prevented from multiplying
Reversed by increasing concentration of normal substrate
Competition is won by whichever molecular species is in greater concentration

26
Q

Non competitive inhibitor is

A

Binds to enzyme at a location other than the active site
Bears no resemblance to normal enzyme substrate
Interaction causes 3-D shape of enzyme and active site to change
Enzyme no longer binds normal substrate or it binds improperly so reaction is not catalyzed
More substrate does not reverse inhibition

27
Q

Regulation of enzyme activity

A

Enzymes must be controlled - an organism must respond to changing conditions and cellular needs
Three control mechanisms:
Activation of zymogens
Allosteric regulation
Genetic control

28
Q

Activation of zymogens

A

Enzymes may be synthesized as inactive precursors called zymogens or proenzymes
Stored in inactive state
When needed zymogen is released and activated at location of reaction
Activation usually involves cleavage of peptide bonds of zymogen

29
Q

Allosteric regulation

A

Combination of enzyme with compound that change 3-D shape
Compound called a modulator
Allosteric enzymes are often located at key control points in cellular processes

30
Q

Allosteric regulation modulators

A

Activators – increase activity
Inhibitors – decrease activity

31
Q

Examples of allosteric regulation

A

Synthesis of isoleucine
Five steps
Product isoleucine binds to enzyme at first step and inhibits enzyme activity
No excess isoleucine is produced
When isoleucine level lowers, the enzyme will be more active and more isoleucine is synthesized
Feedback inhibition – a process in which the end product of a pathway inhibits an earlier step in the process

32
Q

Genetic control

A

Enzyme induction – synthesis of an enzyme in response to cellular need
Allows an organism to adapt to environmental changes
Example: regulation of gluconeogenesis
Activity of PEP carboxykinase is increased during fasting, starvation and diabetes mellitus due to enzyme induction by glucagon

33
Q

enzymes in clinical diagnosis

A

Certain enzymes are normally found only inside cells
Get released into blood and fluid when cells are damaged
Changes in blood serum levels of specific enzymes can be used to clinically detect cell damage or uncontrolled growth
Measurements of enzyme concentrations is a major diagnostic tool

34
Q

Alkaline phosphate indicates what in a clinical diagnosis

A

– liver or bone disease

35
Q

Isozymes are

A

A slightly different form of the same enzyme produced by different tissues
Have similar catalytic properties but different physical properties
Assays for isozymes can pinpoint location and type of disease more accurately

36
Q

Co enzymes

A

Nonprotein organic molecules that may also act as cofactors
Often vitamins, or derived from vitamins
May be bound temporarily or permanently to the enzyme

37
Q

Amylase indicates what in a clinical diagnosis

A

Pancreatic disease

38
Q

Lipase indicates what in a clinical diagnosis

A

acute pancreatitis

39
Q

Alanine transaminase indicates what in clinical diagnosis

A

hepatitis

40
Q

Aspartate transaminase indicates what in a clinical diagnosis

A

hepatitis or heart attack

41
Q

Growing cells need additional protein through anabolic metabolism because

A

Growing cells need additional proteins:
For the expanded cell membranes
To perform many other vital functions
Replacement molecules must be manufactured continuously
Metabolic turnover