Lesson 1 - Enzymology

Front 1

Biocatalysts

Back 1

Primarily or entirely protein in nature

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Catalysts

Back 2

Alter the rate of a chemical reaction without themselves being consumed in the reaction

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Enzymes

Back 3

Very specific and targets specific reactions species

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True

Back 4

Enzymes affects ONLY the rate of reaction and affects the rate on both directions. True or False

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Substrate

Back 5

Precursor of a product in an enzyme reaction; binds to the active site of the enzyme

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Enzyme

Back 6

Mostly consists of proteins

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Holoenzyme

Back 7

Whole enzyme molecule

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Apoenzyme

Back 8

Protein portion of the enzyme

Front 9

Metalloenzyme

Back 9

Apoenzyme + metal ion factor

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Cofactors

Back 10

Non-protein factors

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Coenzymes and Activarors

Back 11

What are the two types of Cofactors?

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Coenzymes

Back 12

Organic factors; Acts as transient carriers of specific functional groups

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Activators

Back 13

Inorganic factors; Can be metallic ion or non-metallic

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Calcium

Magnesium

Zinc

Iron

Manganese

Copper

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Examples of Metallic activators

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Chloride

Back 15

Example/s of non-metallic activator

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NAD/NADH or NADP/NADPH

Cysteine

Pyridoxal

Back 16

Examples of Coenzymes

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Calcium

Back 17

Used for amylase reactions

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Magnesium

Back 18

Used for creatine kinase reactions

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Macroenzymes

Back 19

High-molecular mass forms of the serum enzymes

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Macroenzyme type 1

Back 20

Enzyme bound to an immunoglobulin

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Macroglobulin type 2

Back 21

Enzyme bound to non-immunoglobulin substance

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Emil Fisher’s / Lock and Key Theory

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Based on the premise that the shape of the key (s) must fit into the lock (E)

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Kochland’s / Induced Fit Theory

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Based on the substrate binding to the active site of the enzyme

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Enzyme Kinetics

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Enzymes catalyze physiologic reactions by lowering the activation energy level that the substrate must reach for the reaction to occur

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Enzyme kinetics

Back 25

Chemical reaction may occur spontaneously if the free energy or available kinetic energy is higher with a substrate than the product

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First order reaction

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Reaction rate is directly proportional to substrate concentration

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Zero order reaction

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Reaction rate depends only on enzyme contration

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Michelis-Menten Hypothesis

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The higher, the substrate concentration, the more substrate bound to an enzyme and the greater the rate of velocity of the reaction. When all enzyme is about to substrate, there will be no further increase in velocity- this is the maximum velocity. When the substrate present in adequate amount, the rate of reaction depends only in enzyme concentration

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Zinc

Back 29

Used for lactate dehydrogenase

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Absolute Specificity

Back 30

When an enzyme combines with only one substrate and catalyzes only one reaction

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Group Specificity

Back 31

When an enzyme combines with all the substrate in a chemical group (specifically the functional group)

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Bond Specificity

Back 32

When enzymes reacting with specific chemical bonds

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Stereospecificity

Back 33

The arrangement of the substrate atoms in 3D space binding with an enzyme

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pH

Temperature

Enzyme concentration

Substrate concentration

Inhibitors

Cofactors

Isoenzymes

Storage

Ionic strength or Electrolyte environment

Hemolysis

Lactescence

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What are the factors affecting enzymatic reactions?

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pH 7.0

Back 35

Most reactions occurs at pH_____

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ALP

Back 36

Alkaline: ________

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ACP and Pepsin

Back 37

Acidic : ________

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37-38°C

Back 38

Optimum temperature for most reactions to occur

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25°C, 30°C, and 37°C

Back 39

Temperature for enzyme activity

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Prosthetic group

Back 40

When a coenzyme or metal ion is tightly or even covalently bound to the enzyme protein

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Temperature Coefficient (Q10)

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Means that for every 10°C increase in temperature, there will be two-fold increase in enzyme activity

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Above 42-45°C

Back 42

Less activity because increased velocities denatures the protein

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60°C and above

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Causes denaturation of protein

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0°C and below

Back 44

Inactivity but irreversible

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-20°C to -70°C

Back 45

Recommended storage temp

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False. Directly Proportional

Back 46

Velocity of reaction is inversely proportional to enzyme concentration in the presence of excess substrate; reaction proceeds more rapidly when more enzyme molecules are present to bind substrate. True or False

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Substrate Concentration

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With the amount of enzyme exceeding the amount of substrate, the reaction rate steadily increases as more substrate is added. However, when the substrate concentration reaches a maximal value, higher concentration of substrate no longer results in increased rate of reaction (saturation kinetics)

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Inhibitors

Back 48

Substances that inhibit enzymatic reaction or that decreases the activity of an enzyme

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Mixed inhibition

Back 49

Has characteristics of both competitive and noncompetitive ihibition

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Competitive inhibition

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Compete with the substrate; Binds the active site of an enzyme

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Active site and Allosteric site

Back 51

What are the components of an enzyme

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Reversible

Back 52

Competitive inhibition is? (Reversible or Irreversible)

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Noncompetitive inhbitors

Back 53

Binds an enzyme at a place other than the active site (allosteric site) of enzyme and alter the configuration of the enzyme causing a decrease in enzyme activity

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Both Irreversible or Irreversible

Back 54

Is Noncompetitive inhibitors reversible or irreversible?

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Uncompetitive Inhibitors

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Inhibitor binds to an ES complex; the resulting enzyme-substrate-inhibitor complex does not yield product

Front 56

Cofactors

Back 56

Nonprotein entities that must bind to particular enzymes before a reaction occurs

Front 57

Isoenzymes

Back 57

The importance of the total enzyme activity is enhanced by fractioning ______________

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Low temperature

Back 58

It renders enzymes reversible inactive

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-20 °C

Back 59

Ideal temperature for preservation of enzymes

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2 to 8 °C

Back 60

Ideal storage temperature

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22°C or RT

Back 61

Temperature requirement for LDH

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Active site

Back 62

A water-free cavity where substrate interacts with particular charged amino acids

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Drops

Back 63

If ionic strength is too high, enzyme activity _______

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Hemolysis

Back 64

Increased enzyme concentration resulting to colored specimen

Front 65

Lactescence

Back 65

Increased enzyme concentration resulting to milky specimen

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Allosteric site

Back 66

A cavity other than the active site; may bind to regulator molecules

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Proenzyme

Back 67

Inactive forms of enzymes

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Pepsinogen

Back 68

Inactive form of enzyme pepsin, which promotes protein digestion

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Plasminogen

Back 69

Inactive form of enzyme plasmin which promotes fibrinolysis

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Isoenzyme

Back 70

Enzymes that catalyze the same reaction but differ in terms of physical of chemical characteristics, tissue distribution as well as electrophoretic mobility

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Oxidoreductase

Back 71

Catalyze: Redox Reactions

Examples: Cytochrome Oxidase, LDH, Malate Dehydrogenase, Isocitrate dehydrogenase, G-6-PD

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Fixed-Time (Static or Two-point) Assay

Back 72

Reactants combined and proceeds to reaction at designated time, then stopped, and measured

Front 73

Multiple Continuous Monitoring (Kinetic Assays)

Back 73

Preferred than the fixed-time where there are multiple measurements of change in absorbance made during the reaction

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Spectrophotometric

Manometry

Fluorometry

Coupled enzymatic reactions

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What are the methods for measuring enzymatic activity?

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Transferases

Back 75

Catalyze: The transfer groups of atoms

Examples: CK, AST, ALT, OCT

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Hydrolases

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Catalyze: Hydrolysis

Examples: Esterase, peptodase, aminopeptidases, glycosidases

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Lyases

Back 77

Catalyze: Addition to a double bond to the formation of a double bond

Examples: Glutamate decarboxylase, pyruvate decarboxylase, tryptophan decarboxylase, and aldolase

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Isomerases

Back 78

Catalyze: The isomerization of molecules

Examples: glucose phosphate isomerase and ribose phosphate isomerase

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Ligases or Synthetases

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Catalyze: Joining of two molecules

Examples: Synthase

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1st number: Major enzyme class

2nd and 3rd digits: subclass

Final and 4th digits: Serial number

Back 80

How do you name and classify enzymes?

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International Unit (IU)

Back 81

Micromole of substrate per minute

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Katal unit

Back 82

Mole of substrate per second

Front 83

Change in substrate concentration

Change in product concentration

Change in coenzyme concentration

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Enzyme activity that are measured are?