INTRODUCTION

Question 1

Proteins produced by living cells that hastens chemical reactions in organic matter

Answer 1

Enzymes

Question 2

They are measured in terms of their activity and not in terms of their absolute values

Answer 2

Enzymes

Question 3

They frequently appear in the serum after cellular injury, degradation of cells or from storage areas

Answer 3

Enzymes

Question 4

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

Answer 4

Cofactors

Question 5

An organic compound(second substrates) increasing its concentration will increase the velocity of an enzymatic reaction

Answer 5

Coenzymes

Question 6

It is essential to achieve absolute enzymatic activity

Answer 6

Coenzymes

Question 7

Are inorganic ions which alters the spatial configuration of the enzyme for proper substrate binding

Answer 7

Activators

Question 8

Are inorganic ions attached to a molecule

Answer 8

Metalloenzymes

Question 9

Interferes with the reaction

Answer 9

Inhibitors

Question 10

Physically binds to the active site of an enzyme

Answer 10

Competitive Inhibitor

Question 11

Has the ability to alter the apparent Michaelis-Menten constant (Km)

Answer 11

Competitive Inhibitor

Question 12

It looks for areas other than the active site

Answer 12

Non-Competitive Inhibitor

Question 13

This inhibitor binds to the enzyme-substrate (ES) complex

Answer 13

Uncompetitive Inhibitor

Question 14

These are enzymes having the same catalytic reactions but slightly different molecular structures

Answer 14

Isoenzymes

Question 15

Enzymes are active at what temperature?

Answer 15

25℃, 30℃, or 37℃

Question 16

The optimum temperature for enzymatic activity

Answer 16

37℃

Question 17

The rate of denaturation increases as the temperature increases, and is usually significant at what temperature

Answer 17

40℃ to 50℃

Question 18

Range of temperature that may result to inactivation of enzymes

Answer 18

60-65℃

Question 19

Most physiologic reactions occur at what pH?

Answer 19

pH range of 7 to 8

Question 20

May denature an enzyme or influence its ionic state resulting in structural change or change in the charge of amino acid residue in the active site

Answer 20

Extreme pH level

Question 21

Render enzymes reversibly inactive

Answer 21

Low temperatures (Refrigeration/Freezing)

Question 22

Denature proteins and should be avoided

Answer 22

Repeated freezing thawing

Question 23

Required temp for preservation of enzymes for longer period of time

Answer 23

-20℃

Question 24

Ideal storage temperature for substrate and coenzymes

Answer 24

2℃ to 8℃

Question 25

Ideal storage for LDH (LD4 and LD5)

Answer 25

Room temperature

Question 26

Mostly increases enzyme concentration

Answer 26

Hemolysis

Question 27

Decreases enzyme concentration

Answer 27

Lactescense or Milky specimen

Question 28

Part of the enzyme nomenclature that places the enzyme in its classifications

Answer 28

First digit

Question 29

Represents the subclass to which the enzyme is assigned

Answer 29

Second and Third digits

Question 30

Serial number that is specific to each enzyme

Answer 30

Final and fourth number/s

Question 31

Classification of enzyme that catalyze the removal or addition of electrons (redox reaction)

Answer 31

Oxidoreductases

Question 32

Enzyme classification that catalyze the transfer of a chemical group other than hydrogen from one substrate to another

Answer 32

Transferases

Question 33

Enzyme classification that catalyze hydrolysis or splitting of a bond by the addition of water (hydrolytic reactions)

Answer 33

Hydrolases

Question 34

Enzyme classification that catalyze removal of groups from substrates without hydrolysis. The product contains double bonds

Answer 34

Lyases

Question 35

Enzyme classification that catalyze the intramolecular arrangement of the Substrate compound

Answer 35

Isomerases

Question 36

Enzyme classification that catalyze the joining of two substrate molecules, coupled with breaking of pyrophosphate bond in ATP or similar compound

Answer 36

Ligases

Question 37

General property of enzyme that is a water-free cavity, where the substrate interacts with particular charged amino acid residues; a 3-dimensional protein structure

Answer 37

Active site

Question 38

A cavity other than the active site that may bind regulator molecules

Answer 38

Allosteric site

Question 39

When bound tightly to the enzyme, the coenzyme is called what?

Answer 39

Prosthetic group

Question 40

Apoenzyme + prosthetic group =

Answer 40

Holoenzyme

Question 41

Digestive enzymes in its inactive form originally secreted from the organ of production is called

Answer 41

Proenzyme or zymogen

Question 42

Theory that is based on the premise that the shape of the key (substrate) must fit into the lock (enzyme)

Answer 42

Emil Fisher’s Lock and Key Theory

Question 43

Theory based on the substrate binding to the active site of the enzyme

Answer 43

Kochland’s Induced Fit Theory

Question 44

An enzyme combines with only one substrate and catalyzes only one action

Answer 44

Absolute specificity

Question 45

Enzymes combine with all the substrates in a chemical group

Answer 45

Group Specificity

Question 46

Enzymes reacting with specific chemical bonds

Answer 46

Bond specificity

Question 47

The reaction rate depends only on enzyme concentration

Answer 47

Zero-order reaction

Question 48

The reaction rate is directly proportional to substrate concentration

Answer 48

First-order reaction

Question 49

A general method where the reactants are combined, reaction proceeds for a designated time, the reaction is stopped and measurement is made

Answer 49

Fixed-Time

Question 50

General method where multiple measurements of changed in absorbance are made during the reaction; it is preferred than fixed-time

Answer 50

Continuous monitoring/kinetic assay