De K

Question 1

Enzymes that specifically act on one isomer of a compound and not its mirror image.

Answer 1

Stereochemical specificity

Question 2

The ability of an enzyme to catalyze only one specific reaction among many possibilities.

Answer 2

Reaction specificity

Question 3

Enzymes that act on a specific substrate and no other.

Answer 3

Substrate specificity

Question 4

The type of substrate specificity where an enzyme acts on a single, specific substrate.

Answer 4

Absolute specificity

Question 5

A type of specificity where enzymes target groups or specific bonds within substrates.

Answer 5

Relative specificity

Question 6

The optimum range of this environmental factor for most enzymes is between 4 and 9.

Answer 6

pH

Question 7

Enzymes operate at an optimum temperature; beyond this, activity decreases due to denaturation.

Answer 7

Effect of temperature

Question 8

The effect of this on enzymatic reactions is directly proportional until saturation is reached.

Answer 8

Substrate concentration

Question 9

These small molecules are essential for some enzymes to function and include metal ions.

Answer 9

Activators and coenzymes

Question 10

These substances reduce or stop enzymatic activity by binding to the enzyme.

Answer 10

Inhibitors

Question 11

A theory describing an enzyme as rigid and specific to a particular substrate.

Answer 11

Lock-and-key model

Question 12

A theory suggesting that an enzyme’s active site can adapt to fit the substrate.

Answer 12

Induced-fit model

Question 13

The intermediate complex formed between an enzyme and its substrate.

Answer 13

Enzyme-substrate complex

Question 14

Catalysis involving the formation of a transient covalent bond between enzyme and substrate.

Answer 14

Covalent catalysis

Question 15

Catalysis that depends on the proper alignment and proximity of reactants.

Answer 15

Catalysis by proximity and orientation

Question 16

Catalysis involving the transfer of protons (H⁺) during a reaction.

Answer 16

Acid-base catalysis

Question 17

Catalysis involving metal ions to stabilize negative charges or participate directly in reactions.

Answer 17

Metal ion catalysis

Question 18

A type of inhibition where the inhibitor competes directly with the substrate for the active site.

Answer 18

Competitive inhibition

Question 19

A reversible inhibitor binds outside the active site, altering enzyme conformation.

Answer 19

Noncompetitive inhibition

Question 20

Inhibition where the inhibitor binds only to the enzyme-substrate complex, halting reaction progress.

Answer 20

Uncompetitive inhibition

Question 21

Inhibition involving the formation of a permanent covalent bond with the enzyme.

Answer 21

Irreversible inhibition

Question 22

Enzymes regulated by molecules that bind to sites other than the active site.

Answer 22

Allosteric enzymes

Question 23

The inactive form of an enzyme, which requires activation to function.

Answer 23

Proenzyme

Question 24

A regulatory mechanism where a product inhibits an earlier reaction in a sequence.

Answer 24

Feedback control

Question 25

The part of the enzyme where substrate molecules bind.

Answer 25

Active site

Question 26

A regulatory mechanism that ensures energy conservation in cells.

Answer 26

Regulation of enzyme activity

Question 27

This process alters enzyme activity by covalently attaching or removing chemical groups.

Answer 27

Protein modification

Question 28

Enzyme levels in this biological fluid can indicate specific diseases.

Answer 28

Serum

Question 29

The enzyme catalyzing urea hydrolysis, demonstrating absolute specificity.

Answer 29

Urease

Question 30

The study of enzyme activity in diseases to aid in diagnosis and treatment.

Answer 30

Enzyme in medical diagnosis

Question 31

This enzyme’s activity is elevated in liver or bone diseases.

Answer 31

Alkaline phosphatase

Question 32

This enzyme is elevated in pancreatic disease or mumps.

Answer 32

Amylase

Question 33

This diagnostic enzyme indicates a heart attack when elevated.

Answer 33

Creatine phosphokinase

Question 34

A condition that increases enzyme synthesis, as seen with alkaline phosphatase in obstructive liver disease.

Answer 34

Increased enzyme synthesis

Question 35

This method uses electricity to separate enzyme molecules by size or charge.

Answer 35

Electrophoresis

Question 36

A method used to measure enzyme concentrations involving enzyme reactions.

Answer 36

Enzyme assay

Question 37

These chemical changes can indicate hypoxia in cells.

Answer 37

Increased permeability

Question 38

Changes in concentrations of these biomolecules signal abnormal metabolic activities.

Answer 38

Diagnostic enzymes

Question 39

These enzymes catalyze reactions essential for energy production and metabolism.

Answer 39

Functional enzymes

Question 40

The form of an enzyme when it is associated with its cofactor.

Answer 40

Holoenzyme

Question 41

The molecule required to maintain holoenzyme activity but not part of the protein itself.

Answer 41

Cofactor

Question 42

The regulation of this enzyme ensures efficient glucose metabolism.

Answer 42

Hexokinase

Question 43

Inhibition due to heavy metals like lead or mercury binding to enzymes.

Answer 43

Metal ion inhibition

Question 44

The step in enzyme action where the substrate transforms into the product.

Answer 44

Transition state

Question 45

This environmental factor influences the time required for enzymatic reactions.

Answer 45

Effect of time

Question 46

Enzymes are regulated to avoid depleting cellular energy.

Answer 46

Conservation of energy

Question 47

The three steps in enzyme catalysis involve substrate binding, transition state, and product release.

Answer 47

Mechanism of enzyme catalysis