Enzymes

Question 1

Glycolysis

Pathway for the utilization of glucose

Answer 1

Anaerobic - lactate

Aerobic - pyruvate

Question 2

Glycolysis

Takes place in

Answer 2

Cytosol

Question 3

Enzymes

Catalyze oxidations and reductions

Answer 3

Oxidoreductases

Question 4

Enzymes

Catalyze transfer of moieties such as glycosyl, methyl or phosphoryl groups

Answer 4

Transferases

Question 5

Enzymes

Catalyze hydrolytic cleavage of C-C, C-O, C-N and other bonds

Answer 5

Hydrolases

Question 6

Enzymes

Catalyze cleavage C-C, C-O, C-N, and other bonds by atom elimination, leaving double bonds

Answer 6

Lyases

Question 7

Enzymes

Catalyze geometric or structural changes within a molecule

Answer 7

Isomerases

Question 8

Enzymes

Catalyze tho joining together of two molecules coupled to the hydrolysis of ATP.

Answer 8

Ligases

Question 9

Bind in a transient, dissociable manner either to the enzymes or to a substrate

Answer 9

Cofactor

Question 10

Serve as recyclable shuttles or group transfer agents that transport many substrates from their point of generation to their point of utilization.

Answer 10

Co enzyme

Question 11

Distinguished by their tight stable incorporation into a proteins structure by covalent or non covalent forces.

Answer 11

Prosthetic group

Question 12

Co factors

Answer 12

Required for function
Not protein like enzymes
Co enzymes are organic co factor (vitamins)

Question 13

Effectors

Answer 13

Not required for function
Positive effector will increase rate of reaction
Negative effector will decrease rate of reaction

Question 14

Maximal number of subtrate molecules converted to product per unit.

Answer 14

Maximal velocity Vmax

Question 15

The substrate concentration at which V1 is the half the maximal velocity attainable at a particular concentration of enzyme.

Answer 15

Michaelis Constant (Km)

Question 16

Factors that affect the rate of a reaction

Answer 16

Substrate concentration
Temperature
pH

Question 17

Reciprocal of the Michaelis-Menten equation

Used to calculate Km and Vmax as well as to determine the mechanism of action of enzyme inhibitors.

Answer 17

Lineweaver-burk plot

Question 18

Any substance that can diminish the velocity of an enzyme catalyzed reaction.

Answer 18

Enzyme inhibitor

Inhibition can be: reversible or irreversible

Question 19

Competetive enzyme inhibitors

Answer 19

Shaped similar to substrate and competes for binding site,
Increased Km
No change in Vmax

Question 20

Noncompetetive enzyme inhibitor

Answer 20

Inhibitor binds to enzyme somewhere other than the active site and halts catalysi
No changed in Km
Lowered Vmax

Question 21

Carbohydrates percentage of sugar

Answer 21

Startches and dextrose - 60%
Sucrose- 30%
Lactose- 5%
Other sugar -5%