Bioc Topic 11

Front 1

6 types of enzymes

Back 1

1. oxidoreductases 2. transferases 3. hydrolases 4. lyases 5. isomerases 6. ligases

Front 2

Oxidoreductases

Back 2

Lactate is the substrate. Pyruvate is the product. NAD+/NADH is the co-factor.

Front 3

Transferases

Back 3

L-alanine / alpha-ketoglutarate are the substrates. Pyruvate/ L-glutamate are the products.

Front 4

Hydrolases

Back 4

Pyrophosphate / water are the substrates. Phosphate is the product.

Front 5

Lyases

Back 5

Pyruvate is the substrate. Acetaldehyde and CO2 are the products.

Front 6

Isomerases

Back 6

L-alanine is the substrate. D-alanine is the product

Front 7

Ligases

Back 7

L-glutamate/NH4 + are the substrates. L-glutamine is the product. ATP is the co-factor.

Front 8

3 Conditions for a chemical reaction to occur

Back 8

1. the molecules must collide to react. 2. There must be enough energy for the two molecules to react. 3. The molecules must be oriented properly.

Front 9

Factors influencing enzyme activity

Back 9

Temperature, pH, Substrate Concentration, Product Concentration, Presence of inhibitors or activators.

Front 10

Temperature

Back 10

reflects weak interactions holding native conformation together.

Front 11

pH

Back 11

due to presence of charged amino acids in the active site.

Front 12

Michaelis-Menten equation is derived based on the following 3 conditions

Back 12

1. state steady assumption 2. Initial velocity assumption 3. rate law.

Front 13

Steady state assumption

Back 13

steady state is the state during which the enzyme substrate complex remains constant.

Front 14

Initial velocity Assumption

Back 14

in the beginning of the reaction there is very little product. so the amount of ES contributed by E+P is negligible.

Front 15

Km

Back 15

small Km means tight substrate binding. high Km means weak substrate binding.

Front 16

Vmax

Back 16

vmax is asymptotically approached as substrate is increased.

Front 17

enzyme inhibition

Back 17

two main types exist: reversible enzyme inhibition and irreversible enzyme inhibition.

Front 18

Reversible enzyme inhibition

Back 18

enzyme activity can be recovered by removing the inhibitor.

Front 19

Irreversible enzyme inhibition

Back 19

inhibitor binds covalently to the enzyme which is then irreversibly inactivated.

Front 20

3 main types of catalysis

Back 20

general acid base catalysis. metal ion catalysis. covalent catalysis.

Front 21

Regulation of enzyme activity

Back 21

Allostery. Binding of regulatory subunits. Covalent modification. Degradation of the enzyme. Limited proteolysis.