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Flashcards in German: Enzymes Deck (13):
1

What is an enzyme made of?

Globular proteins

2

What is a coenzyme?

A chemical that binds to the enzyme and allows or helps it to bind to a substrate.

3

What is a cofactor

An inorganic ion that binds to an enzyme and that is necessary to the enzyme to bind a substrate.

4

What is a holoenzyme?

An enzyme that is bound to all the necessary cofactors and coenzymes that is ready to bind a substrate.

5

How do enzymes lower the activation energy of a reaction?

They shift the substrate into the transition state by being complimentary to that transition state.

6

What is the enzyme responsible for the catalysis of the reaction turning glucose 6-Phosphate into Fructose 6-Phosphate?

Phosphohexose isomerase

7

Why is there a Vmax in a reaction?

Saturation of enzymes and more substrates are being turned into product so there is less substrate to bind.

8

What is the Km?

Concentration at which the initial reaction velocity is 1/2 the Vmax. It determines how effective an enzyme is at producing product from a given amount of substrate. The more efficient the enzyme the further to the left the Km will be.

9

What is michaelis-menten kinetics

A reaction the shows a single non-sigmoidal curve. It has a Km and a Vmax.

10

What are two ways an enzyme can catalyze multiple substrates alone a diverse pathway?

1. Involving a ternary complex: Enzyme will bind to S1 and S2 and turn them both into P1 and P2 at the same time.2. Not involving a ternary complex: Enzyme will bind S1 and make P1, then bind S2 and make P2 at a different time.

11

What is an irreversible inhibition?

A suicide mission of an inhibitor that will bind to an enzyme and inhibit. This is non reversible.

12

What is the difference between reversible inhibition and allosteric inhibition?

Reversible inhibition follows michaelis menten kinetics and involves the inhibitor binding directly to the active site. Allosteric inhibition does not follow michaelis-menten kinetics and involves an inhibitor binding to a different site on the enzyme, causing a conformational change that will effect the enzyme in some way.

13

What are the two kinds of allosteric inhibition?

1. Homotropic: When the substrate itself will regulate enzyme function.2. Heterotrophic regulation: When a non-substrate molecule regulates enzyme function.