Enzymes: structure and function

12 important questions on Enzymes: structure and function

What are the enzyme classes?

The enzyme classes are oxidoreductase, transferase, hydrolase, lyase, isomerase, and ligase.

What is the active site of an enzyme?

An enzyme's active site is a hollow or a cleft in the protein with essential amino acids able to bind substrates or participate in the reaction mechanism.

Which amino acids can acts as nucleophiles?

Cysteine and serine can act as nucleophiles. In some enzymes, lysine can also act as a nucleophile.
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What are the amino acids responsable for acid-base catalysis?

Histidine is a common acid-base catalyst. Glutamate, aspartate, and tyrosine can also act as acid-base catalysts.

What involves external control of enzymes?

External control involves the regulation of chemical messengers initiated outside the cell membrane. This ultimatly involves the phosphorylation of enzymes.

What are allosteric inhibitors?

Allosteric inhibitors alter the shape of the binding site so the binding site is no longer recognized by chemical messengers. The shape is altered by binding another binding site that the active site.

What is the effect of genetic polymorphism?

Genetic polymorphism causes differences in amino acids sequence leading to possible different amino acids with possible different/no function.

What euqation subscribes enzyme catalyzed reactions?

Enzyme catalyzed reactions are subscribed by the Michaelis-Menten equation.

What is the role of a Lineweaver-Burk plot?

A Lineweaver-Burk plot provides more accurate values for the maximum rate and the Km.

What is the formula for Km.

Km = K2 + K1 / K3

What is the enzyme, substrate, product relation?

E + S --> ES --> E + P

What is the formula for the concentration of enzyme and substrate.

[E] * [S] / [ES]

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