Enzyme__notes_

Enzyme

Biological catalysts that control and accelerate the rate of biochemical reactions in the cell without being permanently changed in the process.

Cofactors

Molecules that assist enzymes in catalyzing reactions, can be inorganic (like ions) or organic (like vitamins).

Active site

The region on the enzyme where the substrate binds, comprised of functional groups of amino acids and cofactors.

Lock-and-key hypothesis

The active site of an unbound enzyme is complementary in shape to the substrate, allowing them to fit together.

Induced-fit hypothesis

The active site forms a shape complementary to the substrate only after the substrate has been bound.

Specificity

The property of enzymes to be highly specific, with each enzyme catalyzing only one kind of substrate.

Reversible inhibitors

Compounds that bind to enzymes and can dissociate from them, affecting enzyme activity.

Competitive inhibitors

Inhibitors that bind to the active site of an enzyme, competing with the substrate.

Noncompetitive inhibitors

Inhibitors that bind to another part of an enzyme, altering its shape and reducing its activity.

Optimal temperature

The temperature at which an enzyme functions most efficiently.

Optimal pH

The specific pH range where an enzyme operates most effectively, typically between 5-9.

Covalent modification

The regulation of enzyme activity through reversible modifications of one or more amino acid residues.

Phosphorylation

A type of covalent modification crucial for regulating enzyme activity by adding a phosphoryl group.

Allosteric regulation

The regulation of an enzyme's activity through the binding of a regulatory molecule at a site other than the active site.

Cooperativity

An allosteric regulation that amplifies enzyme activity through conformational changes in the enzyme structure.

Feedback inhibition

A process where the end product of a metabolic pathway inhibits the pathway, preventing resource wastage.