A lower activation energy allows more reactant molecules to have sufficient energy to undergo the reaction, thus speeding up the reaction rate.

Activation energy is the minimum energy required for reactants to transform into products, initiating a chemical reaction.

Zymogen is an inactive enzyme precursor that requires a biochemical change, such as cleavage, to become an active enzyme.

Apoenzyme is the protein part of an enzyme without its required cofactor, making it inactive until the cofactor binds.

A prosthetic group is a non-protein component covalently or tightly bound to an enzyme, essential for its catalytic activity.

Cofactors are non-protein molecules, including organic coenzymes and inorganic ions, required for the activity of some enzymes.

Holoenzyme is the complete and active form of an enzyme, consisting of the apoenzyme (protein) and its cofactor.

Nicotinamide adenine dinucleotide (NAD+) is a coenzyme that functions as an electron carrier in redox reactions.

Coenzymes are often derived from vitamins, which are essential organic molecules needed for enzyme activity.

Coenzymes form weak, non-covalent bonds with enzymes, allowing them to be released and reused after catalysis.

Cofactors are typically divided into two groups: organic coenzymes (e.g., NAD+) and inorganic metal ions (e.g., Mg^2+).

The active site is the region of an enzyme where substrate molecules bind and undergo a chemical reaction.

All enzymes are globular proteins, which have a specific three-dimensional shape crucial for their catalytic function.

The active site's structure determines the enzyme’s specificity, allowing it to bind only specific substrates.

Enzymes with high substrate specificity typically act on only one specific substrate due to the active site’s unique structure.

Non-competitive inhibition occurs when an inhibitor binds to an allosteric site, altering the enzyme’s active site and reducing its activity without competing with the substrate.

Enzymes are biological catalysts that speed up chemical reactions without being consumed in the process.

Coenzymes are organic molecules that loosely bind to enzymes and assist in catalyzing reactions, often derived from vitamins.

Not all enzymes are fibrous proteins; most are globular, allowing specific active sites for catalysis.

Enzyme specificity is determined by the shape and charge of the active site, which allows the enzyme to bind only to specific substrates with complementary properties.