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Enzyme-catalyzed Coenzyme
Enzyme catalysis refers to the process in which enzymes act as biocatalysts to accelerate chemical reactions. Many enzymes require coenzymes to perform their catalytic functions. Coenzyme is an essential part of the enzyme catalysis process, which is usually a small non-protein molecule that can assist the conversion of the enzyme catalyzed substrate. Coenzyme can participate in multiple steps in the enzyme catalysis process, such as substrate binding, catalytic reaction and product release, etc.

Common Enzyme-catalyzed Coenzymes include:
NAD+/NADH: Participate in many redox reactions, transfer electrons from the substrate to NAD+, and generate NADH.
FAD/FADH2: Participate in various redox reactions, transfer electrons from the substrate to FAD, and generate FADH2.
Coenzyme A: participates in the metabolism of fatty acids and some amino acids, and can break the ester bond in the substrate.
Biotin: participate in the catalytic reaction of various carboxylases, and can transfer CO2 groups.
TPP: Participates in many decarboxylation reactions, which can promote the cleavage of carboxyl groups in substrates.
CoA: participates in many acyl transfer reactions and can transfer an acyl group from one substrate to another.
Coenzymes play an important role in the process of enzyme catalysis, they can enhance the catalytic activity of enzymes, and can also regulate the catalytic action of enzymes.