Explain how an enzyme catalyzes a biochemical reaction.?

Enzymes are proteins and act as catalysts, meaning they help speed up the chemical reaction by reducing the amount of energy that is needed to get the reaction going (called the activation energy barrier).

Enzymes are substrate-specific, meaning that for every chemical reaction, there is a specific enzyme for the specific reactants (substrates). So, if the reaction is sugar + water (+ Sucrase Enzyme)---> sucrose, then sugar and water are the substrates, and only Sucrase will make this chemical reaction happen.

Co-enzymes (aka co-factors if it is inorganic) are non-protein helpers that are needed in some cases for a particular enzyme to do its job.

Inhibitors basically stop enzymes from working. Competitive inhibitors stop enzymes by directly binding to the active site, so that the correct substrates can't bind there, meaning they can't fit on the enzyme so that the enzyme can help them in their chemical reaction. Non competitive enzymes don't bind to the active site, but bind somewhere else on the enzyme, so that the active site changes shape and the correct substrates don't bind to the active site because they don't fit now that the shape has changed.

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Explain how an enzyme catalyzes a biochemical reaction.?

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