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In an enzyme-catalyzed reaction, the general steps include: substrate binding to the active site of the enzyme, forming an enzyme-substrate complex. This complex undergoes a reaction, leading to the formation of products. Finally, the products are released from the enzyme, which remains unchanged and can continue catalyzing more reactions. The enzyme facilitates the reaction by lowering the activation energy required for the reaction to occur, increasing the reaction rate.
Enzyme-substrate specificity means that a substrate can fit into an enzyme similar to a key fitting into a lock. The active site of the enzyme is what determines its specificity. An enzyme can hence catalyze a reaction with a specific substrate, such as amylase catalyzing starch molecules. During these reactions, the substrate is held in a precise optimum position to create and break bonds, catalyzing the molecule.
an active site in an enzyme is the area that breaks the bond in its substrate. E.g. a maltose molecule's glycocide bond is broken by the active site in a maltase enzyme.
a. The substrate can be altered so it is induced to fit into the enzyme's active site. b. The enzyme changes its shape slightly as it binds to the substrate. c. The enzyme is altered so it is induced to fit many different types of substrate. d. Several sites on an enzyme can be induced to act on a substrate.
A competitive inhibitor often binds to an enzyme's active site. Noncompetitive inhibitors usually bind to a different site on the enzyme.