The active site is the part of an enzyme where substrate molecules bind, while other parts of the enzyme do not interact with the substrates.
When the substrate enters the active site, it undergoes chemical change (catalysis).
The active site of an enzyme has a specific shape that fits only one type of molecule, called its substrate.
Enzymes catalyze the formation and breakdown of cellular metabolites during anabolic and catabolic processes.
Enzyme-substrate complex is formed when the substrate binds to an enzyme.
Enzyme catalysis increases the rate of a chemical reaction by lowering the activation energy barrier.
Active sites have specific shapes to fit their corresponding substrates.
Enzymes lower activation energy by providing a specific environment for the reaction to occur.
Enzymes are proteins that act as biological catalysts to speed up chemical reactions without being consumed or changed themselves.
An example of this is amylase, which breaks down starch into maltose.
Amylose has a helical structure, so if another carbohydrate had a different structure, it would not fit into the active site of amylase.
Enzymes are proteins made up of amino acids joined together by peptide bonds.
Amino acids have two functional groups - an R group and an amine (-NH2) or carboxyl (-COOH) group.
An example of an enzymatic reaction is the conversion of glucose to pyruvic acid by hexokinase.
Glucose-6-phosphate can be converted into fructose-6-phosphate through another enzymaticprocess.
An enzyme's activity can be influenced by factors such as temperature, pH, concentration of reactants, inhibitors, activators, cofactors, and allosteric regulators.
Temperature affects enzyme function because enzymes work best at their optimal temperature, which varies depending on the enzyme.
High temperatures cause denaturation of enzymes, which disrupts their tertiary structure and reduces their ability to function properly.
Enzymes increase the speed at which reactions take place without being used up or changed themselves.