Enzymes are biological catalysts that speed up chemical reactions by lowering the activation energy required. Each enzyme is highly specific for its substrate, determined by the unique structure of the enzyme's active site. One classic model to describe enzyme action is the 'Lock and Key' model, which suggests that the substrate fits into the enzyme's active site like a key in a lock. Another model is the 'Induced Fit' model, which posits that the binding of the substrate induces a change in the enzyme's shape, enhancing the fit between them.
Consider an enzyme that catalyzes the conversion of substrate A into product B. If the enzyme concentration is doubled while keeping substrate concentration constant, what effect would this have on the reaction rate under saturating substrate conditions?