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Figure 6.19 Allosteric Regulation of Enzymes. Conformational change. Inactive form. Active form. The enzyme switches back and forth between the two forms. They are in equilibrium. Figure 6.19 Allosteric Regulation of Enzymes. Allosteric site. Active site. Conformational change.
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Figure 6.19 Allosteric Regulation of Enzymes Conformational change Inactive form Active form The enzyme switches back and forth between the two forms. They are in equilibrium.
Figure 6.19 Allosteric Regulation of Enzymes Allosteric site Active site Conformational change Inactive form Active form
Figure 6.19 Allosteric Regulation of Enzymes Catalytic subunit Regulatory subunit Allosteric regulation Inactive form When the enzyme is in its inactive form, the allosteric sites on the regulatory subunits can accept inhibitor.
Figure 6.19 Allosteric Regulation of Enzymes Catalytic subunit Regulatory subunit Allosteric inhibitor Allosteric regulation Inactive form
Figure 6.19 Allosteric Regulation of Enzymes Allosteric regulation Active form When the enzyme is in its active form, the active sites on the catalytic subunits can accept substrate.
Figure 6.19 Allosteric Regulation of Enzymes Substrate Cooperativity Once a site is filled with a substrate or inhibitor, binding at a second site of the same type is favored.
Figure 6.19 Allosteric Regulation of Enzymes No product formation Product formation Cooperativity