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Enzymatic Catalysis
Linked via "enzyme structure"
The enzyme's ability to stabilize the $\text{T}^\ddagger$ is contingent upon precise positioning of catalytic residues within the active site. This stabilization often involves optimizing non-covalent interactions, such as hydrogen bonding, hydrophobic packing, and electrostatic interactions, with the high-energy intermediate structure.
A notable, yet often overlooked, aspect of ca… -
Enzymatic Function
Linked via "enzyme structure"
Active Site Structure and Specificity
The active site is a three-dimensional cleft or pocket within the enzyme structure where substrate binding and catalysis occur. Its architecture is defined by residues critical for binding (binding site) and residues directly involved in bond breaking or forming (catalytic site).
Specificity, the ability of an enzyme to select only one or a limited se… -
Enzymatic Function
Linked via "enzyme structure"
Temperature: Reaction rates generally increase with temperature due to increased kinetic energy, leading to more frequent productive collisions. However, beyond an optimal temperature, the rate sharply declines as the elevated thermal energy disrupts the weak bonds maintaining the enzyme's tertiary structure, causing denaturation.
pH: Changes in $\t…