Substrate affinity refers to the strength of the interaction between an enzyme and its substrate, often influencing the rate of a biochemical reaction. It is quantitatively represented by the Michaelis constant (Km), with a lower Km indicating higher affinity and efficiency in catalysis.

Substrate Affinity

Enzyme and its substrate

Biochemical reactions are processes that occur within living organisms to sustain life, involving the transformation of molecules through enzyme-catalyzed reactions. These reactions are essential for metabolism, cellular function, and the regulation of biological pathways, enabling organisms to grow, reproduce, and respond to environmental changes.

Biochemical Reaction

The Michaelis constant (Km) is a crucial parameter in enzyme kinetics that measures the substrate concentration at which an enzyme-catalyzed reaction proceeds at half its maximum velocity (Vmax). It provides insight into the affinity between an enzyme and its substrate, with a lower Km indicating higher affinity and vice versa.

Michaelis Constant

Km, or the Michaelis constant, is a crucial parameter in enzyme kinetics that represents the substrate concentration at which the reaction velocity is half of its maximum value. It provides insight into the affinity between an enzyme and its substrate; a lower Km indicates higher affinity, while a higher Km suggests lower affinity.

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