Michaelis-Menten constant, Km, is a vital parameter in enzyme kinetics that sheds light on the substrate affinity, catalytic efficiency, and specificity of enzymes. Its significance spans from fundamental biochemical understanding to practical applications in drug design, biotechnology, and enzyme-related processes.

Michaelis Constant (Km): Enzymes have varying tendencies to bind their substrates (affinities). An enzyme's K m describes the substrate concentration at which half the enzyme's active sites are occupied by substrate. A high K m means a lot of substrate must be present to saturate the enzyme, meaning the enzyme has low affinity for the substrate.

2019年2月2日 · Two commonly encountered parameters in enzyme kinetics are the Michaelis constant (Km) and the dissociation constant (Kd), both report aspects of a substrate’s binding behavior. In this article, I clarify these terms' definitions, differences and biochemical significance .

2024年10月1日 · What Does Km Mean in Enzyme Kinetics? Km is a critical parameter in enzyme’s kinetics. It gives insight into the affinity of an enzyme for its substrate. A lower Km value indicates high affinity, meaning the enzyme can achieve significant reaction rates even at low substrate concentrations. Conversely, a higher Km suggests lower affinity.

2025年1月28日 · When it comes to enzymatic reactions, the Michaelis constant (Km) is a critical parameter that provides insights into the enzyme’s affinity for its substrate. Here’s an in-depth explanation of what high Km means and why it matters:

Kd, or the dissociation constant, reveals the affinity between an enzyme and its inhibitor, whereas Km, the Michaelis constant, measures the enzyme’s affinity for its substrate during catalysis. Grasping the nuances between Kd and Km will not only boost your knowledge but also sharpen your research and application skills in the lab.

2023年8月31日 · Another parameter of an enzyme that is useful is known as KM , the Michaelis constant. What it measures, in simple terms, is the affinity an enzyme has for its substrate. Affinities of enzymes for substrates vary considerably, so knowing KM helps us to understand how well an enzyme is suited to the substrate being used.

2025年1月21日 · The Michaelis constant \(K_m\) is the substrate concentration at which the reaction rate is at half-maximum, and is an inverse measure of the substrate's affinity for the enzyme—as a small \(K_m\) indicates high affinity, meaning that the rate will approach \(V_{max}\) more quickly.

2021年11月29日 · Kinetic parameters (kcat and Km) derived from the Michaelis–Menten equation are widely used to characterize enzymes. kcat / Km is considered the catalytic efficiency or substrate specificity of an enzyme toward its substrate. N-Myristoyltransferases (NMTs) catalyze the N-terminal glycine myristoylation of numerous eukaryotic proteins.

2024年11月14日 · Enzymes with high affinity (low Km) bind substrates more efficiently, achieving ½ Vmax at low substrate concentrations. (1 mark) Example: Lysozyme (Km = 6 µmol dm⁻³) has high affinity for acetylglucosamine, making it highly efficient even with low substrate availability.