Km, or the Michaelis constant, is a measure in enzymology that represents the substrate concentration at which an enzyme operates at half its maximum velocity. It indicates the affinity of the enzyme for its substrate; a lower Km suggests higher affinity, while a higher Km indicates lower affinity.
Km
Km, or the Michaelis constant, is a measure in enzymology that represents the substrate concentration at which an enzyme operates at half its maximum velocity. It indicates the affinity of the enzyme for its substrate; a lower Km suggests higher affinity, while a higher Km indicates lower affinity.
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About Km
Km was introduced in 1913 by Leonor Michaelis and Maud Menten. They developed the concept to describe the kinetics of enzyme-catalyzed reactions, aiming to quantify the relationship between substrate concentration and reaction rate. Their work laid the foundation for modern enzymology and provided a crucial tool for understanding enzyme behavior.
Strengths of Km include its ability to provide insights into enzyme-substrate affinity and its foundational role in enzymology. Weaknesses involve potential inaccuracies in complex systems where multiple substrates or inhibitors are present. Competitors include other kinetic parameters like kcat/Km, which offers a more comprehensive measure of catalytic efficiency.
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How to hire a Km expert
A Km expert must possess strong skills in enzymology, proficiency in kinetic data analysis, and experience with enzyme assays. They should also be adept in using software tools for curve fitting and statistical analysis, and have a solid understanding of biochemical principles governing enzyme-substrate interactions.
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