I wonder if it is possible to determine a correlation between these properties, Do you have any references in regards?
Thanks in advance for your answers.
In most of the cases (because k2 is much lower than k-1), Km is inversely proportional to substrate affinity. As greater Km, as lower affinity.
Puedes encontrar referencias en cualquier texto de bioquimica con algun tema dedicado a la enzimologia. Si quieres mas detalles, solo tiene que decirmelo, .
I do agree with Solano, As per MM kinetics model Km is a reflection of affinity of an enzyme towards its substrate..
The Km is a defined as dissociation constant of the Enzyme-Substrate complexe.
Km = ([E].[S])/([ES)
From the above equation you can see that if the ES concentration is higher the Km value was lower. Therefore the enzyme affinity was higher. But if ES concentration was lower, therefore the enzyme has a less affinitiy toward its substrate.
A standard biochemistry book will give you the answers you need. The Km is not the KD or dissociation constant for the enzyme/ substrate complex except under certain circumstances as Francisco has mentioned.
The Km value is known as the affinity of the enzymes to substrates and the lower values of Km emphasize the higher affinity between enzymes and substrates. As for Vmax, its value is important for chemical reactions optimization. For example, the Km value could be affected after enzyme immobilization due to diffusional limitation of the substrate or to conformational changes of the enzyme.
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Km is complex value, where afinity is only one out of many factors. Km could be changed by immobilization of enzymes. Some more INFO in publication.
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If you will calculate binding of your substrate by titrating a constant concentration of the substrate with the increasing concentartion of the enzyme or protein of your interest. you can calculate its Kd values which will tell you about the affinity of the enzyme to its substarte. additionally, nature of the curve will also tell you about the mode of its binding. But if you want to calculate its Km, then you need to do the time course rate for each of the diffrent concentartion of substrate titrated to constant concentration of the enzyme. Slope of time course will give you the rate and if you will plot the inverse of the rate and the inverse of the concentration used , you will get the Km. This is the biochemical way to elucidate the enzyme Kd and Km. Hope this will help to you.
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