Here is my understanding to this symbol:
The Michaelis Constant, KM determins enzyme-substrate interaction. This value is often dependent on pH, temperature, and ionic strength. The KM is able to detect two factors: One is the concentration of substrate when the reaction velocity is half that of the maximal velocity; thus, the Michaelis constant measures the concentration of substrate required for a significant catalysis to take place. From the graph below one can determine the value of KM. It is found at the substrate concentration when the reaction rate is half of its maximum value (Vmax/2).
Chem. 504. KM at Vmax/2.
Secondly, it is able to detect the strength of binding of the enzyme-substrate complex (ES). Its value includes the affinity of substrate for enzyme, also the rate at which the substrate bound to the enzyme is converted to product. Using the below equation, only if k2 is much smaller than k_1 will KM equal a binding affinity (see equation 1 and Michaelies constant equation below).

Michaelis Constant equation

So for enzymatic reactions which exhibit simple Michaelis–Menten kinetics, the enzymatic reaction is assumed to be irreversible, and the product does not bind to the enzyme. The equation for the Michaelis Constant is KM= (k-1 + k2)/k1 sometimes it can be seen as [ES] = [E][S]/KM. using this equation, a high KM indicates weak binding and low KM indicates strong binding.
The later evidence I present here is quiz five, July 30, 2009 Chem 504. Question eight askes if k2 (the rate of the reaction to form product) is small what does this say about KM?
From the relation between k2 and KM I explained that if k2 is small then it is the rate determining step. KM would be low because it is directly related to k2 which means that the binding between the enzyme and the substrate at Vmax/2 is strong.
In question six for the same quiz, the graph shows the complete understanding of how the Michaelies-Menton equation is a combination of the first and zero order. It is first order when the enzyme is still binding with the substate and a zero order at equilibrium where the break down equals the formation of the enzyme-substrate complex ( [ES]break = [ES]formation ).
Chem 504. Quiz five
Question nine below is another evidence of understanding which enzyme substrate reaction has a better KM. I chose [S]1 because as shown in the diagram, the lower KM the better binding between the substrate and the enzyme at Vmax/2.