The michaelis menten plot is not a linear plot. Therefore most translate to a reciprocal plot, ie lineweaver-burk
The Michaelis constant (Km) is a means of characterising an enzyme's affinity for a substrate. The Km in an enzymatic reaction is the substrate concentration at which the reaction rate is half its maximum speed. Thus, a low Km value means that the enzyme has a high affinity for the substrate (as a "little" substrate is enough to run the reaction at half its max speed). This is only true for reactions where substrate is limiting and the enzyme is NOT allosteric.
The q calorimeter is the constant and will be needed to find the q metal.
This is a linearized version in the michaelis menten plot. It allows one to study inhibitor easily.
Enthalpy is the amount of energy released or used when kept at a constant pressure. Entropy refers to the unavailable energy within a system, which is also a measure of the problems within the system.
dielectric constant
The Michaelis-Menten constant (Km) is calculated by determining the substrate concentration at half of the maximum reaction rate (Vmax). This value can be obtained by plotting reaction rates against substrate concentrations and identifying the point where the reaction rate is half of Vmax. Km represents the affinity of the enzyme for its substrate.
non competitive increase Km
.2.90 BBC
It indicates that the enzyme has a high affinity for the substrate.
Km is defined as Km=1/2(Vmax). However be careful, the Km is a substrate concentration not a rate.
Sandra Ostojic has written: 'A study of the Michaelis constant for the H4 and M4 isoenzymes of lactate dehydrogenase'
K is the equilibrium constant, Q is a concentration.
Paul Michaelis has written: 'Paul Michaelis' -- subject(s): Exhibitions
Robert Michaelis's birth name is Robert Armand Ren Michaelis.
Herbert Michaelis died in 1939.
Herbert Michaelis was born in 1898.
Liane Michaelis was born in 1953.