#lineweaver-burk

[collegeandknowledge]

1st order reaction is just S^-1

2nd order reaction is M^-1S^-1

Michaelis-Menten equation says V0 = Vm[S] / (Km + [S])

Km is measured in Molarity

Catalytic efficiency is Kcat ÷ Km

Perfect enzymes have the highest Kcat÷Km values

A big Km puts your line in Lineweaver-Burk plot closer to the origin

The lower the slope in Lineweaver-Burk, the higher the catalytic efficiency

The number of active sites filled is [substrate]÷(Km + [substrate])

[ubrpirates]

Biochem

Enzyme Turnover = Vmax=Kcat*[S]total 

Michaelis-Menton Equation = V0=(Vmax*[S])/([S]+Km)]

Specificity Constant = Kcat/Km

Lineweaver-Burk Plot =  (1/V0)= (Km/Vmax)*(1/[S])+(1/Vmax)

[S] -- Concentration of substrate.

[S]total -- Total Enzyme Concentration.

V0 -- Initial Velocity of [S].

Vmax -- Maximum formation of product when [S] is saturating.

Kcat -- Number of substrate molecules a single enzyme can convert to product in a single second. 

Km -- Michaelis Constant.