Enzyme Kinetics Flashcards
Isoenzymes
Enzymes with different protein structures that catalyse the same reaction.
They are coded by different genes
Enzyme Kinetics define
Study of enzymes by determining their reaction rates.
- How rate varies with different substrate concentrations, presence of inhibitors, different temperatures, presence of metal ions/co-factors.
- Initial reaction velocity = V0
Michaelis-Menten model - hyperbolic kinetics
E+S <> ES <> E+P E=enzyme S=substrate ES=enzyme-substrate complex P=product K1=forward rate constant K-1=reverse rate constant
Michaelis Menten Equation
Vo = (Vmax[S]) / (Km+[S])
When Vo=1/2 Vmax Km=[S]
Lineweaver-Burke plot
1/Vo=Km/Vmax x 1/[S]
Forms straight line equation.
Y-intercept = 1/Vmax
X-intercept = -1/Km
What does Km tell us about an enzyme?
Km = Substrate concentration at which the enzyme is 50% saturated with substrate.
Higher Km=lower affinity of enzyme for its substrate.
Lower Km=high affinity to substrate.
Kcat is the Turnover number
Kcat = number of molecules of substrate converted to product by a molecule of enzyme at saturating levels of substrate per second.
Specificity Constant
= Kcat/Km
Optimum enzyme function would have low Km(high affinity for substrate) and high Kcat(fast turnover speed)
Therefore most efficient enzymes will have a high specificity constant.