Enzymes.txt

• author "Joshua Ellis"
• tags "HUCM"
• description ""
• fileName "Enzymes"
• freezingBlueDBID -1.0
• What is the Michaelis -Menten Equation

Vo= Vmax[S]/(Km+[S]

• Vmax= maximal velocity
• Km= Michaelis constant = (k-1 + k2)/k1
• [S]=substrate concentration

• Michaelis constant
• (k-1 +k2)/k1 (all the rate constants below)

• k1 k2
• E+S <---> ES ---> E+P
• k-1
• Does not change with concentration of enzyme. Basically equal to reaction velocity = 1/2 Vmax

• Small Km = high affinity of the enzyme for substrate. (low concentration of substrate need to half saturate the enzyme--reach v=1/2vmax)
• Large Km = low affinity. Cuz a high concentration is required.

ALWAYS directly proportional. If you half [E] then the Vo and Vmax will also be halved

• When [S] is much less than Km velocity is proportional to [S]-----FIRST ORDER
• When [S] is much greater than Km velocity is constant and equal to Vmax (independent of [S])----- ZERO ORDER

Its the reciprocal of the Michaelis Menten equation

It can tell you the Km and Vmax (as x and y intercepts)

1/vo= Km/(Vmax[S]) + 1/Vmax

Non-Covalent

Binds to active site

• Vmax is the same
• Increased Km because need more [S]
• Graph y intersect is same but x intercept is increased (obvious slope change)

non active site binding

• Vmax decreased
• Km is the same

The graph x intercept is the same