Formation of enzyme-substrate complex
• It is the fast and reversible reaction
• It attain equilibrium very rapidly
• Formation of E-P & breakdown of E-P to E & P are slow
& irreversible
Michaelies-Menten Theory
• Lenor Michaelies & Mand Menten (1931) proposed this
theory to explain the kinetic properties
• Then combine with it and finally form a stable ES
complex with rate constant K1
ES complex may dissociate in to E & S with rate constant
K2, substrate transform to P & E-S complex become E-P
complex with rate constant K-1
,• Leonor Michaels and Moud Menten (1913)
proposed following assumptions.
• i. Only a single substrate and a single product are
formed in enzymatic reaction.
• ii. The process continued essentially to its
completion.
• iii. Concentration of substrate is much greater than
the enzyme in the system.
• iv. An intermediate enzyme substrate complex is
formed.
, • The rate of decomposition of the substrate is
proportional to the concentration of the ES
• They proposed an equation popularly accepted as
Michaelis -- Menten's equation, which concerned
the velocity of enzymatic reaction.
Vo = Vmax [S]
KM + [S]
• Where Km is the Michaelis constant 'S' is the
substrate concentration, Vmax - maximum velocity
of the reaction and V0 is the initial velocity.
• Km value is constant for all enzymes up to the half
of the maximum velocity of reaction. Greater is the
ES complex period the lower is the Km value.
• It is the fast and reversible reaction
• It attain equilibrium very rapidly
• Formation of E-P & breakdown of E-P to E & P are slow
& irreversible
Michaelies-Menten Theory
• Lenor Michaelies & Mand Menten (1931) proposed this
theory to explain the kinetic properties
• Then combine with it and finally form a stable ES
complex with rate constant K1
ES complex may dissociate in to E & S with rate constant
K2, substrate transform to P & E-S complex become E-P
complex with rate constant K-1
,• Leonor Michaels and Moud Menten (1913)
proposed following assumptions.
• i. Only a single substrate and a single product are
formed in enzymatic reaction.
• ii. The process continued essentially to its
completion.
• iii. Concentration of substrate is much greater than
the enzyme in the system.
• iv. An intermediate enzyme substrate complex is
formed.
, • The rate of decomposition of the substrate is
proportional to the concentration of the ES
• They proposed an equation popularly accepted as
Michaelis -- Menten's equation, which concerned
the velocity of enzymatic reaction.
Vo = Vmax [S]
KM + [S]
• Where Km is the Michaelis constant 'S' is the
substrate concentration, Vmax - maximum velocity
of the reaction and V0 is the initial velocity.
• Km value is constant for all enzymes up to the half
of the maximum velocity of reaction. Greater is the
ES complex period the lower is the Km value.
