Documenti di Didattica
Documenti di Professioni
Documenti di Cultura
TOPIC 4
BIOCATALYST
REACTION
BY: MIRADATUL NAJWA MUHD RODHI
PART 2
MECHANISTIC MODELS FOR
SIMPLE ENZYME KINETICS
Enzyme Kinetics
Enzyme kinetics refers to the quantitative analysis of all factors that
determine the catalytic potential of an enzyme
Several factors affect the expression of such potential, being the most
important the concentrations of active enzyme, substrates and
inhibitors, temperature and pH
Homogeneous catalysts allow for greater mixing and interaction with the reaction mixture
than heterogeneous catalysts.
Simple Mechanisms
• Chemical mechanism
• Enzyme Catalyzed
Major approaches used in developing a rate expression of enzyme catalyzed
reactions
Rapid-Equilibrium
Henri proposed the effect of substrate concentration on enzyme kinetics :
Conversion of substrate into product involved a reversible reaction between enzyme and substrate
to form an active intermediate that brakes down delivering the product.
Michaelis and Menten (1913) who proposed the first formal hypothesis for enzyme catalysis based
on two sequential steps, as suggested by Henri:
•In the first step the substrate is captured in the active site of the enzyme
•In the second step the amino acid residues at that site chemically process the substrate to
transform it into product, which is subsequently released to let the enzyme free and available for
the next catalytic round.
Equilibrium hypothesis was formulated based on the examination of hydrolytic reactions which in
aqueous milieu are virtually irreversible. However, for reversible reactions (S↔P) that hypothesis
is not applicable and steady-state equations must be derived.
Quasi-Steady-State
• High [S]
– Rate independent
What are two things contribute to the – Saturation of E
maximum velocity limit? – Chemistry is rate limiting
• Amount of enzyme
• Chemical ability of enzyme (catalytic
constant)
Deriving Michaelis-Menten Equation
Vmax [ S ]
v
Km S