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regulation
and
catalysis
Content
Active site
Coenzyme,
Nomenclature
Catalysis
Kinetics
Inhibition
Regulation
Special class
Introduction
Biocatalyst—homeostasis
External—Blood clotting
Internal—metabolism
Organic Inorganic
Fe-S cluster
Prosthetic
group
Enzyme nomenclature
Oxidoreductase
Transferase
Hydrolase
Lyase
Isomerase
Ligase
Enzyme kinetics
Equation
Significance
Plots
Mechanism of action
Enzyme velocity vs substrate
concentration
Michalis - Menten equation
Vmax [S]
Velosity = V =
[S] + KM
Significance of Km
kM= k - 1 +k + 2 /k + 1
When k - 1 >>>k + 2
k c a t / K m =K e f f
Assumptions
The concentration of
substrate greater than
enzyme
No cooperativity
product -allosteric
modulator
Plots
Enzyme Inhibition
Enzyme Inhibition
Irreversible Reversible
Competitive
Un-competitive
Non-competitive
Irreversible inhibition
Reversible Competitive inhibition
Reversible
Uncompetitive inhibition
Reversible
Non competitive inhibition
Enzyme regulation
Allosteric Control
Covalent Modification
Protein Processing
Allosteric control
Aspartate trans carbamoylase
Catalytic
trimer
Regulatory
Dimer
Regulatory
Dimer
Regulatory
Dimer
Catalytic
trimer
Cooperativity
Feedback Inhibition
Covalent modification of enzyme
Protein processing Zymogen
activation
Enzyme catalysis
Bond strain
Proximity/Orientation effect
Electrostatic catalysis
Covalent catalysis
Quantum tunnelling
Bond strain
Proximity/orientation
effect
Electrostatic catalysis
phosphoenzyme
synthase
Lys(NH2) class—Fru-
diphosphate-aldolase
Quantum tunnelling
Ribozyme
Abzyme
Isozyme and Allozyme
Bi-substrate reaction
Sequential reaction--Ordered
sequential
Ping-Pong reaction
Emil Fischer
(1852-1919)
Lock and key model
D. Koshland
(1920-2007)
Leonor Michaelis Maud Menten
(1875–1949) (1879–1960)
Linear equation for
Lineweaver-Burk plot
Succinate Dehydrogenase
-competitive inhibitor
Reaction
Positive and negative
co-operativity