Lecture

Enzymatic Catalysis: Carbonic Anhydrase

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In course

CH-160(b): General chemistry

Cet enseignement vise l'acquisition des notions essentielles relatives à la structure de la matière, aux équilibres et à la réactivité chimiques. Le cours et les exercices fournissent la méthodologie permettant de résoudre par le raisonnement et le calcul ...

Description

This lecture covers the enzymatic catalysis process, focusing on the example of carbonic anhydrase. It explains competitive and mixed inhibition, the Lineweaver-Burk representation, and the orthogonality of binding of substrate and inhibitor. The role of carbonic anhydrase in CO2 transport, pH regulation, and various physiological processes is also discussed.

Instructor

Samuel Terrettaz

Teaching & PhD Courses Advanced general chemistry CH-160(f) This course aims at the acquisition of essential notions on the structure of matter, chemical equilibria and reactivity. Theoretical teaching and exercise provide the methodology to analyze and solve by reasoning and calculation novel problems of general chemistry. Advanced general chemistry CH-160(g) This course aims at the acquisition of essential notions on the structure of matter, chemical equilibria and reactivi

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Related concepts (26)

Enzyme catalysis

Enzyme catalysis is the increase in the rate of a process by a biological molecule, an "enzyme". Most enzymes are proteins, and most such processes are chemical reactions. Within the enzyme, generally catalysis occurs at a localized site, called the active site. Most enzymes are made predominantly of proteins, either a single protein chain or many such chains in a multi-subunit complex. Enzymes often also incorporate non-protein components, such as metal ions or specialized organic molecules known as cofactor (e.

Enzyme kinetics

Enzyme kinetics is the study of the rates of enzyme-catalysed chemical reactions. In enzyme kinetics, the reaction rate is measured and the effects of varying the conditions of the reaction are investigated. Studying an enzyme's kinetics in this way can reveal the catalytic mechanism of this enzyme, its role in metabolism, how its activity is controlled, and how a drug or a modifier (inhibitor or activator) might affect the rate. An enzyme (E) is typically a protein molecule that promotes a reaction of another molecule, its substrate (S).

Enzyme

Enzymes (ˈɛnzaɪmz) are proteins that act as biological catalysts by accelerating chemical reactions. The molecules upon which enzymes may act are called substrates, and the enzyme converts the substrates into different molecules known as products. Almost all metabolic processes in the cell need enzyme catalysis in order to occur at rates fast enough to sustain life. Metabolic pathways depend upon enzymes to catalyze individual steps.

Suicide inhibition

In biochemistry, suicide inhibition, also known as suicide inactivation or mechanism-based inhibition, is an irreversible form of enzyme inhibition that occurs when an enzyme binds a substrate analog and forms an irreversible complex with it through a covalent bond during the normal catalysis reaction. The inhibitor binds to the active site where it is modified by the enzyme to produce a reactive group that reacts irreversibly to form a stable inhibitor-enzyme complex.

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