Lecture

Enzymes: Catalytic Strategies

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In course

CH-210: Biochemistry

Les constituants biochimiques de l'organisme, protéines, glucides, lipides, à la lumière de l'évolution des concepts et des progrès en biologie moléculaire et génétique, sont étudiés. ...

Description

This lecture covers the catalytic strategies employed by enzymes, focusing on proteases and carbonic anhydrase. Topics include the cleavage of peptide bonds, stabilization of transition states, covalent catalysis, enzyme inhibition, and the specificity of serine proteases. The mechanisms of catalysis, including the role of zinc ions and water molecules, are discussed. Additionally, the lecture explores the catalytic mechanisms of restriction enzymes and the impact of inhibitors on enzyme kinetics.

Instructor

Christian Heinis

Teaching & PhD PhD Students Thomas Julien Denis Emel, Alessandro Scapozza, Nathan Moïse De Sadeleer, Florian Handel, Hugo André Clerc, Frédéric Brantschen, Grégoire Menoud, Ines Michrafy, Jonathan Schmitt, Laura Elena Massaad Past EPFL PhD Students Jeremy Touati, Shiyu Chen, Sophie Venet-Bonnot, Lisa Pollaro, Inmaculada Rentero Rebollo, Philippe Diderich, Charlotte Urech-Varenne, Silvia Bellotto, Davide Bertoldo, Alessandro Zorzi, Camille Villequey, Jonas Alfred Karl Wilbs, Grigory Karateev, Vanessa Carle

Official source

Ontological neighbourhood

Chemistry

Chemical reactions: Catalysis

Related concepts (32)

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.

Restriction enzyme

A restriction enzyme, restriction endonuclease, REase, ENase or restrictase is an enzyme that cleaves DNA into fragments at or near specific recognition sites within molecules known as restriction sites. Restriction enzymes are one class of the broader endonuclease group of enzymes. Restriction enzymes are commonly classified into five types, which differ in their structure and whether they cut their DNA substrate at their recognition site, or if the recognition and cleavage sites are separate from one another.

Cysteine protease

Cysteine proteases, also known as thiol proteases, are hydrolase enzymes that degrade proteins. These proteases share a common catalytic mechanism that involves a nucleophilic cysteine thiol in a catalytic triad or dyad. Discovered by Gopal Chunder Roy in 1873, the first cysteine protease to be isolated and characterized was papain, obtained from Carica papaya. Cysteine proteases are commonly encountered in fruits including the papaya, pineapple, fig and kiwifruit. The proportion of protease tends to be higher when the fruit is unripe.

Restriction site

Restriction sites, or restriction recognition sites, are located on a DNA molecule containing specific (4-8 base pairs in length) sequences of nucleotides, which are recognized by restriction enzymes. These are generally palindromic sequences (because restriction enzymes usually bind as homodimers), and a particular restriction enzyme may cut the sequence between two nucleotides within its recognition site, or somewhere nearby. For example, the common restriction enzyme EcoRI recognizes the palindromic sequence GAATTC and cuts between the G and the A on both the top and bottom strands.

Chemical specificity

Chemical specificity is the ability of binding site of a macromolecule (such as a protein) to bind specific ligands. The fewer ligands a protein can bind, the greater its specificity. Specificity describes the strength of binding between a given protein and ligand. This relationship can be described by a dissociation constant, which characterizes the balance between bound and unbound states for the protein-ligand system.

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