Related Experiment Video

Updated: Sep 28, 2026

Direct Detection of the Acetate-forming Activity of the Enzyme Acetate Kinase
05:51

Direct Detection of the Acetate-forming Activity of the Enzyme Acetate Kinase

Published on: December 19, 2011

Catalysis by acetylcholinesterase: evidence that the rate-limiting step for acylation with certain substrates

T L Rosenberry

    Proceedings of the National Academy of Sciences of the United States of America
    |October 1, 1975
    PubMed

    More Related Videos

    A Facile Protocol to Generate Site-Specifically Acetylated Proteins in Escherichia Coli11:08

    A Facile Protocol to Generate Site-Specifically Acetylated Proteins in Escherichia Coli

    Published on: December 9, 2017

    An Acetyl-Click Chemistry Assay to Measure Histone Acetyltransferase 1 Acetylation05:44

    An Acetyl-Click Chemistry Assay to Measure Histone Acetyltransferase 1 Acetylation

    Published on: January 26, 2024

    Related Concept Videos

    Introduction to Mechanisms of Enzyme Catalysis01:13

    Introduction to Mechanisms of Enzyme Catalysis

    For many years, scientists thought that enzyme-substrate binding took place in a simple "lock-and-key" fashion. This model stated that the enzyme and substrate fit together perfectly in one instantaneous step. However, current research supports a more refined view scientists call induced fit. The induced-fit model expands upon the lock-and-key model by describing a more dynamic interaction between enzyme and substrate. As the enzyme and substrate come together, their interaction causes a mild...
    Esters to Carboxylic Acids: Acid-Catalyzed Hydrolysis01:13

    Esters to Carboxylic Acids: Acid-Catalyzed Hydrolysis

    Hydrolysis of esters under acidic conditions proceeds through a nucleophilic acyl substitution. In the presence of excess water, the reaction proceeds in a reversible manner, forming carboxylic acids and alcohols.
    During hydrolysis, the ester is first activated towards nucleophilic attack through the protonation of the carboxyl oxygen atom by the acid catalyst. The protonation makes the ester carbonyl carbon more electrophilic. In the next step, water acts as a nucleophile and adds to the...
    Alkylation of β-Ketoester Enolates: Acetoacetic Ester Synthesis01:07

    Alkylation of β-Ketoester Enolates: Acetoacetic Ester Synthesis

    Acetoacetic ester synthesis is a method to obtain ketones from alkyl halides and β-keto esters. The reaction occurs in the presence of an alkoxide base that abstracts the acidic proton of the β-keto esters. The step results in an enolate ion which is doubly stabilized. The enolate then reacts with an alkyl halide via the SN2 process to produce an alkylated ester intermediate with a new C–C bond. The hydrolysis of the intermediate, followed by acidification, results in an alkylated β-keto acid.
    Introduction to Mechanisms of Enzyme Catalysis01:13

    Introduction to Mechanisms of Enzyme Catalysis

    For many years, scientists thought that enzyme-substrate binding took place in a simple "lock-and-key" fashion. This model stated that the enzyme and substrate fit together perfectly in one instantaneous step. However, current research supports a more refined view scientists call induced fit. The induced-fit model expands upon the lock-and-key model by describing a more dynamic interaction between enzyme and substrate. As the enzyme and substrate come together, their interaction causes a mild...
    Indirect-Acting Cholinergic Agonists: Mechanism of Action01:18

    Indirect-Acting Cholinergic Agonists: Mechanism of Action

    Indirect-acting cholinergic agonists work by interacting with an enzyme called acetylcholinesterase (AChE) in the synaptic cleft. They can be reversible or irreversible inhibitors and have different effects on the enzyme.
    Reversible inhibitors like edrophonium bind to a specific part of the enzyme called the anionic catalytic site. They form noncovalent bonds, which means they are not strongly attached to the enzyme. This creates a temporary and less stable enzyme–inhibitor complex, leading to...
    Phase II Reactions: Acetylation Reactions01:24

    Phase II Reactions: Acetylation Reactions

    Acetylation, a phase II biotransformation reaction, introduces an acetyl group to drugs or their metabolites. Acetyltransferase enzymes facilitate this reaction, which resembles α-amino acid conjugation due to the addition of a functional group to the drug molecule.
    The substrates for acetylation are typically drugs or their metabolites with an amino, sulfonamide, or hydrazine functional group. Acetylation can occur at several points in the drug molecule, including primary, secondary, and...