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Amino acids

Amino acids

Amino acids are the monomers that comprise proteins. Each amino acid has the same fundamental structure, which consists of a central carbon atom, or the alpha (α) carbon, bonded to an amino group (NH2), a carboxyl group (COOH), and to a hydrogen atom. Every amino acid also has another atom or group of atoms bonded to the central atom known as the R group. There are 20 common amino acids present in proteins, each with a different R group. Variation in the amino acid sequence is responsible for...

Acid Halides to Carboxylic Acids: Hydrolysis

Acid Halides to Carboxylic Acids: Hydrolysis

Hydrolysis of acid halides is a nucleophilic acyl substitution reaction in which acid halides react with water to give carboxylic acids. The reaction occurs readily and does not require acid or a base catalyst.
As shown below, the mechanism involves a nucleophilic attack by water at the carbonyl carbon to form a tetrahedral intermediate. This is followed by the reformation of the carbon–oxygen π bond along with the departure of a halide ion. A final proton transfer step yields carboxylic acid...

Amides to Carboxylic Acids: Hydrolysis

Amides to Carboxylic Acids: Hydrolysis

Amides can undergo either acid-catalyzed hydrolysis or base-promoted hydrolysis through a typical nucleophilic acyl substitution. Each hydrolysis requires severe conditions.
Acid-catalyzed hydrolysis:
Hydrolysis of amides under acidic conditions yields carboxylic acids. Since the reaction occurs slowly, hydrolysis requires the conditions of heat.
The mechanism begins with the protonation of the carbonyl oxygen by the acid catalyst. The protonation makes the amide carbonyl carbon more...

Esters to Carboxylic Acids: Acid-Catalyzed Hydrolysis

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...

Hydrolysis

Hydrolysis

Overview
Hydrolysis is a chemical reaction in which the addition of water breaks down a polymer into its simpler monomer units. For example, peptides break into amino acids, carbohydrates into simple sugars, and DNA into nucleotides. Enzymes often facilitate these processes.
Hydrolysis Reverses Dehydration Synthesis
Complex carbohydrates can be broken down by breaking the bonds between individual sugar units. The reaction breaks a glycosidic bond as water is added to the compound. The...

Lysosomal Hydrolases

Lysosomal Hydrolases

Lysosomes are the site for the degradation of macromolecules and biological polymers released during membrane trafficking events such as secretory, endocytic, autophagic, and phagocytic pathways. The membrane-enclosed area of the lysosome, called the lumen, contains hydrolytic enzymes active in an acidic environment. These acid hydrolases are functional at a pH between 4.5 and 5 and are involved in cellular processes such as cell signaling, energy metabolism, restoration of the plasma membrane,...

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Related Experiment Video

Updated: May 14, 2026

Sedimentation Equilibrium of a Small Oligomer-forming Membrane Protein: Effect of Histidine Protonation on Pentameric Stability

Sedimentation Equilibrium of a Small Oligomer-forming Membrane Protein: Effect of Histidine Protonation on Pentameric Stability

Published on: April 2, 2015

Ester hydrolysis by a histidine-containing cavitein.

Hui Yang¹, John C Sherman

¹Department of Chemistry, University of British Columbia, 2036 Main Mall, Vancouver, BC, Canada V6T 1Z1.

Bioorganic & Medicinal Chemistry Letters

|February 19, 2013

Summary

Template-assembled synthetic proteins (TASP) were explored for catalytic activity. A histidine-containing cavitein demonstrated an 18-fold rate enhancement for ester hydrolysis, showcasing its catalytic potential.

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Sedimentation Equilibrium of a Small Oligomer-forming Membrane Protein: Effect of Histidine Protonation on Pentameric Stability

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Area of Science:

Biochemistry
Protein Engineering
Catalysis

Background:

Investigating artificial enzymes for specific chemical reactions is crucial.
Template-assembled synthetic proteins (TASP) offer a novel scaffold for designing catalytic molecules.

Purpose of the Study:

To explore the catalytic capabilities of a histidine-containing cavitein within a TASP framework.
To determine the efficiency of this synthetic protein in catalyzing ester hydrolysis.

Main Methods:

Construction of a histidine-containing cavitein using the TASP approach.
Assay development to measure ester hydrolysis rates.
Kinetic analysis to quantify catalytic activity.

Main Results:

The histidine-containing cavitein successfully catalyzed ester hydrolysis.
A significant rate enhancement of 18-fold compared to the uncatalyzed reaction was observed.
This indicates effective catalytic function within the synthetic protein structure.

Conclusions:

Histidine-containing caviteins, when assembled using the TASP method, exhibit notable catalytic activity for ester hydrolysis.
This study validates the TASP approach for creating functional synthetic enzymes.
Further research can explore modifications for enhanced catalytic efficiency and substrate specificity.