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Related Concept Videos

Preparation and Reactions of Thiols02:33

Preparation and Reactions of Thiols

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Thiols are prepared using the hydrosulfide anion as a nucleophile in a nucleophilic substitution reaction with alkyl halides. For instance, bromobutane reacts with sodium hydrosulfide to give butanethiol.
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Structure and Nomenclature of Thiols and Sulfides02:17

Structure and Nomenclature of Thiols and Sulfides

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Thiols and sulfides are sulfur analogs of alcohols and ethers, respectively, where the sulfur atom takes the place of the oxygen atom. Thus, thiols are generally represented as RSH, where R is an alkyl substituent and —SH is the functional group. On the other hand, in sulfides, the central sulfur atom is bonded to two hydrocarbon groups on either side. Depending upon the type of group, sulfides can be either symmetrical or asymmetrical. Both thiols and sulfides display a bent geometry,...
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Cholinesterases: Distribution and Function01:22

Cholinesterases: Distribution and Function

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Cholinesterases are a group of serine hydrolase enzymes that play a crucial role in the breakdown of choline esters. The two primary types of cholinesterases are acetylcholinesterases (AChEs) and butyrylcholinesterase (BuChEs), which differ in their distribution, function, and substrate specificity. AChEs, also known as true cholinesterases, specifically hydrolyze acetylcholine, while BuChEs, often referred to as pseudocholinesterases, can hydrolyze various choline esters, including...
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Acetals and Thioacetals as Protecting Groups for Aldehydes and Ketones01:24

Acetals and Thioacetals as Protecting Groups for Aldehydes and Ketones

5.5K
Acetals are formed by reacting two equivalents of alcohol with carbonyl compounds like aldehydes or ketones. Acetals are unaffected by bases, nucleophiles, oxidizing agents, and reducing agents. They serve as protecting groups for aldehydes and ketones. Acetals can be easily formed and also easily removed via mild acid hydrolysis.
In the presence of multiple functional groups, when selective reduction of one group over the other is desired, groups like aldehydes and ketones that form acetals...
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Protein Modifications in the RER01:26

Protein Modifications in the RER

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Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal...
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Regulated Protein Degradation02:58

Regulated Protein Degradation

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It is vital to regulate the activity of enzymatic as well as non-enzymatic proteins inside the cell. This can be achieved either through creating a balance between their rate of synthesis and degradation or regulating the intrinsic activity of the protein. Both these regulation mechanisms play an essential role in the normal functioning of cells.
Protein degradation plays two important roles in the cells. It helps to protect cells from misfolded or damaged proteins before they lead to a...
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Updated: Dec 21, 2025

Synthesis of a Thiol Building Block for the Crystallization of a Semiconducting Gyroidal Metal-sulfur Framework
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Synthesis of a Thiol Building Block for the Crystallization of a Semiconducting Gyroidal Metal-sulfur Framework

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Structure, function, and regulation of thioesterases.

Crystall M D Swarbrick1, Jeffrey D Nanson2, Edward I Patterson3

  • 1Institute for Glycomics, Griffith University, Southport, Queensland 4222, Australia.

Progress in Lipid Research
|May 17, 2020
PubMed
Summary
This summary is machine-generated.

Thioesterases, crucial enzymes in all cells, are newly understood through structural and functional studies. These studies reveal novel regulatory mechanisms, including ATP/GDP control and conserved structures in the TE4 family.

Keywords:
Coenzyme AFatty acyl-CoAHotdog domainHydrolaseRegulationThioesterase

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Area of Science:

  • Biochemistry
  • Enzymology
  • Molecular Biology

Background:

  • Thioesterases are ubiquitous enzymes catalyzing thioester bond hydrolysis in diverse cellular substrates.
  • They are classified into 25 families based on structural and functional characteristics.
  • Recent advancements have significantly impacted the understanding of thioesterase regulation and cellular roles.

Purpose of the Study:

  • To provide a comprehensive overview of current knowledge on thioesterase structure, function, and regulation.
  • To highlight recent discoveries and dogma shifts in the field.
  • To compare and contrast different thioesterase families.

Main Methods:

  • Review of recent structural and functional characterization studies.
  • Comparative analysis of thioesterase families.
  • Integration of data on enzyme regulation and substrate specificity.

Main Results:

  • Elucidation of ATP and GDP-mediated regulation through oligomerization.
  • Identification of novel key regulatory regions within thioesterases.
  • Discovery of conserved quaternary structures in the TE4 family.

Conclusions:

  • Recent research has reshaped the understanding of thioesterase regulation.
  • New insights into enzyme mechanisms and conserved structural features offer avenues for future research.
  • This review consolidates current knowledge across diverse thioesterase families.