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Related Concept Videos

E2 Reaction: Kinetics and Mechanism02:45

E2 Reaction: Kinetics and Mechanism

SN2 substitutions and E2 eliminations of alkyl halides proceed via a concerted pathway. While the nucleophile attacks the alpha carbon in SN2 reactions, it functions as a strong base and abstracts a beta hydrogen in the E2 mechanism. The rate-limiting transition state in E2 elimination reactions is characterized by partially broken carbon–hydrogen and carbon–halogen bonds and a partially formed pi bond between the alpha and beta carbons. The beta hydrogen and halide are eliminated...
E2 Reaction: Stereochemistry and Regiochemistry02:43

E2 Reaction: Stereochemistry and Regiochemistry

Elimination reactions of alkyl halides can yield one or more alkenes depending on the specific regiochemical and stereochemical considerations. While the regiochemistry of the reaction governs the location of the double bond in the product, the stereochemical requirements often influence the geometry.
When a substrate with two different β hydrogens undergoes an E2 elimination, the presence of a strong base can yield two regioisomeric alkenes. The more-substituted alkene is the major product and...
Structure and Function of Erythrocytes01:29

Structure and Function of Erythrocytes

There are between 4.2 and 6 million erythrocytes, also known as red blood cells, in every microliter of blood. These cells are small, flattened biconcave discs with centers that are depressed.
The erythrocyte plasma membrane is associated with proteins such as spectrin, which forms a flexible cytoplasmic meshwork. This meshwork allows erythrocytes to twist, turn, become cup-shaped, and regain their biconcave shape as they pass through narrow capillaries. Additionally, erythrocytes can form...
E1 Reaction: Stereochemistry and Regiochemistry02:43

E1 Reaction: Stereochemistry and Regiochemistry

One of the critical aspects of the E1 reaction mechanism, as also observed in E2, is the regiochemistry, with multiple regioisomers obtained as products. In the example discussed, the presence of water as a weak base favors elimination over substitution to generate two alkenes. Given that alkenes’ stability increases with the number of alkyl groups across the double bond, typically, E1 reactions lead to the Zaitsev product, for this is more substituted and stable than the Hofmann product.
The Endoplasmic Reticulum01:43

The Endoplasmic Reticulum

The endoplasmic reticulum or ER makes up for more than half of the membranes in a cell and accounts for 10% of total cell volume. It is also the primary protein and lipid synthesis factory for most cell organelles, such as the Golgi apparatus, lysosomes, secretory vesicles, and the plasma membrane. Despite being the most extensive and functionally complex subcellular organelle, ER was the last to be discovered. After years of deliberation, Keith Porter and George Palade in the year 1954,...
Compounds Essential to Human Function01:25

Compounds Essential to Human Function

The human body is composed of cells that are fundamentally made up of several different molecules. These molecules are essential to carry out all physiological processes in the body and are broadly classified into organic and inorganic based on their chemical structures.
Inorganic Compounds Essential to Human Functioning
Inorganic compounds essential to human functioning include water, salts, acids, and bases. These compounds are inorganic, i.e., they do not have a carbon-hydrogen bond. Water...

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Translating Extracellular Electron Transfer Activities with Organic Electrochemical Transistors
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Published on: January 31, 2025

E2s: structurally economical and functionally replete.

Dawn M Wenzel1, Kate E Stoll, Rachel E Klevit

  • 1Department of Biochemistry, University of Washington, Box 357350, Seattle, WA 98195-97350, USA.

The Biochemical Journal
|December 17, 2010
PubMed
Summary
This summary is machine-generated.

Ubiquitin conjugation involves E1, E2, and E3 enzymes. This review details ubiquitin-conjugating (E2) enzyme interactions, their structural diversity, and roles in cellular signaling and disease.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cellular Biology

Background:

  • Ubiquitination is a crucial post-translational modification regulating cellular processes and implicated in diseases.
  • The ubiquitin transfer cascade involves ubiquitin-activating (E1), ubiquitin-conjugating (E2), and ubiquitin ligase (E3) enzymes.
  • E2 enzymes are central to ubiquitin signaling, dictating E3 selection and substrate modification, thus driving signaling diversity.

Purpose of the Study:

  • To review the structural and functional aspects of ubiquitin-conjugating (E2) enzymes.
  • To discuss the E2-E3 interface, methods for identifying E2-E3 partners, and non-canonical E2 interactions.
  • To analyze the structural basis of E2~Ub species and their mechanistic implications in ubiquitin transfer.

Main Methods:

  • Structural analysis of over 90 E2 enzyme three-dimensional structures.
  • Review of literature on E2-E3 interactions and ubiquitin transfer mechanisms.
  • Comparative analysis of conjugated E2~Ub species structures.

Main Results:

  • E2 enzymes exhibit diverse protein interactions across their catalytic domain surfaces.
  • Structural data reveals how E2s are recognized by various protein partners.
  • Non-canonical E2-protein interactions expand the understanding of E2 enzyme function.
  • Comparison of E2~Ub species provides mechanistic insights into ubiquitin transfer.

Conclusions:

  • E2 enzymes are versatile hubs for protein-protein interactions, essential for diverse ubiquitin signaling.
  • Structural insights into E2-E3 complexes and E2~Ub intermediates are key to understanding ubiquitination.
  • Further research into E2 interactions can elucidate their roles in cellular regulation and disease pathogenesis.