Related Experiment Video
Updated: Sep 30, 2025

05:57
Author Spotlight: In Silico Creation and Impact of Carbonylated Amino Acids on Protein Structure and Function
Published on: April 26, 2024
539
Carbon Dioxide and the Carbamate Post-Translational Modification
Lynsay I Blake1, Martin J Cann1
1Department of Biosciences, Durham University, Durham, United Kingdom.
Frontiers in Molecular Biosciences
|March 18, 2022
Summary
Carbon dioxide (CO2) is vital for life, regulating cellular processes. This study explores CO2
Area of Science:
- Biochemistry
- Cell Biology
- Physiology
Background:
- Carbon dioxide (CO2) is fundamental to life, acting as a substrate in photosynthesis and a product of decay.
- CO2 influences diverse biological processes, including cellular reactions, transport, environmental maintenance, and behavior.
- Despite its importance, direct cellular interactions of CO2 remain poorly understood.
Purpose of the Study:
- To investigate the direct interactions between carbon dioxide and cellular components.
- To elucidate the role of carbamate post-translational modifications in protein function and signaling.
- To review known protein carbamates and emerging techniques for their study.
Main Methods:
- Review of existing literature on protein carbamates.
- Description of the chemical mechanism of carbamate formation via CO2 nucleophilic attack.
- Discussion of novel techniques for isolating and studying carbamate modifications.
Main Results:
- Carbamate formation is a key mechanism by which CO2 can alter protein function.
- CO2 modification of N-terminal or lysine amino groups can impact protein activity.
- Recent advancements offer new ways to detect and analyze these modifications.
Conclusions:
- Carbon dioxide directly influences cellular function through post-translational modifications like carbamylation.
- Understanding carbamate formation is crucial for comprehending CO2 sensing and signaling pathways.
- Further research into these modifications is essential for fields like crop science, public health, and disease vector research.
Related Concept Videos
Covalently Linked Protein Regulators
7.6K
Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein....
These groups modify specific amino acids in a protein....
7.6K
Loss of Carboxy Group as CO2: Decarboxylation of β-Ketoacids
3.3K
Carboxylic acids, upon heating, undergo a decarboxylation reaction by releasing carbon dioxide gas. Monocarboxylic acids do not undergo decarboxylation easily. However, a silver salt of carboxylic acid reacts with bromine or iodine under high temperature to release carbon dioxide gas and forms halide with one less carbon. This reaction is called the Hunsdiecker reaction.
3.3K
Protein Glycosylation
7.5K
Glycosylation, the most common post-translational modification for proteins, serves diverse functions. Adding sugars to proteins makes the proteins more resistant to proteolytic digestion. Glycosylated proteins can act as markers and receptors to promote cell-cell adhesion. Additionally, they have many essential quality control functions in the cell, such as correct protein folding and facilitating transport of misfolded proteins to the cytosol, which can be degraded.
Glycosylation occurs in...
Glycosylation occurs in...
7.5K
Protein Modifications in the RER
5.7K
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...
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...
5.7K
Loss of Carboxy Group as CO2: Decarboxylation of Malonic Acid Derivatives
2.1K
Just like β-keto acids—which upon thermal decarboxylation form ketones—β-dicarboxylic acids undergo decarboxylation to generate monocarboxylic acids with the liberation of carbon dioxide.
2.1K
Carbocations
11.9K
Carbocations are one of the reaction intermediates formed during several nucleophilic substitutions or elimination reactions. A carbocation is an electron-deficient species with the central carbon atom having six electrons and three bonded atoms. The central carbon in a carbocation is sp2 hybridized with trigonal planar geometry. It has an empty p orbital perpendicular to the plane of the structure that can accept electrons. Thus, carbocations act as strong electrophiles and may react with any...
11.9K

