Sandbox Reserved 951
From Proteopedia
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=== The different reactions=== | === The different reactions=== | ||
| - | ====Light emission==== | + | =====Light emission===== |
The most known reaction of luciferase is the light emission. In this reaction, luciferase firstly synthetized luciferin-AMP from luciferin and ATP, using a Mg2+ ion to offset the negative charges of the phosphate groups. Then, luciferase turns the luciferin-AMP into oxyluciferin in an excited state thanks to a dioxygen. This step releases AMP and CO2. The excited oxyluciferin relaxes and looses a photon so light is emitted. | The most known reaction of luciferase is the light emission. In this reaction, luciferase firstly synthetized luciferin-AMP from luciferin and ATP, using a Mg2+ ion to offset the negative charges of the phosphate groups. Then, luciferase turns the luciferin-AMP into oxyluciferin in an excited state thanks to a dioxygen. This step releases AMP and CO2. The excited oxyluciferin relaxes and looses a photon so light is emitted. | ||
The wavelength of the light can vary with the pH : at the physiological pH, the emitted light is green and at a lower pH, the color is red. | The wavelength of the light can vary with the pH : at the physiological pH, the emitted light is green and at a lower pH, the color is red. | ||
| - | ====Fatty-acyl-CoA synthesis==== | + | =====Fatty-acyl-CoA synthesis===== |
This reaction uses the luciferin-AMP which is created at the first step of light emission. But then, CoA-SH attacks the oxygen of the carboxylic group to form fatty-acyl-CoA and releases AMP. | This reaction uses the luciferin-AMP which is created at the first step of light emission. But then, CoA-SH attacks the oxygen of the carboxylic group to form fatty-acyl-CoA and releases AMP. | ||
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| + | ===Interactions with ligands=== | ||
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| + | The active site is not strictly highlighted according to the actual state of studies but some residues and motifs strongly modified have been determined and this conformation enables to find the active site. Many of these conserved residue are located on the core of the β-barrel and on the small C-terminal domain and in the surface of the N-terminal domain. They follow a depression caused by of the β sheet against the β-barrel. | ||
== Evolution == | == Evolution == | ||
Revision as of 23:36, 7 January 2015
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Contents |
Introduction
Biological role
Global Structure
Function highlighted with structure
The different reactions
Light emission
The most known reaction of luciferase is the light emission. In this reaction, luciferase firstly synthetized luciferin-AMP from luciferin and ATP, using a Mg2+ ion to offset the negative charges of the phosphate groups. Then, luciferase turns the luciferin-AMP into oxyluciferin in an excited state thanks to a dioxygen. This step releases AMP and CO2. The excited oxyluciferin relaxes and looses a photon so light is emitted. The wavelength of the light can vary with the pH : at the physiological pH, the emitted light is green and at a lower pH, the color is red.
Fatty-acyl-CoA synthesis
This reaction uses the luciferin-AMP which is created at the first step of light emission. But then, CoA-SH attacks the oxygen of the carboxylic group to form fatty-acyl-CoA and releases AMP.
Interactions with ligands
The active site is not strictly highlighted according to the actual state of studies but some residues and motifs strongly modified have been determined and this conformation enables to find the active site. Many of these conserved residue are located on the core of the β-barrel and on the small C-terminal domain and in the surface of the N-terminal domain. They follow a depression caused by of the β sheet against the β-barrel.
Evolution
This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
</StructureSection>
