Glutamate-1-semialdehyde: Difference between revisions

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'''Glutamate-1-semialdehyde''' (GSA), also known as '''5-aminolevulinate synthase''', is a key [[enzyme]] in the [[biosynthesis]] of [[chlorophyll]] and [[heme]]. It is involved in the conversion of [[glutamate]] to [[delta-aminolevulinic acid]] (ALA), the first step in the biosynthesis of these important biological molecules.


== Structure ==
{{Short description|Overview of Glutamate-1-semialdehyde}}
{{Chembox
| Name = Glutamate-1-semialdehyde
| ImageFile = <!-- Image file name -->
| ImageSize = 200px
| IUPACName = 2-Amino-5-oxopentanoic acid
| OtherNames = Glutamate semialdehyde
| Section1 = {{Chembox Identifiers
  | CASNo = 35376-70-0
  | PubChem = 439409
  | ChemSpiderID = 388454
  }}
| Section2 = {{Chembox Properties
  | Formula = C<sub>5</sub>H<sub>9</sub>NO<sub>3</sub>
  | MolarMass = 131.13 g/mol
  }}
}}


The structure of GSA is complex, with multiple [[subunit]]s and [[cofactor]]s. The enzyme is a [[dimer]], with each subunit containing a [[pyridoxal phosphate]] (PLP) cofactor. The PLP is essential for the enzyme's activity, as it forms a [[Schiff base]] with the glutamate substrate, facilitating its conversion to ALA.
'''Glutamate-1-semialdehyde''' is an important intermediate in the biosynthesis of [[porphyrins]] and [[chlorophyll]]. It is a derivative of [[glutamic acid]] and plays a crucial role in the [[C5 pathway]] of [[tetrapyrrole]] synthesis.


[[File:Glutamate-1-semialdehyde_structure.png|thumb|right|300px|Structure of Glutamate-1-semialdehyde]]
== Biosynthesis ==
Glutamate-1-semialdehyde is synthesized from [[glutamyl-tRNA]] by the enzyme [[glutamyl-tRNA reductase]]. This reaction is a key step in the conversion of [[glutamate]] to [[5-aminolevulinic acid]] (ALA), which is the first common precursor in the biosynthesis of all tetrapyrroles, including [[heme]], [[chlorophyll]], and [[vitamin B12]].


== Function ==
== Function ==
In the [[C5 pathway]], glutamate-1-semialdehyde is converted to [[5-aminolevulinic acid]] by the enzyme [[glutamate-1-semialdehyde aminotransferase]]. This conversion is essential for the production of [[porphyrin]] rings, which are the building blocks of many important biological molecules.


GSA catalyzes the conversion of glutamate to ALA in a two-step reaction. First, the enzyme binds to glutamate and the PLP cofactor, forming a Schiff base. This is then converted to an intermediate, glutamate-1-semialdehyde, through a process known as [[transamination]]. The GSA is then converted to ALA through a [[decarboxylation]] reaction.
== Clinical Significance ==
Disruptions in the biosynthesis of glutamate-1-semialdehyde can lead to disorders in [[heme]] production, such as [[porphyria]]. Understanding the role of glutamate-1-semialdehyde in these pathways can help in the development of treatments for such conditions.


== Role in Disease ==
== See also ==
* [[Porphyrin synthesis]]
* [[Chlorophyll biosynthesis]]
* [[Tetrapyrrole]]


Mutations in the gene encoding GSA can lead to a variety of diseases. For example, defects in GSA are associated with [[porphyria]], a group of rare genetic disorders that affect the nervous system and skin. In addition, GSA has been implicated in the development of certain types of [[cancer]], as it is involved in the biosynthesis of heme, a molecule essential for the function of many proteins, including those involved in [[cell division]] and [[DNA repair]].
== References ==
 
<references />
== See Also ==
 
* [[Glutamate]]
* [[Delta-aminolevulinic acid]]
* [[Biosynthesis]]
* [[Enzyme]]
* [[Porphyria]]
* [[Cancer]]


[[Category:Biochemistry]]
[[Category:Biochemistry]]
[[Category:Enzymes]]
[[Category:Metabolism]]
[[Category:Metabolism]]
[[Category:Medicine]]
[[Category:Organic compounds]]
 
[[Category:Tetrapyrrole biosynthesis]]
{{biochemistry-stub}}
<gallery>
{{medicine-stub}}
File:Glutamate-1-semialdehyde.svg|Glutamate-1-semialdehyde
</gallery>

Latest revision as of 05:21, 3 March 2025


Overview of Glutamate-1-semialdehyde


Chemical Compound
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References

Glutamate-1-semialdehyde is an important intermediate in the biosynthesis of porphyrins and chlorophyll. It is a derivative of glutamic acid and plays a crucial role in the C5 pathway of tetrapyrrole synthesis.

Biosynthesis[edit]

Glutamate-1-semialdehyde is synthesized from glutamyl-tRNA by the enzyme glutamyl-tRNA reductase. This reaction is a key step in the conversion of glutamate to 5-aminolevulinic acid (ALA), which is the first common precursor in the biosynthesis of all tetrapyrroles, including heme, chlorophyll, and vitamin B12.

Function[edit]

In the C5 pathway, glutamate-1-semialdehyde is converted to 5-aminolevulinic acid by the enzyme glutamate-1-semialdehyde aminotransferase. This conversion is essential for the production of porphyrin rings, which are the building blocks of many important biological molecules.

Clinical Significance[edit]

Disruptions in the biosynthesis of glutamate-1-semialdehyde can lead to disorders in heme production, such as porphyria. Understanding the role of glutamate-1-semialdehyde in these pathways can help in the development of treatments for such conditions.

See also[edit]

References[edit]

<references />

  • Glutamate-1-semialdehyde
    Glutamate-1-semialdehyde
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