Glutamate-1-semialdehyde

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| PIN=(4S)-4-Amino-5-oxopentanoic acid

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|Section1={{Chembox Identifiers

| CASNo_Ref = {{cascite|correct|??}}

| CASNo=68462-55-5

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| UNII = 6KX9PX9562

| PubChem=129297

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| ChemSpiderID = 114525

| SMILES = C(CC(=O)O)[C@@H](C=O)N

| InChI = 1/C5H9NO3/c6-4(3-7)1-2-5(8)9/h3-4H,1-2,6H2,(H,8,9)/t4-/m0/s1

| InChIKey = MPUUQNGXJSEWTF-BYPYZUCNBY

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| StdInChI = 1S/C5H9NO3/c6-4(3-7)1-2-5(8)9/h3-4H,1-2,6H2,(H,8,9)/t4-/m0/s1

| StdInChIKey_Ref = {{stdinchicite|changed|chemspider}}

| StdInChIKey = MPUUQNGXJSEWTF-BYPYZUCNSA-N

| MeSHName=glutamate-1-semialdehyde

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|Section2={{Chembox Properties

| C=5 | H=9 | N=1 | O=3

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Glutamate-1-semialdehyde is a molecule formed from by the reduction of tRNA bound glutamate, catalyzed by glutamyl-tRNA reductase. It is isomerized by glutamate-1-semialdehyde 2,1-aminomutase to give aminolevulinic acid in the biosynthesis of porphyrins, including heme and chlorophyll.{{cite journal |author=Beale SI |title=Biosynthesis of the Tetrapyrrole Pigment Precursor, delta-Aminolevulinic Acid, from Glutamate |journal=Plant Physiol. |volume=93 |issue=4 |pages=1273–9 |date=August 1990 |pmid=16667613 |pmc=1062668 |doi=10.1104/pp.93.4.1273}}{{cite book |author=Willows, R.D. |chapter=Chlorophylls |editor=Goodman, Robert M. |title=Encyclopaedia of Plant and Crop Science |publisher=Marcel Dekker |year=2004 |isbn=0-8247-4268-0 |pages=258–262}}

See also

References

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{{Amino acid metabolism intermediates}}

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Category:Aldehydes

Category:Gamma-Amino acids