Glutamate-1-semialdehyde
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Names | |
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IUPAC name
(4S)-4-Amino-5-oxo-pentanoic acid | |
Identifiers | |
68462-55-5 ![]() | |
3D model (Jmol) | Interactive image |
ChemSpider | 114525 ![]() |
MeSH | glutamate-1-semialdehyde |
PubChem | 129297 |
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Properties | |
C5H9NO3 | |
Molar mass | 131.13 g·mol−1 |
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa). | |
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Infobox references | |
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.[1][2]
See also
References
- ↑ Beale SI (August 1990). "Biosynthesis of the Tetrapyrrole Pigment Precursor, delta-Aminolevulinic Acid, from Glutamate". Plant Physiol. 93 (4): 1273–9. doi:10.1104/pp.93.4.1273. PMC 1062668
. PMID 16667613.
- ↑ Willows, R.D. (2004). "Chlorophylls". In Goodman, Robert M. Encyclopaedia of Plant and Crop Science. Marcel Dekker. pp. 258–262. ISBN 0-8247-4268-0.
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