Biology:Glutamate-1-semialdehyde 2,1-aminomutase
| glutamate-1-semialdehyde 2,1-aminomutase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 2epj, Aeropyrum pernix (Archaea) | |||||||||
| Identifiers | |||||||||
| EC number | 5.4.3.8 | ||||||||
| CAS number | 68518-07-0 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
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In enzymology, glutamate-1-semialdehyde 2,1-aminomutase (EC 5.4.3.8) is an enzyme that catalyzes the chemical reaction
- REDIRECT Template:Chemical reaction
The enzyme converts its substrate, glutamate-1-semialdehyde into aminolevulinic acid.[1][2][3]
This enzyme belongs to the family of isomerases, specifically those intramolecular transferases transferring amino groups. The systematic name of this enzyme class is (S)-4-amino-5-oxopentanoate 4,5-aminomutase. This enzyme is also called glutamate-1-semialdehyde aminotransferase. This enzyme participates in porphyrin and chlorophyll biosynthesis. It employs one cofactor, pyridoxal phosphate.[1]
Structural studies
As of late 2007, 10 structures have been solved for this class of enzymes, with PDB accession codes 2CFB, 2E7U, 2EPJ, 2GSA, 2HOY, 2HOZ, 2HP1, 2HP2, 3GSB, and 4GSA.
References
- ↑ 1.0 1.1 Enzyme 5.4.3.8 at KEGG Pathway Database.
- ↑ "Biosynthesis of Δ-aminolevulinate in greening barley leaves: Glutamate 1-semialdehyde aminotransferase". Carlsberg Research Communications 43 (3): 185–194. 1978. doi:10.1007/BF02914241.
- ↑ "Biosynthesis of the Tetrapyrrole Pigment Precursor, delta-Aminolevulinic Acid, from Glutamate". Plant Physiology 93 (4): 1273–1279. August 1990. doi:10.1104/pp.93.4.1273. PMID 16667613.
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