Glutamate-1-semialdehyde 2,1-aminomutase
| glutamate-1-semialdehyde 2,1-aminomutase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 2epj, Aeropyrum pernix (Archaea) | |||||||||
| Identifiers | |||||||||
| EC no. | 5.4.3.8 | ||||||||
| CAS no. | 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 | ||||||||
| |||||||||
In enzymology, a glutamate-1-semialdehyde 2,1-aminomutase (EC 5.4.3.8) is an enzyme that catalyzes the chemical reaction
- L-glutamate 1-semialdehyde 5-aminolevulinate
Hence, this enzyme has one substrate, L-glutamate-1-semialdehyde, and one product, 5-aminolevulinate.
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.
Structural studies
[edit]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
[edit]- Gough SP, Kannangara CG (1978). "Biosynthesis of delta-aminolevulinate in greening barley leaves: glutamate 1-semialdehyde aminotransferase". Carlsberg Res. Commun. 43 (3): 185–194. doi:10.1007/BF02914241.
