Glutamate-1-semialdehyde 2,1-aminomutase
| glutamate-1-semialdehyde 2,1-aminomutase | |||||||||
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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 / EGO | ||||||||
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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
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
- 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.