Wikipedia

Glutamate-1-semialdehyde 2,1-aminomutase

In enzymology, glutamate-1-semialdehyde 2,1-aminomutase (EC 5.4.3.8) is an enzyme that catalyzes the chemical reaction

glutamate-1-semialdehyde 2,1-aminomutase
2epj, Aeropyrum pernix (Archaea)
Identifiers
EC no.5.4.3.8
CAS no.68518-07-0
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

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

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As of late 2007, 10 structures have been solved for this class of enzymes, with PDB accession codes PDB: 2CFB​, PDB: 2E7U​, PDB: 2EPJ​, PDB: 2GSA​, PDB: 2HOY​, PDB: 2HOZ​, PDB: 2HP1​, PDB: 2HP2​, PDB: 3GSB​, and PDB: 4GSA​.

References

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  1. 1 2 Enzyme 5.4.3.8 at KEGG Pathway Database.
  2. ↑ Gamini Kannangara C, Gough SP (1978). "Biosynthesis of Δ-aminolevulinate in greening barley leaves: Glutamate 1-semialdehyde aminotransferase". Carlsberg Research Communications. 43 (3): 185–194. doi:10.1007/BF02914241.
  3. ↑ Beale SI (August 1990). "Biosynthesis of the Tetrapyrrole Pigment Precursor, delta-Aminolevulinic Acid, from Glutamate". Plant Physiology. 93 (4): 1273–1279. doi:10.1104/pp.93.4.1273. PMC 1062668. PMID 16667613.
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