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

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.


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