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Glutamate-1-semialdehyde 2,1-aminomutase

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glutamate-1-semialdehyde 2,1-aminomutase
2epj.jpg
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
Search
PMC articles
PubMed articles
NCBI proteins

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
 
 
 

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. 1 2 Enzyme 5.4.3.8 at KEGG Pathway Database.
  2. Gamini Kannangara, C.; Gough, Simon P. (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, S.I. (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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