4-aminobutyrate transaminase

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4-aminobutyrate transaminase
1ohv.jpg
Identifiers
EC number 2.6.1.19
CAS number Template:CAS
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
4-aminobutyrate transaminase
Identifiers
Symbol ABAT
Entrez 18
HUGO 23
OMIM 137150
RefSeq NM_020686
UniProt P80404
Other data
Locus Chr. 16 p13.2

In enzymology, 4-aminobutyrate transaminase (EC 2.6.1.19), also called GABA transaminase or 4-aminobutyrate aminotransferase, is an enzyme that catalyzes the chemical reaction:

4-aminobutanoate + 2-oxoglutarate \rightleftharpoons succinate semialdehyde + L-glutamate

Thus, the two substrates of this enzyme are 4-aminobutanoate (GABA) and 2-oxoglutarate. The two products are succinate semialdehyde and L-glutamate.

This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is 4-aminobutanoate:2-oxoglutarate aminotransferase. This enzyme participates in 5 metabolic pathways: alanine and aspartate metabolism, glutamate metabolism, beta-alanine metabolism, propanoate metabolism, and butanoate metabolism. It employs one cofactor, pyridoxal phosphate.

Structural Studies

As of late 2007, 9 structures have been solved for this class of enzymes, with PDB accession codes 1OHV, 1OHW, 1OHY, 1SF2, 1SFF, 1SZK, 1SZS, 1SZU, and 2EO5.

Inhibitors

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References

  1. Bioassay-guided fractionation of lemon balm (Melissa officinalis L.) using an in vitro measure of GABA transaminase activity. Awad R, Muhammad A, Durst T, Trudeau VL and Arnason JT, Phytother Res., August 2009, volume 23, issue 8, pages 1075-1081, doi:10.1002/ptr.2712
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External links