In enzymology, 4-aminobutyrate transaminase (), 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 , , , , , , , , and .

Inhibitors

• Aminooxyacetic acid
• Gabaculine
• Phenelzine
• Phenylethylidenehydrazine (PEH)
• Valproic acid
• Vigabatrin

References

External links