4-aminobutyrate transaminase

4-aminobutyrate transaminase
4-Aminobutyrate transaminase homodimer, Pig
Identifiers
EC no.2.6.1.19
CAS no.9037-67-6
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins
4-aminobutyrate transaminase
Identifiers
SymbolABAT
NCBI gene18
HGNC23
OMIM137150
RefSeqNM_020686
UniProtP80404
Other data
LocusChr. 16 p13.2
Search for
StructuresSwiss-model
DomainsInterPro

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

4-aminobutanoate + 2-oxoglutarate 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.

This enzyme is found in prokaryotes, plants, fungi, and animals (including humans).[1] Pigs have often been used when studying how this protein may work in humans.[2]

  1. ^ "4-aminobutyrate aminotransferase - Identical Protein Groups - NCBI". www.ncbi.nlm.nih.gov. Retrieved 2020-09-29.
  2. ^ Iftikhar H, Batool S, Deep A, Narasimhan B, Sharma PC, Malhotra M (February 2017). "In silico analysis of the inhibitory activities of GABA derivatives on 4-aminobutyrate transaminase". Arabian Journal of Chemistry. 10: S1267–75. doi:10.1016/j.arabjc.2013.03.007.