4-aminobutyrate transaminase
| 4-aminobutyrate transaminase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 | |||||||||
| Identifiers | |||||||||
| EC no. | 2.6.1.19 | ||||||||
| CAS no. | 9037-67-6 | ||||||||
| 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 | ||||||||
| |||||||||
| 4-aminobutyrate transaminase | |||||||
|---|---|---|---|---|---|---|---|
| Identifiers | |||||||
| Symbol | ABAT | ||||||
| NCBI gene | 18 | ||||||
| HGNC | 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 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
- Aminooxyacetic acid
- Gabaculine
- Phenelzine
- Phenylethylidenehydrazine (PEH)
- Rosmarinic acid[1]
- Valproic acid
- Vigabatrin
References
- ^ Awad R, Muhammad A, Durst T, Trudeau VL, Arnason JT (August 2009). "Bioassay-guided fractionation of lemon balm (Melissa officinalis L.) using an in vitro measure of GABA transaminase activity". Phytotherapy Research. 23 (8): 1075–81. doi:10.1002/ptr.2712. PMID 19165747.
Further reading
- Scott EM, Jakoby WB (April 1959). "Soluble gamma-aminobutyric-glutamic transaminase from Pseudomonas fluorescens". The Journal of Biological Chemistry. 234 (4): 932–6. PMID 13654294.
- Aurich H (October 1961). "[On the beta-alanine-alpha-ketoglutarate transaminase from Neurospora crassa]" [On the beta-alanine-alpha-ketoglutarate transaminase from Neurospora crassa]. Hoppe-Seyler's Zeitschrift für Physiologische Chemie (in German). 326: 25–33. doi:10.1515/bchm2.1961.326.1.25. PMID 13863304.
- Schousboe A, Wu JY, Roberts E (July 1973). "Purification and characterization of the 4-aminobutyrate--2,ketoglutarate transaminase from mouse brain". Biochemistry. 12 (15): 2868–73. doi:10.1021/bi00739a015. PMID 4719123.
- Parviz M, Vogel K, Gibson KM, Pearl PL (November 2014). "Disorders of GABA metabolism: SSADH and GABA-transaminase deficiencies" (PDF). Journal of Pediatric Epilepsy. 3 (4): 217–227. doi:10.3233/PEP-14097. PMC 4256671. PMID 25485164.
External links
- 4-Aminobutyrate+Transaminase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
- Pearl, Phillip L., Parviz, Mahsa, Hodgeman, Ryan, Gibson, K. Michael. GABA-transaminase deficiency. In: Reimschisel T (ed.) MedLink Neurology. San Diego, California: MedLink Corporation. http://medlink.com/article/gaba-transaminase_deficiency
