4-aminobutyrate transaminase
4-aminobutyrate transaminase | |||||||||
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Identifiers | |||||||||
EC number | 2.6.1.19 | ||||||||
CAS number | 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 | ||||||||
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4-aminobutyrate transaminase | |
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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 ⇌{displaystyle 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.
Contents
1 Structural Studies
2 Inhibitors
3 References
4 Further reading
5 External links
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..mw-parser-output cite.citation{font-style:inherit}.mw-parser-output .citation q{quotes:"""""""'""'"}.mw-parser-output .citation .cs1-lock-free a{background:url("//upload.wikimedia.org/wikipedia/commons/thumb/6/65/Lock-green.svg/9px-Lock-green.svg.png")no-repeat;background-position:right .1em center}.mw-parser-output .citation .cs1-lock-limited a,.mw-parser-output .citation .cs1-lock-registration a{background:url("//upload.wikimedia.org/wikipedia/commons/thumb/d/d6/Lock-gray-alt-2.svg/9px-Lock-gray-alt-2.svg.png")no-repeat;background-position:right .1em center}.mw-parser-output .citation .cs1-lock-subscription a{background:url("//upload.wikimedia.org/wikipedia/commons/thumb/a/aa/Lock-red-alt-2.svg/9px-Lock-red-alt-2.svg.png")no-repeat;background-position:right .1em center}.mw-parser-output .cs1-subscription,.mw-parser-output .cs1-registration{color:#555}.mw-parser-output .cs1-subscription span,.mw-parser-output .cs1-registration span{border-bottom:1px dotted;cursor:help}.mw-parser-output .cs1-ws-icon a{background:url("//upload.wikimedia.org/wikipedia/commons/thumb/4/4c/Wikisource-logo.svg/12px-Wikisource-logo.svg.png")no-repeat;background-position:right .1em center}.mw-parser-output code.cs1-code{color:inherit;background:inherit;border:inherit;padding:inherit}.mw-parser-output .cs1-hidden-error{display:none;font-size:100%}.mw-parser-output .cs1-visible-error{font-size:100%}.mw-parser-output .cs1-maint{display:none;color:#33aa33;margin-left:0.3em}.mw-parser-output .cs1-subscription,.mw-parser-output .cs1-registration,.mw-parser-output .cs1-format{font-size:95%}.mw-parser-output .cs1-kern-left,.mw-parser-output .cs1-kern-wl-left{padding-left:0.2em}.mw-parser-output .cs1-kern-right,.mw-parser-output .cs1-kern-wl-right{padding-right:0.2em}
Further reading
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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
Wikimedia Commons has media related to 4-aminobutyrate transaminase. |
4-Aminobutyrate+Transaminase at the US 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
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