4-aminobutyrate transaminase

4-aminobutyrate transaminase
4-aminobutyrate transaminase
Identifiers EC number CAS number 2.6.1.19 [1] [2]

9037-67-6

Databases IntEnz BRENDA ExPASy KEGG MetaCyc PRIAM PDB structures Gene Ontology IntEnz view [3] [4] [5]

BRENDA entry NiceZyme view KEGG entry [6]

metabolic pathway profile [8] [9]

[7]

RCSB PDB AmiGO

PDBe

[10]

PDBsum

[11]

[12]

/ EGO

[13]

Search PMC articles [14]

PubMed articles [15] NCBI proteins [16]

4-aminobutyrate transaminase
Identifiers Symbol Entrez HUGO OMIM RefSeq UniProt ABAT 18 23 [17] [18] [19] [20]

137150

NM_020686 P80404 Other data [21]

Locus

Chr. 16 p13.2

[22]

In enzymology, 4-aminobutyrate transaminase (EC 2.6.1.19 [23]), also called GABA transaminase or 4-aminobutyrate aminotransferase, is an enzyme that catalyzes the chemical reaction: 4-aminobutanoate + 2-oxoglutarate succinate semialdehyde + L-glutamate

4-aminobutyrate transaminase 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 [25], 1OHY [26], 1SF2 [27], 1SFF [28], 1SZK [29], 1SZS [30], 1SZU [31], and 2EO5 [32].
[24]

Inhibitors
Aminooxyacetic acid Gabaculine Phenelzine Phenylethylidenehydrazine (PEH)

Rosmarinic acid[33] Valproic acid Vigabatrin

References
[1] [2] [3] [4] [5] [6] [7] [8] [9] http:/ / www. chem. qmul. ac. uk/ iubmb/ enzyme/ EC2/ 6/ 1/ 19. html http:/ / tools. wmflabs. org/ magnustools/ cas. php?language=en& cas=9037-67-6& title= http:/ / www. ebi. ac. uk/ intenz/ query?cmd=SearchEC& ec=2. 6. 1. 19 http:/ / www. brenda-enzymes. org/ php/ result_flat. php4?ecno=2. 6. 1. 19 http:/ / www. expasy. org/ enzyme/ 2. 6. 1. 19 http:/ / www. genome. ad. jp/ dbget-bin/ www_bget?enzyme+ 2. 6. 1. 19 http:/ / biocyc. org/ META/ substring-search?type=NIL& object=2. 6. 1. 19 http:/ / priam. prabi. fr/ cgi-bin/ PRIAM_profiles_CurrentRelease. pl?EC=2. 6. 1. 19 http:/ / www. rcsb. org/ pdb/ search/ smartSubquery. do?smartSearchSubtype=EnzymeClassificationQuery& Enzyme_Classification=2. 6. 1. 19 [10] http:/ / www. ebi. ac. uk/ pdbe-srv/ PDBeXplore/ enzyme/ ?ec=2. 6. 1. 19 [11] http:/ / www. ebi. ac. uk/ thornton-srv/ databases/ cgi-bin/ enzymes/ GetPage. pl?ec_number=2. 6. 1. 19 [12] http:/ / amigo. geneontology. org/ cgi-bin/ amigo/ go. cgi?query=GO:0003867& view=details [13] http:/ / www. ebi. ac. uk/ ego/ DisplayGoTerm?id=GO:0003867& format=normal [14] http:/ / www. ncbi. nlm. nih. gov/ entrez/ query. fcgi?db=pubmed& term=2. 6. 1. 19%5BEC/ RN%20Number%5D%20AND%20pubmed%20pmc%20local%5Bsb%5D [15] http:/ / www. ncbi. nlm. nih. gov/ entrez/ query. fcgi?db=pubmed& term=2. 6. 1. 19%5BEC/ RN%20Number%5D [16] http:/ / www. ncbi. nlm. nih. gov/ protein?term=2. 6. 1. 19%5BEC/ RN%20Number%5D [17] http:/ / www. ncbi. nlm. nih. gov/ entrez/ query. fcgi?db=gene& amp;cmd=retrieve& amp;dopt=default& amp;list_uids=18& rn=1 [18] http:/ / www. genenames. org/ data/ hgnc_data. php?hgnc_id=23 [19] http:/ / www. omim. org/ 137150 [20] http:/ / genome. ucsc. edu/ cgi-bin/ hgTracks?Submit=Submit& position=NM_020686& rn=1 [21] http:/ / www. uniprot. org/ uniprot/ P80404 [22] http:/ / omim. org/ search?index=geneMap& search=16p13. 2 [23] http:/ / enzyme. expasy. org/ EC/ 2. 6. 1. 19 [24] http:/ / www. ebi. ac. uk/ thornton-srv/ databases/ cgi-bin/ pdbsum/ GetPage. pl?pdbcode=1OHV [25] http:/ / www. ebi. ac. uk/ thornton-srv/ databases/ cgi-bin/ pdbsum/ GetPage. pl?pdbcode=1OHW [26] http:/ / www. ebi. ac. uk/ thornton-srv/ databases/ cgi-bin/ pdbsum/ GetPage. pl?pdbcode=1OHY [27] http:/ / www. ebi. ac. uk/ thornton-srv/ databases/ cgi-bin/ pdbsum/ GetPage. pl?pdbcode=1SF2 [28] http:/ / www. ebi. ac. uk/ thornton-srv/ databases/ cgi-bin/ pdbsum/ GetPage. pl?pdbcode=1SFF [29] http:/ / www. ebi. ac. uk/ thornton-srv/ databases/ cgi-bin/ pdbsum/ GetPage. pl?pdbcode=1SZK

4-aminobutyrate transaminase
[30] http:/ / www. ebi. ac. uk/ thornton-srv/ databases/ cgi-bin/ pdbsum/ GetPage. pl?pdbcode=1SZS [31] http:/ / www. ebi. ac. uk/ thornton-srv/ databases/ cgi-bin/ pdbsum/ GetPage. pl?pdbcode=1SZU [32] http:/ / www. ebi. ac. uk/ thornton-srv/ databases/ cgi-bin/ pdbsum/ GetPage. pl?pdbcode=2EO5 [33] 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,

Scott EM, Jakoby WB (1959). "Soluble gamma-aminobutyric-glutamic transaminase from Pseudomonas fluorescens". J. Biol. Chem. 234 (4): 932936. PMID 13654294 (http://www.ncbi.nlm.nih.gov/pubmed/ 13654294). Aurich H (1961). "Ueber die beta-Alanin-alpha-Ketoglutarat-Transaminase aus Neurospora crassa". Hoppe-Seyler's Z. Physiol. Chem. 326: 2533. Schousboe A, Wu JY, Roberts E (1973). "Purification and characterization of the 4-aminobutyrate:2-ketoglutarate transaminase from mouse brain". Biochemistry 12 (15): 286873. doi: 10.1021/bi00739a015 (http://dx.doi.org/ 10.1021/bi00739a015). PMID 4719123 (http://www.ncbi.nlm.nih.gov/pubmed/4719123).

External links
4-Aminobutyrate Transaminase (http://www.nlm.nih.gov/cgi/mesh/2011/MB_cgi?mode=& term=4-Aminobutyrate+Transaminase) at the US National Library of Medicine Medical Subject Headings (MeSH)

Article Sources and Contributors

Article Sources and Contributors

4-aminobutyrate transaminase Source: http://en.wikipedia.org/w/index.php?oldid=562213483 Contributors: AndrewJD, Arcadian, Fuse809, Neonfuzz, Nikkimaria, NotWith, Pts925, WillowW

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