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| | <StructureSection load='5eun' size='340' side='right'caption='[[5eun]], [[Resolution|resolution]] 1.82Å' scene=''> | | <StructureSection load='5eun' size='340' side='right'caption='[[5eun]], [[Resolution|resolution]] 1.82Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5eun]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EUN OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5EUN FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5eun]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EUN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5EUN FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.825Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AADAT, KAT2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5eun FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5eun OCA], [http://pdbe.org/5eun PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5eun RCSB], [http://www.ebi.ac.uk/pdbsum/5eun PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5eun ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5eun FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5eun OCA], [https://pdbe.org/5eun PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5eun RCSB], [https://www.ebi.ac.uk/pdbsum/5eun PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5eun ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/AADAT_HUMAN AADAT_HUMAN]] Transaminase with broad substrate specificity. Has transaminase activity towards aminoadipate, kynurenine, methionine and glutamate. Shows activity also towards tryptophan, aspartate and hydroxykynurenine. Accepts a variety of oxo-acids as amino-group acceptors, with a preference for 2-oxoglutarate, 2-oxocaproic acid, phenylpyruvate and alpha-oxo-gamma-methiol butyric acid. Can also use glyoxylate as amino-group acceptor (in vitro).<ref>PMID:18620547</ref> | + | [https://www.uniprot.org/uniprot/AADAT_HUMAN AADAT_HUMAN] Transaminase with broad substrate specificity. Has transaminase activity towards aminoadipate, kynurenine, methionine and glutamate. Shows activity also towards tryptophan, aspartate and hydroxykynurenine. Accepts a variety of oxo-acids as amino-group acceptors, with a preference for 2-oxoglutarate, 2-oxocaproic acid, phenylpyruvate and alpha-oxo-gamma-methiol butyric acid. Can also use glyoxylate as amino-group acceptor (in vitro).<ref>PMID:18620547</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Church, W B]] | + | [[Category: Church WB]] |
| - | [[Category: Hanrahan, J R]] | + | [[Category: Hanrahan JR]] |
| - | [[Category: Harrop, S J]] | + | [[Category: Harrop SJ]] |
| - | [[Category: Jeffries, C M]] | + | [[Category: Jeffries CM]] |
| - | [[Category: Kwan, A]] | + | [[Category: Kwan A]] |
| - | [[Category: Nadvi, N A]] | + | [[Category: Nadvi NA]] |
| - | [[Category: Nematollahi, A]] | + | [[Category: Nematollahi A]] |
| - | [[Category: Sun, G]] | + | [[Category: Sun G]] |
| - | [[Category: Kynurenine aminotransferase ii]]
| + | |
| - | [[Category: Llp]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
AADAT_HUMAN Transaminase with broad substrate specificity. Has transaminase activity towards aminoadipate, kynurenine, methionine and glutamate. Shows activity also towards tryptophan, aspartate and hydroxykynurenine. Accepts a variety of oxo-acids as amino-group acceptors, with a preference for 2-oxoglutarate, 2-oxocaproic acid, phenylpyruvate and alpha-oxo-gamma-methiol butyric acid. Can also use glyoxylate as amino-group acceptor (in vitro).[1]
Publication Abstract from PubMed
Kynurenine aminotransferase II (KAT-II) is a 47 kDa pyridoxal phosphate (PLP)-dependent enzyme, active as a homodimer, which catalyses the transamination of the amino acids kynurenine (KYN) and 3-hydroxykynurenine (3-HK) in the tryptophan pathway, and is responsible for producing metabolites that lead to kynurenic acid (KYNA), which is implicated in several neurological diseases such as schizophrenia. In order to fully describe the role of KAT-II in the pathobiology of schizophrenia and other brain disorders, the crystal structure of full-length PLP-form hKAT-II was determined at 1.83 A resolution, the highest available. The electron density of the active site reveals an aldimine linkage between PLP and Lys263, as well as the active site residues, which characterize the fold-type I PLP-dependent enzymes.
Structure of the PLP-Form of the Human Kynurenine Aminotransferase II in a Novel Spacegroup at 1.83 A Resolution.,Nematollahi A, Sun G, Harrop SJ, Hanrahan JR, Church WB Int J Mol Sci. 2016 Mar 25;17(4). pii: E446. doi: 10.3390/ijms17040446. PMID:27023527[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Han Q, Cai T, Tagle DA, Robinson H, Li J. Substrate specificity and structure of human aminoadipate aminotransferase/kynurenine aminotransferase II. Biosci Rep. 2008 Aug;28(4):205-15. PMID:18620547 doi:10.1042/BSR20080085
- ↑ Nematollahi A, Sun G, Harrop SJ, Hanrahan JR, Church WB. Structure of the PLP-Form of the Human Kynurenine Aminotransferase II in a Novel Spacegroup at 1.83 A Resolution. Int J Mol Sci. 2016 Mar 25;17(4). pii: E446. doi: 10.3390/ijms17040446. PMID:27023527 doi:http://dx.doi.org/10.3390/ijms17040446
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