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| | <StructureSection load='5ax8' size='340' side='right'caption='[[5ax8]], [[Resolution|resolution]] 2.99Å' scene=''> | | <StructureSection load='5ax8' size='340' side='right'caption='[[5ax8]], [[Resolution|resolution]] 2.99Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5ax8]] is a 4 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=5AX8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5AX8 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5ax8]] is a 4 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=5AX8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5AX8 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3pdb|3pdb]]</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]] 2.989Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GOT2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=5ax8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ax8 OCA], [https://pdbe.org/5ax8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ax8 RCSB], [https://www.ebi.ac.uk/pdbsum/5ax8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ax8 ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ax8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ax8 OCA], [http://pdbe.org/5ax8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ax8 RCSB], [http://www.ebi.ac.uk/pdbsum/5ax8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ax8 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/AATM_HUMAN AATM_HUMAN]] Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). Plays a key role in amino acid metabolism. Important for metabolite exchange between mitochondria and cytosol. Facilitates cellular uptake of long-chain free fatty acids.<ref>PMID:9537447</ref> | + | [https://www.uniprot.org/uniprot/AATM_HUMAN AATM_HUMAN] Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). Plays a key role in amino acid metabolism. Important for metabolite exchange between mitochondria and cytosol. Facilitates cellular uptake of long-chain free fatty acids.<ref>PMID:9537447</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: Chang, H]] | + | [[Category: Chang H]] |
| - | [[Category: Jiang, X]] | + | [[Category: Jiang X]] |
| - | [[Category: Wang, J]] | + | [[Category: Wang J]] |
| - | [[Category: Zhou, Y]] | + | [[Category: Zhou Y]] |
| - | [[Category: Aspartate aminotransferase]]
| + | |
| - | [[Category: Kynurenine aminotransferase-iv]]
| + | |
| - | [[Category: Plasma membrane fatty acid binding protein]]
| + | |
| - | [[Category: Three-dimensional structure]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
AATM_HUMAN Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). Plays a key role in amino acid metabolism. Important for metabolite exchange between mitochondria and cytosol. Facilitates cellular uptake of long-chain free fatty acids.[1]
Publication Abstract from PubMed
Mitochondrial aspartate aminotransferase (mAspAT) was recognized as a moonlighting enzyme because it has not only aminotransferase activity but also a high-affinity long-chain fatty acids (LCFA) binding site. This enzyme plays a key role in amino acid metabolism, biosynthesis of kynurenic acid and transport of the LCFA. Therefore, it is important to study the structure-function relationships of human mAspAT protein. In this work, the mature form of human mAspAT was expressed to a high level in Escherichia coli periplasmic space using pET-22b vector, purified by a combination of immobilized metal-affinity chromatography and cation exchange chromatography. Optimal activity of the enzyme occurred at a temperature of 47.5 masculineC and a pH of 8.5. Crystals of human mAspAT were grown using the hanging-drop vapour diffusion method at 277K with 0.1 M HEPES pH 6.8 and 25%(v/v) Jeffamine((R)) ED-2001 pH 6.8. The crystals diffracted to 2.99 A and belonged to the space group P1 with the unit-cell parameters a =56.7, b = 76.1, c = 94.2 A, alpha =78.0, beta =85.6, gamma = 78.4 masculine. Elucidation of mAspAT structure can provide a molecular basis towards understanding catalysis mechanism and substrate binding site of enzyme.
Recombinant expression, purification and crystallographic studies of the mature form of human mitochondrial aspartate aminotransferase.,Jiang X, Wang J, Chang H, Zhou Y Biosci Trends. 2016 Mar 10;10(1):79-84. doi: 10.5582/bst.2015.01150. Epub 2016, Feb 22. PMID:26902786[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Zhou SL, Gordon RE, Bradbury M, Stump D, Kiang CL, Berk PD. Ethanol up-regulates fatty acid uptake and plasma membrane expression and export of mitochondrial aspartate aminotransferase in HepG2 cells. Hepatology. 1998 Apr;27(4):1064-74. PMID:9537447 doi:http://dx.doi.org/10.1002/hep.510270423
- ↑ Jiang X, Wang J, Chang H, Zhou Y. Recombinant expression, purification and crystallographic studies of the mature form of human mitochondrial aspartate aminotransferase. Biosci Trends. 2016 Mar 10;10(1):79-84. doi: 10.5582/bst.2015.01150. Epub 2016, Feb 22. PMID:26902786 doi:http://dx.doi.org/10.5582/bst.2015.01150
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