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| | <StructureSection load='1b5o' size='340' side='right'caption='[[1b5o]], [[Resolution|resolution]] 2.20Å' scene=''> | | <StructureSection load='1b5o' size='340' side='right'caption='[[1b5o]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1b5o]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thet8 Thet8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B5O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1B5O FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1b5o]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB8 Thermus thermophilus HB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B5O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1B5O FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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]] 2.2Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Aspartate_transaminase Aspartate transaminase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.1 2.6.1.1] </span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></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=1b5o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b5o OCA], [https://pdbe.org/1b5o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1b5o RCSB], [https://www.ebi.ac.uk/pdbsum/1b5o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1b5o 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=1b5o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b5o OCA], [https://pdbe.org/1b5o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1b5o RCSB], [https://www.ebi.ac.uk/pdbsum/1b5o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1b5o ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/AAPAT_THET8 AAPAT_THET8] Catalyzes the reversible conversion of aspartate and 2-oxoglutarate to glutamate and oxaloacetate (PubMed:8907187, PubMed:25070637). Can also transaminate prephenate in the presence of aspartate (PubMed:25070637, PubMed:30771275).<ref>PMID:25070637</ref> <ref>PMID:30771275</ref> <ref>PMID:8907187</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Aspartate transaminase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Thet8]] | + | [[Category: Thermus thermophilus HB8]] |
| - | [[Category: Hirotsu, K]] | + | [[Category: Hirotsu K]] |
| - | [[Category: Kawaguchi, S I]] | + | [[Category: Kawaguchi SI]] |
| - | [[Category: Kuramitsu, S]] | + | [[Category: Kuramitsu S]] |
| - | [[Category: Miyahara, I]] | + | [[Category: Miyahara I]] |
| - | [[Category: Nakai, T]] | + | [[Category: Nakai T]] |
| - | [[Category: Ura, H]] | + | [[Category: Ura H]] |
| - | [[Category: Aminotransferase]]
| + | |
| - | [[Category: Pyridoxal enzyme]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
AAPAT_THET8 Catalyzes the reversible conversion of aspartate and 2-oxoglutarate to glutamate and oxaloacetate (PubMed:8907187, PubMed:25070637). Can also transaminate prephenate in the presence of aspartate (PubMed:25070637, PubMed:30771275).[1] [2] [3]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Aspartate aminotransferase from an extremely thermophilic bacterium, Thermus thermophilus HB8 (ttAspAT), has been believed to be specific for an acidic substrate. However, stepwise introduction of mutations in the active-site residues finally changed its substrate specificity to that of a dual-substrate enzyme. The final mutant, [S15D, T17V, K109S, S292R] ttAspAT, is active toward both acidic and hydrophobic substrates. During the course of stepwise mutation, the activities toward acidic and hydrophobic substrates changed independently. The introduction of a mobile Arg292* residue into ttAspAT was the key step in the change to a "dual-substrate" enzyme. The substrate recognition mechanism of this thermostable "dual-substrate" enzyme was confirmed by X-ray crystallography. This work together with previous studies on various enzymes suggest that this unique "dual-substrate recognition" mechanism is a feature of not only aminotransferases but also other enzymes.
Substrate recognition mechanism of thermophilic dual-substrate enzyme.,Ura H, Nakai T, Kawaguchi SI, Miyahara I, Hirotsu K, Kuramitsu S J Biochem. 2001 Jul;130(1):89-98. PMID:11432784[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Dornfeld C, Weisberg AJ, K C R, Dudareva N, Jelesko JG, Maeda HA. Phylobiochemical characterization of class-Ib aspartate/prephenate aminotransferases reveals evolution of the plant arogenate phenylalanine pathway. Plant Cell. 2014 Jul;26(7):3101-14. PMID:25070637 doi:10.1105/tpc.114.127407
- ↑ Giustini C, Graindorge M, Cobessi D, Crouzy S, Robin A, Curien G, Matringe M. Tyrosine metabolism: identification of a key residue in the acquisition of prephenate aminotransferase activity by 1beta aspartate aminotransferase. FEBS J. 2019 Feb 16. doi: 10.1111/febs.14789. PMID:30771275 doi:http://dx.doi.org/10.1111/febs.14789
- ↑ Okamoto A, Kato R, Masui R, Yamagishi A, Oshima T, Kuramitsu S. An aspartate aminotransferase from an extremely thermophilic bacterium, Thermus thermophilus HB8. J Biochem. 1996 Jan;119(1):135-44. PMID:8907187 doi:10.1093/oxfordjournals.jbchem.a021198
- ↑ Ura H, Nakai T, Kawaguchi SI, Miyahara I, Hirotsu K, Kuramitsu S. Substrate recognition mechanism of thermophilic dual-substrate enzyme. J Biochem. 2001 Jul;130(1):89-98. PMID:11432784
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