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4dbc
From Proteopedia
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| - | [[ | + | ==Substrate Activation in Aspartate Aminotransferase== |
| + | <StructureSection load='4dbc' size='340' side='right' caption='[[4dbc]], [[Resolution|resolution]] 1.50Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4dbc]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DBC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4DBC FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=3QP:(E)-N-{2-HYDROXY-3-METHYL-6-[(PHOSPHONOOXY)METHYL]BENZYLIDENE}-L-ASPARTIC+ACID'>3QP</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Aspartate_transaminase Aspartate transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.1 2.6.1.1] </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=4dbc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dbc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4dbc RCSB], [http://www.ebi.ac.uk/pdbsum/4dbc PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Binding isotope effects for l-aspartate reacting with the inactive K258A mutant of PLP-dependent aspartate aminotransferase to give a stable external aldimine intermediate are reported. They provide direct evidence for electronic ground-state destabilization via hyperconjugation. The smaller equilibrium isotope effect with deazaPLP-reconstituted K258A indicates that the pyridine nitrogen plays an important role in labilizing the Calpha-H bond. | ||
| - | + | Ground-state electronic destabilization via hyperconjugation in aspartate aminotransferase.,Griswold WR, Castro JN, Fisher AJ, Toney MD J Am Chem Soc. 2012 May 23;134(20):8436-8. doi: 10.1021/ja302809e. Epub 2012 May , 10. PMID:22551424<ref>PMID:22551424</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| - | + | ==See Also== | |
| - | + | *[[Aspartate Aminotransferase|Aspartate Aminotransferase]] | |
| - | == | + | == References == |
| - | [[ | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Aspartate transaminase]] | [[Category: Aspartate transaminase]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
| - | [[Category: Fisher, A J | + | [[Category: Fisher, A J]] |
| - | [[Category: Griswold, W R | + | [[Category: Griswold, W R]] |
| - | [[Category: Toney, M D | + | [[Category: Toney, M D]] |
[[Category: Aminotransferase]] | [[Category: Aminotransferase]] | ||
[[Category: Transferase]] | [[Category: Transferase]] | ||
Revision as of 15:24, 9 December 2014
Substrate Activation in Aspartate Aminotransferase
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