1ivr

<StructureSection load='1ivr' size='340' side='right' caption='[[1ivr]], [[Resolution|resolution]] 2.40&Aring;' scene=''>

<table><tr><td colspan='2'>[[1ivr]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Chick Chick]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IVR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IVR FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CBA:N-PYRIDOXYL-2,3-DIHYDROXYASPARTIC+ACID-5-MONOPHOSPHATE'>CBA</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=1ivr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ivr OCA], [http://pdbe.org/1ivr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ivr RCSB], [http://www.ebi.ac.uk/pdbsum/1ivr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ivr ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/AATM_CHICK AATM_CHICK]] 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. May facilitate cellular uptake of long-chain free fatty acids (By similarity).

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== Publication Abstract from PubMed ==

The crystal structure of mitochondrial aspartate aminotransferase (mAAT) of chicken complexed with erythro-beta-hydroxyaspartate has been determined at 2.4 A resolution. Pregrown crystals of mAAT complexed with the inhibitor maleate (closed enzyme conformation, orthorhombic space group C222(1)) were soaked in solutions of erythro-beta-hydroxyaspartate. The ligand exchange was monitored by microspectrophotometry. The active site turned out to be predominantly occupied by the carbinolamine intermediate. The carbinolamine is a true intermediate of the catalytic cycle forming the last covalently bound enzyme:substrate complex before release of the keto acid product. Occupancies of approximately 80% for the carbinolamine and of approximately 20% for the quinonoid intermediate were obtained. Two hydrogen bonds were identified that are potentially relevant for the accumulation of the carbinolamine intermediate: one to the hydroxyl group of Tyr 70* and the other to the epsilon-NH2 group of Lys 258.

Aspartate aminotransferase complexed with erythro-beta-hydroxyaspartate: crystallographic and spectroscopic identification of the carbinolamine intermediate.,von Stosch AG Biochemistry. 1996 Dec 3;35(48):15260-8. PMID:8952476<ref>PMID:8952476</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1ivr" style="background-color:#fffaf0;"></div>

*[[Aspartate Aminotransferase|Aspartate Aminotransferase]]

[[Category: Aspartate transaminase]]

[[Category: Chick]]

[[Category: Stosch, A Graf Von]]

[[Category: Erythro-beta-hydroxyaspartate]]