View source for 2i0r

==Crystal structure of aromatic amine dehydrogenase TTQ-formamide adduct==
<StructureSection load='2i0r' size='340' side='right' caption='[[2i0r]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2i0r]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Alcaligenes_faecalis Alcaligenes faecalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2I0R OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2I0R FirstGlance]. <br>
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=1TQ:6-(FORMYLAMINO)-7-HYDROXY-L-TRYPTOPHAN'>1TQ</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2i0s|2i0s]], [[2i0t|2i0t]], [[2hxc|2hxc]]</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Aralkylamine_dehydrogenase_(azurin) Aralkylamine dehydrogenase (azurin)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.9.2 1.4.9.2] </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=2i0r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2i0r OCA], [http://pdbe.org/2i0r PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2i0r RCSB], [http://www.ebi.ac.uk/pdbsum/2i0r PDBsum]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/AAUB_ALCFA AAUB_ALCFA]] Oxidizes primary aromatic amines and, more slowly, some long-chain aliphatic amines, but not methylamine or ethylamine. Uses azurin as an electron acceptor to transfer electrons from the reduced tryptophylquinone cofactor.<ref>PMID:11495996</ref> <ref>PMID:16279953</ref> <ref>PMID:8188594</ref> <ref>PMID:16614214</ref>  
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/i0/2i0r_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2i0r ConSurf].
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== Publication Abstract from PubMed ==
Aromatic amine dehydrogenase uses a tryptophan tryptophylquinone (TTQ) cofactor to oxidatively deaminate primary aromatic amines. In the reductive half-reaction, a proton is transferred from the substrate C1 to betaAsp-128 O-2, in a reaction that proceeds by H-tunneling. Using solution studies, kinetic crystallography, and computational simulation we show that the mechanism of oxidation of aromatic carbinolamines is similar to amine oxidation, but that carbinolamine oxidation occurs at a substantially reduced rate. This has enabled us to determine for the first time the structure of the intermediate prior to the H-transfer/reduction step. The proton-betaAsp-128 O-2 distance is approximately 3.7A, in contrast to the distance of approximately 2.7A predicted for the intermediate formed with the corresponding primary amine substrate. This difference of approximately 1.0 A is due to an unexpected conformation of the substrate moiety, which is supported by molecular dynamic simulations and reflected in the approximately 10(7)-fold slower TTQ reduction rate with phenylaminoethanol compared with that with primary amines. A water molecule is observed near TTQ C-6 and is likely derived from the collapse of the preceding carbinolamine TTQ-adduct. We suggest this water molecule is involved in consecutive proton transfers following TTQ reduction, and is ultimately repositioned near the TTQ O-7 concomitant with protein rearrangement. For all carbinolamines tested, highly stable amide-TTQ adducts are formed following proton abstraction and TTQ reduction. Slow hydrolysis of the amide occurs after, rather than prior to, TTQ oxidation and leads ultimately to a carboxylic acid product.

New insights into the reductive half-reaction mechanism of aromatic amine dehydrogenase revealed by reaction with carbinolamine substrates.,Roujeinikova A, Hothi P, Masgrau L, Sutcliffe MJ, Scrutton NS, Leys D J Biol Chem. 2007 Aug 17;282(33):23766-77. Epub 2007 May 1. PMID:17475620<ref>PMID:17475620</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 2i0r" style="background-color:#fffaf0;"></div>

==See Also==
*[[Aromatic amine dehydrogenase|Aromatic amine dehydrogenase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Alcaligenes faecalis]]
[[Category: Leys, D]]
[[Category: Roujeinikova, A]]
[[Category: Carbinolamine oxidation]]
[[Category: Oxidoreductase]]
[[Category: Ttq]]