1u5u

<table><tr><td colspan='2'>[[1u5u]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Black_sea_rod Black sea rod]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U5U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1U5U FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Hydroperoxide_dehydratase Hydroperoxide dehydratase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.92 4.2.1.92] </span></td></tr>

[[https://www.uniprot.org/uniprot/AOSL_PLEHO AOSL_PLEHO]] Bifunctional enzyme which is responsible for allene oxide biosynthesis via a two-step reaction which involves conversion of arachidonic acid to a 8R-hydroperoxide intermediate followed by conversion of the hydroperoxide to allene oxide.<ref>PMID:9302294</ref> <ref>PMID:10559269</ref>

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== Publication Abstract from PubMed ==

8R-Lipoxygenase and allene oxide synthase (AOS) are parts of a naturally occurring fusion protein from the coral Plexaura homomalla. AOS catalyses the production of an unstable epoxide (an allene oxide) from the fatty acid hydroperoxide generated by the lipoxygenase activity. Here, we report the structure of the AOS domain and its striking structural homology to catalase. Whereas nominal sequence identity between the enzymes had been previously described, the extent of structural homology observed was not anticipated, given that this enzyme activity had been exclusively associated with the P450 superfamily, and conservation of a catalase fold without catalase activity is unprecedented. Whereas the heme environment is largely conserved, the AOS heme is planar and the distal histidine is flanked by two hydrogen-bonding residues. These critical differences likely facilitate the switch from a catalatic activity to that of a fatty acid hydroperoxidase.

The structure of coral allene oxide synthase reveals a catalase adapted for metabolism of a fatty acid hydroperoxide.,Oldham ML, Brash AR, Newcomer ME Proc Natl Acad Sci U S A. 2005 Jan 11;102(2):297-302. Epub 2004 Dec 29. PMID:15625113<ref>PMID:15625113</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 1u5u" style="background-color:#fffaf0;"></div>

[[Category: Black sea rod]]

[[Category: Hydroperoxide dehydratase]]

[[Category: Brash, A R]]

[[Category: Newcomer, M E]]

[[Category: Oldham, M L]]

[[Category: Allene oxide synthase]]

[[Category: Lyase]]