5aa6

<StructureSection load='5aa6' size='340' side='right' caption='[[5aa6]], [[Resolution|resolution]] 2.26&Aring;' scene=''>

<table><tr><td colspan='2'>[[5aa6]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Ascophyllum_nodosum Ascophyllum nodosum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AA6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5AA6 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=VO4:VANADATE+ION'>VO4</scene></td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Bromide_peroxidase Bromide peroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.18 1.11.1.18] </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=5aa6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5aa6 OCA], [http://pdbe.org/5aa6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5aa6 RCSB], [http://www.ebi.ac.uk/pdbsum/5aa6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5aa6 ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

The sequence of bromoperoxidase II from the brown alga Ascophyllum nodosum was determined from a full length cloned cDNA, obtained from a tandem mass spectrometry RT-PCR-approach. The clone encodes a protein composed of 641 amino-acids, which provides a mature 67.4 kDa-bromoperoxidase II-protein (620 amino-acids). Based on 43% sequence homology with the previously characterized bromoperoxidase I from A. nodosum, a tertiary structure was modeled for the bromoperoxidase II. The structural model was refined on the basis of results from gel filtration and vanadate-binding studies, showing that the bromoperoxidase II is a hexameric metalloprotein, which binds 0.5 equivalents of vanadate as cofactor per 67.4 kDa-subunit, for catalyzing oxidation of bromide by hydrogen peroxide in a bi-bi-ping-pong mechanism (k(cat) = 153 s(-1), 22 degrees C, pH 5.9). Bromide thereby is converted into a bromoelectrophile of reactivity similar to molecular bromine, based on competition kinetic data on phenol bromination and correlation analysis. Reactivity provided by the bromoperoxidase II mimics biosynthesis of methyl 4-bromopyrrole-2-carboxylate, a natural product isolated from the marine sponge Axinella tenuidigitata.

 

== References ==

[[Category: Bromide peroxidase]]

[[Category: Czjzek, M]]

[[Category: Dabin, J]]

[[Category: Delage, L]]

[[Category: Hartung, J]]

[[Category: Jeudy, A]]

[[Category: Leblanc, C]]

[[Category: Radlow, M]]

[[Category: Vanadium-dependant halogenperoxidase]]