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6wpu
From Proteopedia
(Difference between revisions)
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==Structure of S-allyl-L-cysteine S-oxygenase from Allium sativum== | ==Structure of S-allyl-L-cysteine S-oxygenase from Allium sativum== | ||
| - | <StructureSection load='6wpu' size='340' side='right'caption='[[6wpu]]' scene=''> | + | <StructureSection load='6wpu' size='340' side='right'caption='[[6wpu]], [[Resolution|resolution]] 2.08Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6WPU OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6WPU FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6wpu]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Allsa Allsa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6WPU OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6WPU FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6wpu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6wpu OCA], [http://pdbe.org/6wpu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6wpu RCSB], [http://www.ebi.ac.uk/pdbsum/6wpu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6wpu ProSAT]</span></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AsFMO1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4682 ALLSA])</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6wpu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6wpu OCA], [http://pdbe.org/6wpu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6wpu RCSB], [http://www.ebi.ac.uk/pdbsum/6wpu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6wpu ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Allicin is a component of the characteristic smell and flavor of garlic (Allium sativum). A flavin-containing monooxygenase (FMO) produced by A. sativum (AsFMO) was previously proposed to oxidize S-allyl-L-cysteine (SAC) to alliin, an allicin precursor. Here, we present a kinetic and structural characterization of AsFMO that suggests a possible contradiction to this proposal. Results of steady-state kinetic analyses revealed that AsFMO exhibits negligible activity with SAC; however, the enzyme was highly active with L-cysteine, N-acetyl-L-cysteine, and allyl mercaptan. We found that allyl mercaptan with NADPH is the preferred substrate-cofactor combination. Rapid-reaction kinetic analyses showed that NADPH binds tightly (KD ~2 muM) to AsFMO and that the hydride transfer occurs with pro-R stereospecificity. We detected formation of a long-wavelength band when AsFMO was reduced by NADPH, probably representing the formation of a charge transfer complex. In the absence of substrate, the reduced enzyme, in complex with NADP+, reacted with oxygen and formed an intermediate with a spectrum characteristic of C4a-hydroperoxyflavin, which decays several orders of magnitude slower than the kcat. The presence of substrate enhanced C4a-hydroperoxyflavin formation, and upon hydroxylation, oxidation occurred at a rate constant similar to the kcat. The structure of AsFMO complexed with FAD at 2.08 A resolution features two domains for binding of FAD and NADPH, representative of class B flavin monooxygenases. These biochemical and structural results are consistent with AsFMO being an S-monooxygenase involved in allicin biosynthesis by direct formation of sulfenic acid, and not by SAC oxidation. | ||
| + | |||
| + | Structure and function of a flavin-dependent S-monooxygenase from garlic (Allium sativum).,Valentino H, Campbell AC, Schuermann JP, Sultana N, Nam HG, LeBlanc S, Tanner JJ, Sobrado P J Biol Chem. 2020 Jun 11. pii: RA120.014484. doi: 10.1074/jbc.RA120.014484. PMID:32527723<ref>PMID:32527723</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6wpu" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Allsa]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Campbell | + | [[Category: Campbell, A C]] |
| - | [[Category: Schuermann | + | [[Category: Schuermann, J P]] |
| - | [[Category: Tanner | + | [[Category: Tanner, J J]] |
| + | [[Category: Flavin-containing monooxygenase]] | ||
| + | [[Category: Flavoprotein]] | ||
| + | [[Category: Oxidoreductase]] | ||
Revision as of 07:14, 25 June 2020
Structure of S-allyl-L-cysteine S-oxygenase from Allium sativum
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