4a9w
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 4a9w is ON HOLD Authors: Jensen, C.N., Cartwright, J., Hart, S., Turkenburg, J.P., Ali, S.T., Allen, M.J., Grogan, G. Description: Flavin-containin...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Flavin-containing monooxygenase from Stenotrophomonas maltophilia== | |
| + | <StructureSection load='4a9w' size='340' side='right'caption='[[4a9w]], [[Resolution|resolution]] 2.72Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4a9w]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Stenotrophomonas_maltophilia Stenotrophomonas maltophilia]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4A9W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4A9W FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.72Å</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4a9w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a9w OCA], [https://pdbe.org/4a9w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4a9w RCSB], [https://www.ebi.ac.uk/pdbsum/4a9w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4a9w ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/B2FRL2_STRMK B2FRL2_STRMK] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | A gene from the marine bacterium Stenotrophomonas maltophilia encodes a 38.6 kDa FAD-containing flavoprotein (Uniprot B2FLR2) named S. maltophilia flavin-containing monooxygenase (SMFMO), which catalyses the oxidation of thioethers and also the regioselective Baeyer-Villiger oxidation of the model substrate bicyclo[3.2.0]hept-2-en-6-one. The enzyme was unusual in its ability to employ either NADH or NADPH as nicotinamide cofactor. The K(M) and k(cat) values for NADH were 23.7+/-9.1 muM and 0.029 s(-1) and 27.3+/-5.3 muM and 0.022 s(-1) for NADPH. However, k(cat) /K(M) value for the ketone substrate in the presence of 100 muM cofactor was 17 times greater for NADH than for NADPH. SMFMO catalysed the quantitative conversion of 5 mM ketone in the presence of substoichiometric concentrations of NADH with the formate dehydrogenase cofactor recycling system, to give the 2-oxa and 3-oxa lactone products of Baeyer-Villiger reaction in a ratio of 5:1, albeit with poor enantioselectivity. The conversion with NADPH was 15 %. SMFMO also catalysed the NADH-dependent transformation of prochiral aromatic thioethers, giving in the best case, 80 % ee for the transformation of p-chlorophenyl methyl sulfide to its R enantiomer. The structure of SMFMO reveals that the relaxation in cofactor specificity appears to be accomplished by the substitution of an arginine residue, responsible for recognition of the 2'-phosphate on the NADPH ribose in related NADPH-dependent FMOs, with a glutamine residue in SMFMO. SMFMO is thus representative of a separate class of single-component, flavoprotein monooxygenases that catalyse NADH-dependent oxidations from which possible sequences and strategies for developing NADH-dependent biocatalysts for asymmetric oxygenation reactions might be identified. | ||
| - | + | A Flavoprotein Monooxygenase that Catalyses a Baeyer-Villiger Reaction and Thioether Oxidation Using NADH as the Nicotinamide Cofactor.,Jensen CN, Cartwright J, Ward J, Hart S, Turkenburg JP, Ali ST, Allen MJ, Grogan G Chembiochem. 2012 Apr 16;13(6):872-8. doi: 10.1002/cbic.201200006. Epub 2012 Mar , 13. PMID:22416037<ref>PMID:22416037</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 4a9w" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Monooxygenase 3D structures|Monooxygenase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Stenotrophomonas maltophilia]] | ||
| + | [[Category: Ali ST]] | ||
| + | [[Category: Allen MJ]] | ||
| + | [[Category: Cartwright J]] | ||
| + | [[Category: Grogan G]] | ||
| + | [[Category: Hart S]] | ||
| + | [[Category: Jensen CN]] | ||
| + | [[Category: Turkenburg JP]] | ||
Current revision
Flavin-containing monooxygenase from Stenotrophomonas maltophilia
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