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| | <StructureSection load='4a9w' size='340' side='right'caption='[[4a9w]], [[Resolution|resolution]] 2.72Å' scene=''> | | <StructureSection load='4a9w' size='340' side='right'caption='[[4a9w]], [[Resolution|resolution]] 2.72Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4a9w]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"pseudomonas_maltophilia"_hugh_and_ryschenkow_1961 "pseudomonas maltophilia" hugh and ryschenkow 1961]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4A9W FirstGlance]. <br> | + | <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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Flavin-containing_monooxygenase Flavin-containing monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.13.8 1.14.13.8] </span></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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4a9w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a9w OCA], [http://pdbe.org/4a9w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4a9w RCSB], [http://www.ebi.ac.uk/pdbsum/4a9w PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4a9w ProSAT]</span></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> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/B2FRL2_STRMK B2FRL2_STRMK] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Monooxygenase|Monooxygenase]] | + | *[[Monooxygenase 3D structures|Monooxygenase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Pseudomonas maltophilia hugh and ryschenkow 1961]] | + | [[Category: Large Structures]] |
| - | [[Category: Flavin-containing monooxygenase]] | + | [[Category: Stenotrophomonas maltophilia]] |
| - | [[Category: Ali, S T]] | + | [[Category: Ali ST]] |
| - | [[Category: Allen, M J]] | + | [[Category: Allen MJ]] |
| - | [[Category: Cartwright, J]] | + | [[Category: Cartwright J]] |
| - | [[Category: Grogan, G]] | + | [[Category: Grogan G]] |
| - | [[Category: Hart, S]] | + | [[Category: Hart S]] |
| - | [[Category: Jensen, C N]] | + | [[Category: Jensen CN]] |
| - | [[Category: Turkenburg, J P]] | + | [[Category: Turkenburg JP]] |
| - | [[Category: Baeyer-villiger]]
| + | |
| - | [[Category: Fad]]
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| - | [[Category: Oxidoreductase]]
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| Structural highlights
Function
B2FRL2_STRMK
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Jensen CN, Cartwright J, Ward J, Hart S, Turkenburg JP, Ali ST, Allen MJ, Grogan G. A Flavoprotein Monooxygenase that Catalyses a Baeyer-Villiger Reaction and Thioether Oxidation Using NADH as the Nicotinamide Cofactor. Chembiochem. 2012 Apr 16;13(6):872-8. doi: 10.1002/cbic.201200006. Epub 2012 Mar , 13. PMID:22416037 doi:10.1002/cbic.201200006
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