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| | <StructureSection load='2ylr' size='340' side='right'caption='[[2ylr]], [[Resolution|resolution]] 2.26Å' scene=''> | | <StructureSection load='2ylr' size='340' side='right'caption='[[2ylr]], [[Resolution|resolution]] 2.26Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2ylr]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"thermonospora_fusca"_henssen_1957 "thermonospora fusca" henssen 1957]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YLR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2YLR FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2ylr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermobifida_fusca Thermobifida fusca]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YLR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YLR 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=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</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]] 2.26Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1w4x|1w4x]], [[2ylx|2ylx]], [[2ylz|2ylz]], [[2ylt|2ylt]], [[2ym1|2ym1]], [[2ym2|2ym2]], [[2ylw|2ylw]], [[2yls|2yls]]</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=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phenylacetone_monooxygenase Phenylacetone monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.13.92 1.14.13.92] </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=2ylr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ylr OCA], [https://pdbe.org/2ylr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ylr RCSB], [https://www.ebi.ac.uk/pdbsum/2ylr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ylr ProSAT]</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=2ylr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ylr OCA], [http://pdbe.org/2ylr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ylr RCSB], [http://www.ebi.ac.uk/pdbsum/2ylr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2ylr ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PAMO_THEFY PAMO_THEFY]] Catalyzes a Baeyer-Villiger oxidation reaction, i.e. the insertion of an oxygen atom into a carbon-carbon bond adjacent to a carbonyl, which converts ketones to esters. Is most efficient with phenylacetone as substrate, leading to the formation of benzyl acetate. Can also oxidize other aromatic ketones (benzylacetone, alpha-methylphenylacetone and 4-hydroxyacetophenone), some aliphatic ketones (dodecan-2-one and bicyclohept-2-en-6-one) and sulfides (e.g. methyl 4-tolylsulfide). | + | [https://www.uniprot.org/uniprot/PAMO_THEFY PAMO_THEFY] Catalyzes a Baeyer-Villiger oxidation reaction, i.e. the insertion of an oxygen atom into a carbon-carbon bond adjacent to a carbonyl, which converts ketones to esters. Is most efficient with phenylacetone as substrate, leading to the formation of benzyl acetate. Can also oxidize other aromatic ketones (benzylacetone, alpha-methylphenylacetone and 4-hydroxyacetophenone), some aliphatic ketones (dodecan-2-one and bicyclohept-2-en-6-one) and sulfides (e.g. methyl 4-tolylsulfide). |
| | <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: Thermonospora fusca henssen 1957]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Phenylacetone monooxygenase]] | + | [[Category: Thermobifida fusca]] |
| - | [[Category: Dudek, H M]] | + | [[Category: Dudek HM]] |
| - | [[Category: Fraaije, M W]] | + | [[Category: Fraaije MW]] |
| - | [[Category: Martinoli, C]] | + | [[Category: Martinoli C]] |
| - | [[Category: Mattevi, A]] | + | [[Category: Mattevi A]] |
| - | [[Category: Orru, R]] | + | [[Category: Orru R]] |
| - | [[Category: Pazmino, D E.Torres]] | + | [[Category: Royant A]] |
| - | [[Category: Royant, A]] | + | [[Category: Torres Pazmino DE]] |
| - | [[Category: Weik, M]] | + | [[Category: Weik M]] |
| - | [[Category: Baeyer-villiger reaction]]
| + | |
| - | [[Category: Fad]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Oxygenase]]
| + | |
| Structural highlights
Function
PAMO_THEFY Catalyzes a Baeyer-Villiger oxidation reaction, i.e. the insertion of an oxygen atom into a carbon-carbon bond adjacent to a carbonyl, which converts ketones to esters. Is most efficient with phenylacetone as substrate, leading to the formation of benzyl acetate. Can also oxidize other aromatic ketones (benzylacetone, alpha-methylphenylacetone and 4-hydroxyacetophenone), some aliphatic ketones (dodecan-2-one and bicyclohept-2-en-6-one) and sulfides (e.g. methyl 4-tolylsulfide).
Publication Abstract from PubMed
Baeyer-Villiger monooxygenases catalyze the oxidation of carbonylic substrates to ester or lactone products using NADPH as electron donor and molecular oxygen as oxidative reactant. Using protein engineering, kinetics, microspectrophotometry, crystallography, and intermediate analogs, we have captured several snapshots along the catalytic cycle which highlight key features in enzyme catalysis. After acting as electron donor, the enzyme-bound NADP(H) forms an H-bond with the flavin cofactor. This interaction is critical for stabilizing the oxygen-activating flavin-peroxide intermediate that results from the reaction of the reduced cofactor with oxygen. An essential active-site arginine acts as anchoring element for proper binding of the ketone substrate. Its positively charged guanidinium group can enhance the propensity of the substrate to undergo a nucleophilic attack by the flavin-peroxide intermediate. Furthermore, the arginine side chain, together with the NADP(+) ribose group, forms the niche that hosts the negatively charged Criegee intermediate that is generated upon reaction of the substrate with the flavin-peroxide. The fascinating ability of Baeyer-Villiger monooxygenases to catalyze a complex multistep catalytic reaction originates from concerted action of this Arg-NADP(H) pair and the flavin subsequently to promote flavin reduction, oxygen activation, tetrahedral intermediate formation, and product synthesis and release. The emerging picture is that these enzymes are mainly oxygen-activating and "Criegee-stabilizing" catalysts that act on any chemically suitable substrate that can diffuse into the active site, emphasizing their potential value as toolboxes for biocatalytic applications.
Snapshots of Enzymatic Baeyer-Villiger Catalysis: OXYGEN ACTIVATION AND INTERMEDIATE STABILIZATION.,Orru R, Dudek HM, Martinoli C, Torres Pazmino DE, Royant A, Weik M, Fraaije MW, Mattevi A J Biol Chem. 2011 Aug 19;286(33):29284-91. Epub 2011 Jun 22. PMID:21697090[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Orru R, Dudek HM, Martinoli C, Torres Pazmino DE, Royant A, Weik M, Fraaije MW, Mattevi A. Snapshots of Enzymatic Baeyer-Villiger Catalysis: OXYGEN ACTIVATION AND INTERMEDIATE STABILIZATION. J Biol Chem. 2011 Aug 19;286(33):29284-91. Epub 2011 Jun 22. PMID:21697090 doi:10.1074/jbc.M111.255075
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