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2ym2

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Current revision (13:36, 30 August 2023) (edit) (undo)
 
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<StructureSection load='2ym2' size='340' side='right'caption='[[2ym2]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
<StructureSection load='2ym2' size='340' side='right'caption='[[2ym2]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2ym2]] is a 1 chain structure with sequence from [https://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=2YM2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YM2 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2ym2]] 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=2YM2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YM2 FirstGlance]. <br>
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</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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2ylz|2ylz]], [[2ylt|2ylt]], [[1w4x|1w4x]], [[2ym1|2ym1]], [[2yls|2yls]], [[2ylr|2ylr]], [[2ylx|2ylx]], [[2ylw|2ylw]]</div></td></tr>
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<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>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Phenylacetone_monooxygenase Phenylacetone monooxygenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.13.92 1.14.13.92] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ym2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ym2 OCA], [https://pdbe.org/2ym2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ym2 RCSB], [https://www.ebi.ac.uk/pdbsum/2ym2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ym2 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=2ym2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ym2 OCA], [https://pdbe.org/2ym2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ym2 RCSB], [https://www.ebi.ac.uk/pdbsum/2ym2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ym2 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[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).
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[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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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Thermonospora fusca henssen 1957]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Phenylacetone monooxygenase]]
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[[Category: Thermobifida fusca]]
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[[Category: Dudek, H M]]
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[[Category: Dudek HM]]
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[[Category: Fraaije, M W]]
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[[Category: Fraaije MW]]
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[[Category: Martinoli, C]]
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[[Category: Martinoli C]]
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[[Category: Mattevi, A]]
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[[Category: Mattevi A]]
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[[Category: Orru, R]]
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[[Category: Orru R]]
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[[Category: Pazmino, D E.Torres]]
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[[Category: Royant A]]
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[[Category: Royant, A]]
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[[Category: Torres Pazmino DE]]
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[[Category: Weik, M]]
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[[Category: Weik M]]
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[[Category: Oxidoreductase]]
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[[Category: Oxygenase]]
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Current revision

SNAPSHOTS OF ENZYMATIC BAEYER-VILLIGER CATALYSIS: OXYGEN ACTIVATION AND INTERMEDIATE STABILIZATION: Arg337Lys MUTANT REDUCED STATE WITH NADP

PDB ID 2ym2

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