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2ylw

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<StructureSection load='2ylw' size='340' side='right'caption='[[2ylw]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
<StructureSection load='2ylw' size='340' side='right'caption='[[2ylw]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2ylw]] 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=2YLW OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2YLW FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2ylw]] 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=2YLW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YLW FirstGlance]. <br>
</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=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></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=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr>
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<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]], [[2yls|2yls]], [[2ylr|2ylr]]</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;'>[[1w4x|1w4x]], [[2ylx|2ylx]], [[2ylz|2ylz]], [[2ylt|2ylt]], [[2ym1|2ym1]], [[2ym2|2ym2]], [[2yls|2yls]], [[2ylr|2ylr]]</div></td></tr>
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<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>
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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'>[http://proteopedia.org/fgij/fg.htm?mol=2ylw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ylw OCA], [http://pdbe.org/2ylw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ylw RCSB], [http://www.ebi.ac.uk/pdbsum/2ylw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2ylw ProSAT]</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=2ylw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ylw OCA], [https://pdbe.org/2ylw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ylw RCSB], [https://www.ebi.ac.uk/pdbsum/2ylw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ylw ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[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).
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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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<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==

Revision as of 12:32, 27 April 2022

SNAPSHOTS OF ENZYMATIC BAEYER-VILLIGER CATALYSIS: OXYGEN ACTIVATION AND INTERMEDIATE STABILIZATION: Arg337Lys MUTANT IN COMPLEX WITH MES

PDB ID 2ylw

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