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2ylw

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Revision as of 12:56, 22 July 2020

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

Structural highlights

2ylw is a 1 chain structure with sequence from "thermonospora_fusca"_henssen_1957 "thermonospora fusca" henssen 1957. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Related:	1w4x, 2ylx, 2ylz, 2ylt, 2ym1, 2ym2, 2yls, 2ylr
Activity:	Phenylacetone monooxygenase, with EC number 1.14.13.92
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.

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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2ylw"

@@ Line 1: / Line 1: @@
 ==SNAPSHOTS OF ENZYMATIC BAEYER-VILLIGER CATALYSIS: OXYGEN ACTIVATION AND INTERMEDIATE STABILIZATION: Arg337Lys MUTANT IN COMPLEX WITH MES==
-<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 ==
-<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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2YLW FirstGlance]. <br>
+<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>
-</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=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>
 <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>
 <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'>[http://oca.weizmann.ac.il/oca-docs/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>
+<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>
 </table>
 == Function ==
@@ Line 22: / Line 22: @@
 ==See Also==
-*[[Monooxygenase|Monooxygenase]]
+*[[Monooxygenase 3D structures|Monooxygenase 3D structures]]
 == References ==
 <references/>
@@ Line 28: / Line 28: @@
 </StructureSection>
 [[Category: Thermonospora fusca henssen 1957]]
+[[Category: Large Structures]]
 [[Category: Phenylacetone monooxygenase]]
 [[Category: Dudek, H M]]

2ylw

From Proteopedia

Revision as of 12:56, 22 July 2020

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

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

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