4d03: Difference between revisions
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==Structure of the Cys65Asp mutant of phenylacetone monooxygenase: oxidised state== | ==Structure of the Cys65Asp mutant of phenylacetone monooxygenase: oxidised state== | ||
<StructureSection load='4d03' size='340' side='right' caption='[[4d03]], [[Resolution|resolution]] 1.81Å' scene=''> | <StructureSection load='4d03' size='340' side='right'caption='[[4d03]], [[Resolution|resolution]] 1.81Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4d03]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4D03 OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[4d03]] 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=4D03 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4D03 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.81Å</td></tr> | ||
<tr id=' | <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>, <scene name='pdbligand=P6G:HEXAETHYLENE+GLYCOL'>P6G</scene></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=4d03 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d03 OCA], [https://pdbe.org/4d03 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4d03 RCSB], [https://www.ebi.ac.uk/pdbsum/4d03 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4d03 ProSAT]</span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [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 == | ||
| Line 20: | Line 19: | ||
</div> | </div> | ||
<div class="pdbe-citations 4d03" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 4d03" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Monooxygenase 3D structures|Monooxygenase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Brondani | [[Category: Thermobifida fusca]] | ||
[[Category: Dudek | [[Category: Brondani PB]] | ||
[[Category: Fraaije | [[Category: Dudek HM]] | ||
[[Category: Martinoli | [[Category: Fraaije MW]] | ||
[[Category: Mattevi | [[Category: Martinoli C]] | ||
[[Category: Mattevi A]] | |||
Latest revision as of 15:18, 20 December 2023
Structure of the Cys65Asp mutant of phenylacetone monooxygenase: oxidised stateStructure of the Cys65Asp mutant of phenylacetone monooxygenase: oxidised state
Structural highlights
FunctionPAMO_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 PubMedBy a targeted enzyme engineering approach, we were able to create an efficient NADPH oxidase from a monooxygenase. Intriguingly, replacement of only one specific single amino acid was sufficient for such a monooxygenase-to-oxidase switch-a complete transition in enzyme activity. Pre-steady-state kinetic analysis and elucidation of the crystal structure of the C65D PAMO mutant revealed that the mutation introduces small changes near the flavin cofactor, resulting in a rapid decay of the peroxyflavin intermediate. The engineered biocatalyst was shown to be a thermostable, solvent tolerant, and effective cofactor-regenerating biocatalyst. Therefore, it represents a valuable new biocatalytic tool. Finding the Switch: Turning a Baeyer-Villiger Monooxygenase into a NADPH Oxidase.,Brondani PB, Dudek HM, Martinoli C, Mattevi A, Fraaije MW J Am Chem Soc. 2014 Dec 1. PMID:25423359[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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