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=''> | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4czz|4czz]], [[4d04|4d04]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4czz|4czz]], [[4d04|4d04]]</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='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=4d03 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d03 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4d03 RCSB], [http://www.ebi.ac.uk/pdbsum/4d03 PDBsum]</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=4d03 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d03 OCA], [http://pdbe.org/4d03 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4d03 RCSB], [http://www.ebi.ac.uk/pdbsum/4d03 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4d03 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4d03" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 01:41, 5 August 2016
Structure of the Cys65Asp mutant of phenylacetone monooxygenase: oxidised stateStructure of the Cys65Asp mutant of phenylacetone monooxygenase: oxidised state
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 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. References
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