8d1c
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of T252E-CYP199A4 in complex with 4-(Trifluoromethoxy)benzoic acid== | |
| + | <StructureSection load='8d1c' size='340' side='right'caption='[[8d1c]], [[Resolution|resolution]] 1.95Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8d1c]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodopseudomonas_palustris_HaA2 Rhodopseudomonas palustris HaA2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8D1C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8D1C FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=M4F:4-(trifluoromethoxy)benzoic+acid'>M4F</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=8d1c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8d1c OCA], [https://pdbe.org/8d1c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8d1c RCSB], [https://www.ebi.ac.uk/pdbsum/8d1c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8d1c ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q2IU02_RHOP2 Q2IU02_RHOP2] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Cytochrome P450 monooxygenase enzymes are versatile catalysts, which have been adapted for multiple applications in chemical synthesis. Mutation of a highly conserved active site threonine to a glutamate can convert these enzymes into peroxygenases that utilise hydrogen peroxide (H(2) O(2) ). Here, we use the T252E-CYP199A4 variant to study peroxide-driven oxidation activity by using H(2) O(2) and urea-hydrogen peroxide (UHP). We demonstrate that the T252E variant has a higher stability to H(2) O(2) in the presence of substrate that can undergo carbon-hydrogen abstraction. This peroxygenase variant could efficiently catalyse O-demethylation and an enantioselective epoxidation reaction (94 % ee). Neither the monooxygenase nor peroxygenase pathways of the P450 demonstrated a significant kinetic isotope effect (KIE) for the oxidation of deuterated substrates. These new peroxygenase variants offer the possibility of simpler cytochrome P450 systems for selective oxidations. To demonstrate this, a light driven H(2) O(2) generating system was used to support efficient product formation with this peroxygenase enzyme. | ||
| - | + | Selective Oxidations Using a Cytochrome P450 Enzyme Variant Driven with Surrogate Oxygen Donors and Light.,Lee JHZ, Podgorski MN, Moir M, Gee AR, Bell SG Chemistry. 2022 Sep 1;28(49):e202201366. doi: 10.1002/chem.202201366. Epub 2022 , Jul 14. PMID:35712785<ref>PMID:35712785</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 8d1c" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| - | [[Category: | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Rhodopseudomonas palustris HaA2]] | ||
| + | [[Category: Bell SG]] | ||
| + | [[Category: Bruning JB]] | ||
| + | [[Category: Lee JHZ]] | ||
Revision as of 06:03, 2 March 2023
Crystal structure of T252E-CYP199A4 in complex with 4-(Trifluoromethoxy)benzoic acid
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