4wg2: Difference between revisions
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==P411BM3-CIS T438S I263F regioselective C-H amination catalyst== | ==P411BM3-CIS T438S I263F regioselective C-H amination catalyst== | ||
<StructureSection load='4wg2' size='340' side='right' caption='[[4wg2]], [[Resolution|resolution]] 2.66Å' scene=''> | <StructureSection load='4wg2' size='340' side='right' caption='[[4wg2]], [[Resolution|resolution]] 2.66Å' scene=''> | ||
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4h23|4h23]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4h23|4h23]]</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=4wg2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wg2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4wg2 RCSB], [http://www.ebi.ac.uk/pdbsum/4wg2 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=4wg2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wg2 OCA], [http://pdbe.org/4wg2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4wg2 RCSB], [http://www.ebi.ac.uk/pdbsum/4wg2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4wg2 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 4wg2" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Cytochrome P450|Cytochrome P450]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 14:23, 4 August 2016
P411BM3-CIS T438S I263F regioselective C-H amination catalystP411BM3-CIS T438S I263F regioselective C-H amination catalyst
Structural highlights
Function[CPXB_BACME] Functions as a fatty acid monooxygenase. Catalyzes hydroxylation of medium and long-chain fatty acids at omega-1, omega-2 and omega-3 positions, with optimum chain lengths of 12-16 carbons (lauric, myristic, and palmitic acids). The reductase domain is required for electron transfer from NADP to cytochrome P450. Publication Abstract from PubMedWe recently demonstrated that variants of cytochrome P450BM3 (CYP102A1) catalyze the insertion of nitrogen species into benzylic C-H bonds to form new C-N bonds. An outstanding challenge in the field of C-H amination is catalyst-controlled regioselectivity. Here, we report two engineered variants of P450BM3 that provide divergent regioselectivity for C-H amination-one favoring amination of benzylic C-H bonds and the other favoring homo-benzylic C-H bonds. The two variants provide nearly identical kinetic isotope effect values (2.8-3.0), suggesting that C-H abstraction is rate-limiting. The 2.66-A crystal structure of the most active enzyme suggests that the engineered active site can preorganize the substrate for reactivity. We hypothesize that the enzyme controls regioselectivity through localization of a single C-H bond close to the iron nitrenoid. Enzyme-Controlled Nitrogen-Atom Transfer Enables Regiodivergent C-H Amination.,Hyster TK, Farwell CC, Buller AR, McIntosh JA, Arnold FH J Am Chem Soc. 2014 Oct 24. PMID:25325618[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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