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3rwl
From Proteopedia
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| - | [[ | + | ==Structure of P450pyr hydroxylase== |
| + | <StructureSection load='3rwl' size='340' side='right' caption='[[3rwl]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3rwl]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Sphingopyxis_macrogoltabida Sphingopyxis macrogoltabida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RWL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3RWL FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene><br> | ||
| + | <tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ahpG1, Sphingomonas sp. ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=33050 Sphingopyxis macrogoltabida])</td></tr> | ||
| + | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alkane_1-monooxygenase Alkane 1-monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.15.3 1.14.15.3] </span></td></tr> | ||
| + | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3rwl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rwl OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3rwl RCSB], [http://www.ebi.ac.uk/pdbsum/3rwl PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Directed evolution of a monooxygenase to achieve very high enantioselectivity for hydroxylation at non-activated carbon atoms is demonstrated for the first time, where a triple mutant of P450pyr hydroxylase is obtained via determination of enzyme structure, iterative saturation mutagenesis, and high-throughput screening with a MS-based ee assay to increase the product ee from 53% to 98% for the hydroxylation of N-benzyl pyrrolidine to (S)-N-benzyl 3-hydroxypyrrolidine. | ||
| - | + | Evolving P450pyr hydroxylase for highly enantioselective hydroxylation at non-activated carbon atom.,Pham SQ, Pompidor G, Liu J, Li XD, Li Z Chem Commun (Camb). 2012 May 14;48(38):4618-20. Epub 2012 Mar 19. PMID:22430002<ref>PMID:22430002</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
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| - | == | + | |
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[[Category: Alkane 1-monooxygenase]] | [[Category: Alkane 1-monooxygenase]] | ||
[[Category: Sphingopyxis macrogoltabida]] | [[Category: Sphingopyxis macrogoltabida]] | ||
Revision as of 04:42, 5 June 2014
Structure of P450pyr hydroxylase
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