3rwl: Difference between revisions
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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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
< | |||
[[Category: Alkane 1-monooxygenase]] | [[Category: Alkane 1-monooxygenase]] | ||
[[Category: Sphingopyxis macrogoltabida]] | [[Category: Sphingopyxis macrogoltabida]] | ||
