5m0z
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==Cyclohexanone Monooxygenase from T. municipale: reduced enzyme bound to NADP+== | |
| + | <StructureSection load='5m0z' size='340' side='right' caption='[[5m0z]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5m0z]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5M0Z OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5M0Z FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA7:[(2R,3R,4R,5R)-5-(6-AMINO-9H-PURIN-9-YL)-3-HYDROXY-4-(PHOSPHONOOXY)TETRAHYDROFURAN-2-YL]METHYL+[(2R,3S,4S)-3,4-DIHYDROXYTETRAHYDROFURAN-2-YL]METHYL+DIHYDROGEN+DIPHOSPHATE'>NA7</scene></td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cyclohexanone_monooxygenase Cyclohexanone monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.13.22 1.14.13.22] </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=5m0z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5m0z OCA], [http://pdbe.org/5m0z PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5m0z RCSB], [http://www.ebi.ac.uk/pdbsum/5m0z PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5m0z ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Cyclohexanone monooxygenase (CHMO) is a promising biocatalyst for industrial reactions owing to its broad substrate spectrum and excellent regio-, chemo-, and enantioselectivity. However, the low stability of many Baeyer-Villiger monooxygenases is an obstacle for their exploitation in industry. Characterization and crystal structure determination of a robust CHMO from Thermocrispum municipale is reported. The enzyme efficiently converts a variety of aliphatic, aromatic, and cyclic ketones, as well as prochiral sulfides. A compact substrate-binding cavity explains its preference for small rather than bulky substrates. Small-scale conversions with either purified enzyme or whole cells demonstrated the remarkable properties of this newly discovered CHMO. The exceptional solvent tolerance and thermostability make the enzyme very attractive for biotechnology. | ||
| - | + | Characterization and Crystal Structure of a Robust Cyclohexanone Monooxygenase.,Romero E, Castellanos JR, Mattevi A, Fraaije MW Angew Chem Int Ed Engl. 2016 Nov 22. doi: 10.1002/anie.201608951. PMID:27873437<ref>PMID:27873437</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Gomez-Castellanos, J | + | <div class="pdbe-citations 5m0z" style="background-color:#fffaf0;"></div> |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Cyclohexanone monooxygenase]] | ||
| + | [[Category: Gomez-Castellanos, J R]] | ||
[[Category: Mattevi, A]] | [[Category: Mattevi, A]] | ||
| + | [[Category: Baeyer-villiger monooxygenases flavoenzyme]] | ||
| + | [[Category: Oxidoreductase]] | ||
Revision as of 19:40, 9 December 2016
Cyclohexanone Monooxygenase from T. municipale: reduced enzyme bound to NADP+
| |||||||||||
