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4ovi
From Proteopedia
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| - | ''' | + | ==Phenylacetone monooxygenase: oxidised enzyme in complex with APADP== |
| + | <StructureSection load='4ovi' size='340' side='right' caption='[[4ovi]], [[Resolution|resolution]] 1.87Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4ovi]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OVI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4OVI FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=N01:3-ACETYLPYRIDINE+ADENINE+DINUCLEOTIDE'>N01</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene><br> | ||
| + | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phenylacetone_monooxygenase Phenylacetone monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.13.92 1.14.13.92] </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=4ovi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ovi OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ovi RCSB], [http://www.ebi.ac.uk/pdbsum/4ovi PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | A general question in biochemistry is the interplay between the chemical properties of cofactors and the surrounding protein matrix. Here, the functions of NADP+ and FAD are explored by investigation of a representative monooxygenase reconstituted with chemically-modified cofactor analogues. Like pieces of a jigsaw puzzle, the enzyme active site juxtaposes the flavin and nicotinamide rings, harnessing their H-bonding and steric properties to finely construct an oxygen-reacting center that restrains the flavin-peroxide intermediate in a catalytically-competent orientation. Strikingly, the regio- and stereoselectivities of the reaction are essentially unaffected by cofactor modifications. These observations indicate a remarkable robustness of this complex multi-cofactor active site, which has implications for enzyme design based on cofactor engineering approaches. | ||
| - | + | Beyond the Protein Matrix: Probing Cofactor Variants in a Baeyer-Villiger Oxygenation Reaction.,Martinoli C, Dudek HM, Orru R, Edmondson DE, Fraaije MW, Mattevi A ACS Catal. 2013;3(12):3058-3062. PMID:24443704<ref>PMID:24443704</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Phenylacetone monooxygenase]] | ||
| + | [[Category: Fraaije, M W.]] | ||
| + | [[Category: Martinoli, C.]] | ||
| + | [[Category: Mattevi, A.]] | ||
| + | [[Category: Baeyer-villiger]] | ||
| + | [[Category: Cofactor]] | ||
| + | [[Category: Flavin]] | ||
Revision as of 09:35, 28 May 2014
Phenylacetone monooxygenase: oxidised enzyme in complex with APADP
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