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4c74
From Proteopedia
(Difference between revisions)
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| - | + | ==Phenylacetone monooxygenase: Reduced enzyme in complex with APADP== | |
| - | ===Phenylacetone monooxygenase | + | <StructureSection load='4c74' size='340' side='right' caption='[[4c74]], [[Resolution|resolution]] 1.97Å' scene=''> |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[4c74]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"thermonospora_fusca"_henssen_1957 "thermonospora fusca" henssen 1957]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C74 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C74 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=N01:3-ACETYLPYRIDINE+ADENINE+DINUCLEOTIDE'>N01</scene>, <scene name='pdbligand=P6G:HEXAETHYLENE+GLYCOL'>P6G</scene></td></tr> | ||
| + | <tr id='activity'><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 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=4c74 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c74 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4c74 RCSB], [http://www.ebi.ac.uk/pdbsum/4c74 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: Thermonospora fusca henssen 1957]] | ||
[[Category: Phenylacetone monooxygenase]] | [[Category: Phenylacetone monooxygenase]] | ||
| - | [[Category: Fraaije, M W | + | [[Category: Fraaije, M W]] |
| - | [[Category: Martinoli, C | + | [[Category: Martinoli, C]] |
| - | [[Category: Mattevi, A | + | [[Category: Mattevi, A]] |
[[Category: Baeyer-villiger]] | [[Category: Baeyer-villiger]] | ||
[[Category: Cofactor]] | [[Category: Cofactor]] | ||
[[Category: Flavin]] | [[Category: Flavin]] | ||
[[Category: Oxidoreductase]] | [[Category: Oxidoreductase]] | ||
Revision as of 17:24, 21 December 2014
Phenylacetone monooxygenase: Reduced enzyme in complex with APADP
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