4c74: 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 20:24, 21 December 2014
Phenylacetone monooxygenase: Reduced enzyme in complex with APADPPhenylacetone monooxygenase: Reduced enzyme in complex with APADP
Structural highlights
Publication Abstract from PubMedA 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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