4c77: Difference between revisions
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==Phenylacetone monooxygenase: oxidised R337K mutant in complex with APADP== | ==Phenylacetone monooxygenase: oxidised R337K mutant in complex with APADP== | ||
<StructureSection load='4c77' size='340' side='right' caption='[[4c77]], [[Resolution|resolution]] 2.70Å' scene=''> | <StructureSection load='4c77' size='340' side='right'caption='[[4c77]], [[Resolution|resolution]] 2.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4c77]] 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=4C77 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C77 FirstGlance]. <br> | <table><tr><td colspan='2'>[[4c77]] 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=4C77 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C77 FirstGlance]. <br> | ||
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</div> | </div> | ||
<div class="pdbe-citations 4c77" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 4c77" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Monooxygenase|Monooxygenase]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Thermonospora fusca henssen 1957]] | [[Category: Thermonospora fusca henssen 1957]] | ||
[[Category: Large Structures]] | |||
[[Category: Phenylacetone monooxygenase]] | [[Category: Phenylacetone monooxygenase]] | ||
[[Category: Fraaije, M W]] | [[Category: Fraaije, M W]] | ||
Revision as of 12:57, 20 March 2019
Phenylacetone monooxygenase: oxidised R337K mutant in complex with APADPPhenylacetone monooxygenase: oxidised R337K mutant in complex with APADP
Structural highlights
Function[PAMO_THEFY] Catalyzes a Baeyer-Villiger oxidation reaction, i.e. the insertion of an oxygen atom into a carbon-carbon bond adjacent to a carbonyl, which converts ketones to esters. Is most efficient with phenylacetone as substrate, leading to the formation of benzyl acetate. Can also oxidize other aromatic ketones (benzylacetone, alpha-methylphenylacetone and 4-hydroxyacetophenone), some aliphatic ketones (dodecan-2-one and bicyclohept-2-en-6-one) and sulfides (e.g. methyl 4-tolylsulfide). 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. See AlsoReferences
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