4c77

Phenylacetone monooxygenase: oxidised R337K mutant in complex with APADP

spinqualitylabelsall models 4c77, resolution 2.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4c77 is a 1 chain structure with sequence from "thermonospora_fusca"_henssen_1957 "thermonospora fusca" henssen 1957. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: FAD, N01, P6G Related: 4c74 Activity: Phenylacetone monooxygenase, with EC number 1.14.13.92 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Monooxygenase

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