5mq6

Polycyclic Ketone Monooxygenase from the Thermophilic Fungus Thermothelomyces thermophila

spinqualitylabelsall models 5mq6, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5mq6 is a 1 chain structure with sequence from Thermothelomyces thermophilus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2Å Ligands: FAD, GOL, NDP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function G2QA95_THET4 Publication Abstract from PubMed Regio- and stereoselective Baeyer-Villiger oxidations are difficult to achieve by classical chemical means, particularly when large, functionalized molecules are to be converted. Biocatalysis using flavin-containing Baeyer-Villiger monooxygenases (BVMOs) is a well-established tool to address these challenges, but known BVMOs have shortcomings in either stability or substrate selectivity. We characterized a novel BVMO from the thermophilic fungus Thermothelomyces thermophila, determined its three-dimensional structure, and demonstrated its use as a promising biocatalyst. This fungal enzyme displays excellent enantioselectivity, acts on various ketones, and is particularly active on polycyclic molecules. Most notably we observed that the enzyme can perform oxidations on both the A and D ring when converting steroids. These functional properties can be linked to unique structural features, which identify enzymes acting on bulky substrates as a distinct subgroup of the BVMO class. Polycyclic Ketone Monooxygenase from the Thermophilic Fungus Thermothelomyces thermophila: A Structurally Distinct Biocatalyst for Bulky Substrates.,Furst MJ, Savino S, Dudek HM, Gomez Castellanos JR, Gutierrez de Souza C, Rovida S, Fraaije MW, Mattevi A J Am Chem Soc. 2017 Jan 3. doi: 10.1021/jacs.6b12246. PMID:28010060 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA