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Flavoprotein monooxygenases, a diverse class of oxidative biocatalysts.
An inventory of known flavoprotein monooxygenases belonging to these different enzyme subclasses is provided and the biocatalytic potential of a selected number of flavop protein monooxyGENases is highlighted. Expand
Crystal structure of a Baeyer-Villiger monooxygenase.
The structural studies highlight the functional complexity of this class of flavoenzymes, which coordinate the binding of three substrates in proximity of the flavin cofactor with formation of two distinct catalytic intermediates. Expand
Flavoenzymes: diverse catalysts with recurrent features.
Modulation of substrate and cofactor reactivity and exact positioning of the substrate are key elements in the mode of action of these enzymes. Expand
The possible role of matrix metalloproteinase (MMP)-2 and MMP-9 in cancer, e.g. acute leukemia.
The role for MMPs and MMP-inhibition in cancer with special focus on acute leukemia is discussed and the mechanisms underlying M MP-expression in cancer have to be further elucidated. Expand
Identification of a Baeyer–Villiger monooxygenase sequence motif
Using newly characterized BVMO sequences, a BV MO‐identifying sequence motif is uncovered: FXGXXXHXXXW(P/D). Expand
Monooxygenases as biocatalysts: Classification, mechanistic aspects and biotechnological applications.
An exclusive overview of known monooxygenases is presented, based on the type of cofactor that these enzymes require, which includes not only the cytochrome P450 and flavin-dependent mono oxygengenases, but also enzymes that utilize pterin, metal ions, or no cofactor at all. Expand
Baeyer-Villiger monooxygenases, an emerging family of flavin-dependent biocatalysts
Baeyer-Villiger monooxygenases (BVMOs) are flavoenzymes that catalyze a remarkably wide variety of oxidative reactions such as regio- and enantioselective Baeyer-Villiger oxidations andExpand
Structures of Michaelis and product complexes of plant cytokinin dehydrogenase: implications for flavoenzyme catalysis.
The crystal structure of Zea mays cytokinin dehydrogenase displays the same two-domain topology of the flavoenzymes of the vanillyl-alcohol oxidase family but its active site cannot be related to that of any other family member. Expand
Halohydrin Dehalogenases Are Structurally and Mechanistically Related to Short-Chain Dehydrogenases/Reductases
A site-directed mutagenesis study, with HheC as a model enzyme, supports a mechanism for halohydrin dehalogenases in which the conserved Tyr145 acts as a catalytic base and Ser132 is involved in substrate binding, since it does not involve a covalent enzyme-substrate intermediate. Expand
Bacterial enzymes involved in lignin degradation.
An overview of recent advances in the identification and use of bacterial enzymes acting on lignin or lignIn-derived products is provided, including DyP-type peroxidases and laccases. Expand