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Crystal structures and inhibitor binding in the octameric flavoenzyme vanillyl-alcohol oxidase: the shape of the active-site cavity controls substrate specificity.

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BACKGROUND Lignin degradation leads to the formation of a broad spectrum of aromatic molecules that can be used by various fungal micro-organisms as their sole source of carbon. When grown on phenolic compounds, Penicillium simplicissimum induces the strong impression of a flavin-containing

Inversion of stereospecificity of vanillyl-alcohol oxidase.

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Vanillyl-alcohol oxidase (VAO) is the prototype of a newly recognized family of structurally related oxidoreductases sharing a conserved FAD-binding domain. The active site of VAO is formed by a cavity where the enzyme is able to catalyze many reactions with phenolic substrates. Among these

Shorter and modular synthesis of hemicryptophane-tren derivatives.

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Hemicryptophanes are host molecules with many applications as supramolecular catalysts or in ion selective recognition. A very convenient and efficient modular approach for the synthesis of hemicryptophane-tren (tren, tris(2-aminoethyl)-amine) derivatives has been developed. For instance,

Structural analysis of the catalytic mechanism and stereoselectivity in Streptomyces coelicolor alditol oxidase.

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Alditol oxidase (AldO) from Streptomyces coelicolor A3(2) is a soluble monomeric flavin-dependent oxidase that performs selective oxidation of the terminal primary hydroxyl group of several alditols. Here, we report the crystal structure of the recombinant enzyme in its native state and in complex

Biocatalytic Properties and Structural Analysis of Eugenol Oxidase from Rhodococcus jostii RHA1: A Versatile Oxidative Biocatalyst.

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Eugenol oxidase (EUGO) from Rhodococcus jostii RHA1 had previously been shown to convert only a limited set of phenolic compounds. In this study, we have explored the biocatalytic potential of this flavoprotein oxidase, resulting in a broadened substrate scope and a deeper insight into its

Synomone or kairomone?--Bulbophyllum apertum flower releases raspberry ketone to attract Bactrocera fruit flies.

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Bulbophyllum apertum flower (Orchidaceae) releases raspberry ketone (RK) in its fragrance, which attracts males of several fruit fly species belonging to the genus Bactrocera. Besides RK as a major component, the flower contains smaller amounts of 4-(4-hydroxylphenyl)-2-butanol, plus two minor

Rationally engineered flavin-dependent oxidase reveals steric control of dioxygen reduction.

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The ability of flavoenzymes to reduce dioxygen varies greatly, and is controlled by the protein environment, which may cause either a rapid reaction (oxidases) or a sluggish reaction (dehydrogenases). Previously, a 'gatekeeper' amino acid residue was identified that controls the reactivity to

Structures of Michaelis and product complexes of plant cytokinin dehydrogenase: implications for flavoenzyme catalysis.

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Cytokinins form a diverse class of compounds that are essential for plant growth. Cytokinin dehydrogenase has a major role in the control of the levels of these plant hormones by catalysing their irreversible oxidation. The crystal structure of Zea mays cytokinin dehydrogenase displays the same

Crystal Structure of Alcohol Oxidase from Pichia pastoris.

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FAD-dependent alcohol oxidases (AOX) are key enzymes of methylotrophic organisms that can utilize lower primary alcohols as sole source of carbon and energy. Here we report the crystal structure analysis of the methanol oxidase AOX1 from Pichia pastoris. The crystallographic phase problem was solved

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