Primary citation
Title Crystal structures and inhibitor binding in the octameric flavoenzyme vanillyl-alcohol oxidase: the shape of the active-site cavity controls substrate specificity.
Authors Mattevi,; Fraaije,; Mozzarelli,; Olivi,; Coda,; van Berkel,
Journal STRUCTUREsearch vol:5, pag:907-920 (1997), Identifiers: PubMed ID (9261083)search DOI (10.1016/S0969-2126(97)00245-1)
Abstract 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 vanillyl-alcohol oxidase (VAO). The enzyme catalyses the oxidation of a vast array of substrates, ranging from aromatic amines to 4-alkyphenols. VAO is a member of a novel class of widely distributed oxidoreductases, which use flavin adenine dinucleotide (FAD) as a cofactor covalently bound to the protein. We have carried out the determination of the structure of VAO in order to shed light on the most interesting features of these novel oxidoreductases, such as the functional significance of covalent flavinylation and the mechanism of catalysis.
MeSH terms Alcohol Oxidoreductasessearch, Binding Sitessearch, Bindingsearch, Competitivesearch, Catalysissearch, Computer Graphicssearch, Cresolssearch, Crystallizationsearch, Crystallographysearch, X-Raysearch, Enzyme Inhibitorssearch, Eugenolsearch, Flavin-Adenine Dinucleotidesearch, Molecular Structuresearch, Protein Bindingsearch, Protein Conformationsearch, Substrate Specificitysearch
Other entries described in this publication 1ahu, 1ahv, 2vao, 1ahz