Flavoproteins of Known Three-Dimensional Structure
作者： R. H. Schirmer , G. E. Schulz
DOI: 10.1007/978-3-642-69467-7_5
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摘要: About 50 years ago FMN (Theorell 1935) and FAD (Warburg Christian 1938) were discovered as prosthetic groups of the old yellow enzyme D-amino acid oxidase, respectively. More than 100 flavoenzymes have been described in meantime (Dixon Webb 1979); for four them, structural data are known. These glycolate oxidase (Lind quist Branden 1980), an FMN-dependent which probably has a chain fold common with triose phosphate isomerase one domain pyruvate kinase, three FAD-dependent enzymes: ferredoxin-NADP+ reductase (Sheriff Herriott 1981; Karplus 1982) p-hydroxybenzoate hydroxylase (Wierenga et al. 1979; Wierenga 1982; Weijer glutathione (Schulz 1978; Thieme Pai Schulz 1983). The last mentioned two enzymes analyzed atomic detail. In our presentation, we shall first describe we11-understood flavoenzyme then compare its structure hydroxylase. Whenever possible include aspects other flavoproteins discussion.
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