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Flavoproteine
ββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββ
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Flavoproteine (Flavinenzyme, Flavoenzyme) sind eine in Tieren, Pflanzen und Mikroorganismen weit verbreitete Gruppe von Proteinen bzw. Oxidoreduktasen, die als Kofaktor Flavinnukleotide (Flavinadenindinukleotid (FAD), Flavinmononukleotid (FMN)) enthalten.cite-ref-1[1]
Es handelt sich um Enzyme, die Redox-Reaktionen katalysieren, wobei Flavin als ElektronenΓΌbertrΓ€ger dient, der umkehrbar oxidiert und reduziert werden kann.
Flavoproteine sind grundlegend fΓΌr alle VorgΓ€nge der Zellatmung, da sie an den entsprechenden Elektronentransportketten beteiligt sind.
Beispiele sind unter anderem die Succinat-Dehydrogenase und die Glucose-Oxidase.
Contents
β’ Siehe auch
β’ Literatur
β’ Einzelnachweise
ββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββββ
Siehe auch
Literatur
β’ V. Massey: The chemical and biological versatility of riboflavin. In: Biochemical Society transactions. Band 28, Nummer 4, 2000, S. 283β296, ISSN 0300-5127. PMID 10961912.
β’ H. Theorell: Preparation in pure state of the effect group of yellow enzymes. In: Biochemische Zeitschrift. 275, 1935, S. 344β346.
β’ O. Warburg, W. Christian: Isolation of the prosthetic group of the amino acid oxydase. In: Biochemische Zeitschrift. 298, 1938, S. 150β168.
β’ S. M. H. Christie, G. W. Kenner, A. R. Todd: NUCLEOTIDES .25. A SYNTHESIS OF FLAVIN ADENINE DINUCLEOTIDE. In: Journal of the Chemical Society. 1954, S. 46β52.
β’ T. Kupke, S. Stevanovic, H. G. Sahl, F. Gotz: Purification and characterization of EpiD, a flavoprotein involved in the biosynthesis of the lantibiotic epidermin. In: J. Bacteriol. 174 (16), Aug 1992, S. 5354β5361. PMC 206373 (freier Volltext). PMID 1644762.
β’ R. A. Daniel, J. Errington: Cloning, DNA sequence, functional analysis and transcriptional regulation of the genes encoding dipicolinic acid synthetase required for sporulation in Bacillus subtilis. In: J. Mol. Biol. 232 (2), Jul 1993, S. 468β483. doi:10.1006/jmbi.1993.1403. PMID 8345520.
β’ M. Clausen, C. J. Lamb, R. Megnet, P. W. Doerner: PAD1 encodes phenylacrylic acid decarboxylase which confers resistance to cinnamic acid in Saccharomyces cerevisiae. In: Gene. 142 (1), Mai 1994, S. 107β112. doi:10.1016/0378-1119(94)90363-8. PMID 8181743.
Einzelnachweise