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autoflavinylation (6HDNO; DMGDH)

Hritcu L, Stefan M, Brandsch R, Mihasan M. (2015) Enhanced behavioral response by decreasing brain oxidative stress to 6-hydroxy-l-nicotine in Alzheimer's disease rat model. Neurosci Lett. 591:41-7.

Giancaspero TA, Colella M, Brizio C, Difonzo G, Fiorino GM, Leone P, Brandsch R, Bonomi F, Iametti S, Barile M. (2015) Remaining challenges in cellular flavin cofactor homeostasis and flavoprotein biogenesis. Front. Chem. 30: 1-14


Brizio C., Brandsch R., Douka M., Wait R., Barile M. (2008) The purified recombinant precursor of rat mitochondrial dimethylglycine dehydrogenase binds FAD via an autocatalytic reaction. Int J Biol Macromol 42:455-462

Brizio C., Brandsch R., Bufano D., Pochini L., Indiveri C., Barile M. (2004) Over-expression in Escherichia coli, functional characterization and refolding of rat dimethylglycine dehydrogenase. Protein Expr Purif. 37:434-42
Brizio C., Barile M., Brandsch R. (2002) Flavinylation of the precursor of mitochondrial dimethylglycine dehydrogenase by intact and solubilised mitochondria. FEBS Lett 522:141-146
Brizio C., Otto A., Brandsch R., Passarella S., Barile M. (2000) A protein factor of rat liver mitochondrial matrix involved in flavinylation of dimethylglycine dehydrogenase. Eur J Biochem 267:4346-54
Bergeron F., Otto A., Blache P., Day R., Denoroy L., Brandsch R., Bataille D. (1998) Molecular cloning and tissue distribution of rat sarcosine dehydrogenase. Eur J Biochem 257:556-61
Stoltz M. and Brandsch R. (1998) The conformational change induced by FAD in covalently flavinylated 6-hydroxy-D-nicotine oxidase does not require (8alpha)FAD-(N3)histidyl bond formation. J Biochem 123:445-9
Stoltz M., Rassow J., Bückmann A. F., Brandsch R. (1996) Covalent attachment of FAD derivatives to a fusion protein consisting of 6-hydroxy-D-nicotine oxidase and a mitochondrial presequence. Folding, enzyme activity, and import of the modified protein into yeast mitochondria. J Biol Chem 271:25208-12
Stoltz M., Henninger H. P., Brandsch R. (1996) The design of an alternative, covalently flavinylated 6-hydroxy-D-nicotine oxidase by replacing the FAD-binding histidine by cysteine and reconstitution of the holoenzyme with 8-(methylsulfonyl)FAD. FEBS Lett. 386:194-6
Otto A., Stoltz M., Sailer H. P., Brandsch R. (1996) Biogenesis of the covalently flavinylated mitochondrial enzyme dimethylglycine dehydrogenase. J Biol Chem 271:9823-9
Stoltz M., Rysavy P., Kalousek F., Brandsch R. (1995) Folding, flavinylation, and mitochondrial import of 6-hydroxy-D-nicotine oxidase fused to the presequence of rat dimethylglycine dehydrogenase. J Biol Chem 270:8016-22
Lang H., Minaian K., Freudenberg N., Hoffmann R., Brandsch R. (1994) Tissue specificity of rat mitochondrial dimethylglycine dehydrogenase expression. Biochem J 299:393-8
Brandsch R., Bichler V., Mauch L., Decker K. (1993) Cysteine to serine replacements in 6-hydroxy-D-nicotine oxidase. Consequences for enzyme activity, cofactor incorporation, and formation of high molecular weight protein complexes with molecular chaperones (GroEL). J Biol Chem 268:12724-9
Brandsch R., Bichler V., Schmidt M., Buchner J. (1992) GroE dependence of refolding and holoenzyme formation of 6-hydroxy-D-nicotine oxidase. J Biol Chem 267:20844-20849
Brandsch R. and Bichler V. (1991) Autoflavinylation of apo6-hydroxy-D-nicotine oxidase. J Biol Chem 266:19056-62
Lang H., Polster M., Brandsch R. (1991) Rat liver dimethylglycine dehydrogenase. Flavinylation of the enzyme in hepatocytes in primary culture and characterization of a cDNA clone. Eur J Biochem. 198:793-9
Brandsch R. and Bichler V. 1990 Riboflavin-dependent expression of flavoenzymes of the nicotine regulon of Arthrobacter oxidans. Biochem J 270:673-8
Mauch L., Bichler V., Brandsch R. (1990) Lysine can replace arginine 67 in the mediation of covalent attachment of FAD to histidine 71 of 6-hydroxy-D-nicotine oxidase. J Biol Chem 265:12761-2
Mauch L., Bichler V., Brandsch R. (1989) Site-directed mutagenesis of the FAD-binding histidine of 6-hydroxy-D-nicotine oxidase. Consequences on flavinylation and enzyme activity. FEBS Lett 257:86-8
Brandsch R., Hederstedt L. (1989) Expression and flavinylation of Arthrobacter oxydans 6-hydroxy-D-nicotine oxidase in Bacillus subtilis. J Gen Microbiol 135: 1093-1099
Brandsch R. and Bichler V. (1989) Covalent cofactor binding to flavoenzymes requires specific effectors. Eur J Biochem 182:125-8
Brandsch R., Bichler V, Krauss B. (1989) Binding of FAD to 6-hydroxy-D-nicotine oxidase apoenzyme prevents degradation of the holoenzyme. Biochem J. 258:187-92
Nagursky H., Bichler V., Brandsch R. (1988) Phosphoenolpyruvate-dependent flavinylation of 6-hydroxy-D-nicotine oxidase. Eur J Biochem 177:319-25
Brandsch R. and Bichler V. (1987) Covalent flavinylation of 6-hydroxy-D-nicotine oxidase involves an energy-requiring process. FEBS Lett. 224:121-4
Brandsch R., Bichler V., Nagursky H. (1987) Covalent flavinylation of 6-hydroxy-D-nicotine oxidase analyzed by partial deletions of the gene. Eur J Biochem. 165:559-64
Brandsch R. and Bichler V. (1986) Studies in vitro on the flavinylation of 6-hydroxy-D-nicotine oxidase. Eur J Biochem 160:285-9
Brandsch R. and Bichler V. (1985) In vivo and in vitro expression of the 6-hydroxy-D-nicotine oxidase gene of Arthrobacter oxidans, cloned into Escherichia coli, as an enzymatically active, covalently flavinylated polypeptide. FEBS Lett 192:204-8
Swafford JR, Reeves HC, Brandsch R. (1985) Localization of the enantiozymes of 6-hydroxy-nicotine oxidase in Arthrobacter oxidans by electron immunochemistry. J Bacteriol 163:792-795