Sie sind hier: Startseite Prof. (em.) Dr. R. … Publications bacterial nicotine catabolism

bacterial nicotine catabolism

Hritcu L., Stefan M., Brandsch R and Mihasan M. (2015) Enhanced behavioral response by decreasing brain oxidative stress to 6-hydroxy-L-nicotine in Alzheiner’s disease rat model. Neuroscience Letters 591: 41 - 47

Mihasan M. and Brandsch R. (2013) pAO1 of Arthrobacter nicotinovorans and the spread of catabolic traits by horizontal gene transfer in Gram-positive soil bacteria. J Mol Evol 77: 22-30

 
Hritcu L., Stefan M., Brandsch R. and Mihasan M. (2013) 6-Hydroxy-L-nicotine from Arthrobacter nicotinovorans sustain spatial memory formation by decreasing brain oxidative stress in rats. J Physiol Biochem 69: 25-34
 
Cobzaru C., Ganas P., Mihasan M., Schleberger P., Brandsch R. (2011) Homologous gene clusters of nicotine catabolism, including a new ω-amidase for α-ketoglutaramate, in species of three genera of Gram-positive bacteria. Res Microbiol 162: 285-291
 
Mihasan M., Artenie V., Brandsch R . (2010) Cloning and purification of a tetrameric oxidoreductase from Arthrobacter nicotinovorans pAO1. An. Stiin.Univ. “A. I. Cuza” TOM XI: 1-6
 
Ganas P. and Brandsch R. (2009) Uptake of L-nicotine and of 6-hydroxy-L-nicotine by Arthrobacter nicotinovorans and by Escherichia coli is mediated by facilitated diffusion and not by passive diffusion or active transport. Microbiology 155: 1866-1877
 
Ganas P., Sachelaru P., Mihasan M., Igloi G. L., Brandsch R. (2008) Two closely related pathways of nicotine catabolism in Arthrobacter nicotinovorans and Nocardioides sp. strain JS614. Arch Microbiol 189:511-7
 
Ganas P., Mihasan M., Igloi G. L., Brandsch R. (2007) A two-component small multidrug resistance pump functions as a metabolic valve during nicotine catabolism by Arthrobacter nicotinovorans. Microbiology 153:1546-55
 
Mihasan M., Chiribau C. B., Friedrich T., Artenie V., Brandsch R. (2007) An NAD(P)H-nicotine blue oxidoreductase is part of the nicotine regulon and may protect Arthrobacter nicotinovorans from oxidative stress during nicotine catabolism. Appl Environ Microbiol 73:2479-85
 
Schleberger C., Sachelaru P., Brandsch R., Schulz G. E. (2007) Structure and action of a C-C bond cleaving alpha/beta-hydrolase involved in nicotine degradation. J Mol Biol 367:409-18
 
Sachelaru P., Schiltz E., Brandsch R. (2006) A functional mobA gene for molybdopterin cytosine dinucleotide cofactor biosynthesis is required for activity and holoenzyme assembly of the heterotrimeric nicotine dehydrogenases of Arthrobacter nicotinovorans. Appl Environ Microbiol 72:5126-31
 
Chiribau C. B., Mihasan M., Ganas P., Igloi G. L., Artenie V., Brandsch R. (2006) Final steps in the catabolism of nicotine. FEBS J 273:1528-36
 
Sandu C., Chiribau C. B., Sachelaru P., Brandsch R. (2005) Plasmids for nicotine-dependent and -independent gene expression in Arthrobacter nicotinovorans and other arthrobacter species. Appl Environ Microbiol 71:8920-4
 
Sachelaru P., Schiltz E., Igloi G. L., Brandsch R. (2005) An alpha/beta-fold C--C bond hydrolase is involved in a central step of nicotine catabolism by Arthrobacter nicotinovorans. J Bacteriol 187:8516-9
 
Chiribau C. B., Sandu C , Igloi G. L., Brandsch R. (2005) Characterization of PmfR, the transcriptional activator of the pAO1-borne purU-mabO-folD operon of Arthrobacter nicotinovorans. J Bacteriol 187:3062-70
 
Chiribau C. B., Sandu C., Fraaije M., Schiltz E., Brandsch R. (2004) A novel gamma-N-methylaminobutyrate demethylating oxidase involved in catabolism of the tobacco alkaloid nicotine by Arthrobacter nicotinovorans pAO1. Eur J Biochem 271:4677-84
 
Sandu C., Chiribau C. B., Brandsch R. (2003) Characterization of HdnoR, the transcriptional repressor of the 6-hydroxy-D-nicotine oxidase gene of Arthrobacter nicotinovorans pAO1, and its DNA-binding activity in response to L- and D-nicotine Derivatives. J Biol Chem. 278:51307-15
 
Sandu C. and Brandsch R. (2002) Evidence for MoeA-dependent formation of the molybdenum cofactor from molybdate and molybdopterin in Escherichia coli. Arch Microbiol. 178:465-70
 
Sandu C, Brandsch R. (2002) Functional analysis of the Escherichia coli molybdopterin cofactor biosynthesis protein MoeA by site-directed mutagenesis. Biol Chem 383(2):319-23
 
Baitsch D., Sandu C., Brandsch R., Igloi G. L. (2001) Gene cluster on pAO1 of Arthrobacter nicotinovorans involved in degradation of the plant alkaloid nicotine: cloning, purification, and characterization of 2,6-dihydroxypyridine 3-hydroxylase. J Bacteriol 183:5262-7
 
Sandu C., Nick P., Hess D., Schiltz E., Garrow T. A., Brandsch R. (2000) Association of betaine-homocysteine S-methyltransferase with microtubules. Biol Chem 381:619-622
 
Menéndez C., Otto A., Igloi G., Nick P., Brandsch R., Schubach B., Böttcher B., Brandsch R. (1997) Molybdate-uptake genes and molybdopterin-biosynthesis genes on a bacterial plasmid--characterization of MoeA as a filament-forming protein with adenosinetriphosphatase activity. Eur J Biochem 250:524-31
 
Grether-Beck S., Igloi G. L., Pust S., Schilz E., Decker K., Brandsch R. (1994) Structural analysis and molybdenum-dependent expression of the pAO1-encoded nicotine dehydrogenase genes of Arthrobacter nicotinovorans. Mol Microbiol 13:929-936
 
Bernauer H., Mauch L., Brandsch R. (1992) Interaction of the regulatory protein NicR1 with the promoter region of the pAO1-encoded 6-hydroxy-D-nicotine oxidase gene of Arthrobacter oxidans. Mol Microbiol 6:1809-20
 
Mauch L., Bichler V., Brandsch R. (1990) Functional analysis of the 5' regulatory region and the UUG translation initiation codon of the Arthrobacter oxidans 6-hydroxy-D-nicotine oxidase gene. Mol Gen Genet 221:427-34
 
Brandsch R., Hinkkanen A. E., Mauch L., Nagursky H., Decker K. (1987) 6-Hydroxy-D-nicotine oxidase of Arthrobacter oxidans. Gene structure of the flavoenzyme and its relationship to 6-hydroxy-L-nicotine oxidase. Eur J Biochem 167:315-20
 
 
Brandsch R. and Decker K. (1982) The effect of gyrase inhibitors and cyclic AMP on induction and glucose repression of the 6-hydroxy-nicotine oxidases in Arthrobacter oxidans. Arch Microbiol 133:274-7