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  • 1
    Monograph available for loan
    Monograph available for loan
    München [u.a.] : Hanser
    Call number: M 01.0346
    Type of Medium: Monograph available for loan
    Pages: 706 S. + 1 CD-ROM
    Edition: 15., neu bearb. und erw. Aufl.
    ISBN: 3446215255
    Classification:
    C.5.2.
    Location: Upper compact magazine
    Branch Library: GFZ Library
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  • 2
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 111 (1976), S. 111-115 
    ISSN: 1432-072X
    Keywords: Inducible enzyme ; Nicotine ; Flavin adenine dinucleotide ; Apoprotein ; Enantiozyme ; Resting cells
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Resting cell suspensions of Arthrobacter oxidans were shown to synthesize the inducible enantiozyme, d-6-hydroxynicotine oxidase, in the presence of d-nicotine or d-6-hydroxynicotine. The corresponding l-enantiomers, as well as γ-methylaminopropyl-(6-OH-pyridyl-3)-ketone, which is the product of the reaction catalyzed by the enzyme, were ineffective as inducers. l-6-Hydroxynicotine inhibited induction by d-nicotine and d-6-hydroxynicotine while l-nicotine inhibited induction by d-6-hydroxynicotine and had no effect on induction by d-nicotine. Enzyme induction was also found to be inhibited by glucose, 2-deoxy-d-glucose and by several intermediates of the tricarboxylic acid cycle. An absolute requirement for protein synthesis and for oxygen was also demonstrated to be necessary for the reactions involved in the covalent attachment of flavin adenine dinucleotide to pre-existing precursor protein to yield the catalytically active d-6-hydroxynicotine oxidase.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 119 (1978), S. 65-70 
    ISSN: 1432-072X
    Keywords: Biosynthesis of flavoproteins ; Regulation of translation ; Accumulation of mRNA ; Differential effects of transcription inhibitors ; 6-Hydroxy-d-nicotine oxidase ; 6-Hydroxy-l-nicotine oxidase ; Covalently bound FAD ; Holoenzyme synthesis ; Riboflavin-requiring mutants of Arthrobacter oxidans
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The biosynthesis of two flavoproteins, 6-hydroxy-d-nicotine oxidase with covalently bound FAD and 6-hydroxy-l-nicotine oxidase containing non-covalently bound FAD, was studied in wild-type cells and in a riboflavin-requiring mutant of Arthrobacter oxidans. In the mutant cells, the rate of synthesis and the maximal activity level of both enzymes after induction by nicotine depended on the amount of added riboflavin. The low rate of synthesis in the presence of 2 μM riboflavin could be enhanced during the induction phase by further addition of riboflavin (33 μM). Inhibitors of translation (chloramphenicol or streptomycin) completely blocked the synthesis of both flavoproteins. Inhibitors of transcription (rifamycin S or actinomycin D) stopped the synthesis of both enantiozymes in wild-type cells and in the mutant grown in the presence of a saturating supply of riboflavin (15 μM). Under conditions of restricted flavoprotein synthesis (2 μM riboflavin in the medium), however, the mutant cells continued to synthesize the enzyme for 2–3 h after the addition of the transcription inhibitors. It appears, that in these cells a rather stable m-RNA accumulated during riboflavin-limited flavoprotein synthesis. The dependence of the effect of transcription inhibitors on the extracellular supply of riboflavin suggests that the regulation of the synthesis of both flavoproteins occurs not only by control of gene expression (induction by nicotine), but also at the level of translation through the availability of FAD.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 130 (1981), S. 288-293 
    ISSN: 1432-072X
    Keywords: Clostridium kluyveri ; Acetyl-CoA content of C. kluyveri ; CoASH content of C. kluyveri ; Regulatory function of the acetyl-CoA/CoASH ratio ; Isotope assay of acetyl-CoA ; Quantitative determination of CoASH with 14C-N-ethyl-maleimide
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract CoASH and some of its acyl derivatives, especially acetyl-SCoA, occupy a central position in the energy metabolism of the anaerobic Clostridium kluyveri, both as intermediates and as regulatory effectors. The steady state concentrations of these compounds were determined in growing cultures of this organism using an anaerobic and fast deproteinization technique and radio isotope assays. Acetyl-SCoA was determined as [1-14C]citrate formed in the presence of [4-14C]oxaloacetate and citrate synthase; 0.49 μmol/g cell wet wt. were found CoASH, CoAS-SCoA after borohydride reduction, and total acyl derivatives of coenzyme A after hydrolysis of the thiol esters were converted to thioethers with [2,3-14C]N-ethylmaleimide and brought to radiochemical purity by chromatographic methods. While disulfides of coenzyme A were undetectable, 0.13 μmol CoASH and 1.17 μmol of total acyl-SCoA per g wet wt. were found. These data are consistent with the regulatory scheme of the energy metabolism of C. kluyveri previously proposed.
    Type of Medium: Electronic Resource
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  • 6
    ISSN: 1432-072X
    Keywords: Arthrobacter oxidans ; cAMP ; Catabolite repression ; DNA gyrase ; Nalidixic acid ; Novobiocin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The induction by d,l-nicotine of the enantiozymes 6-hydroxy-L-nicotine oxidase and 6-hydroxy-D-nicotine oxidase in Archrobacter oxidans was differently affected by the inhibitors of Escherichia coli gyrase, novobiocin and nalidixic acid. These compounds inhibited 6-hydroxy-L-nicotine oxidase induction slightly, but led to an increase in the level of 6-hydroxy-D-nicotine oxidase activity. Furthermore, the specific repression by glucose of 6-hydroxy-D-nicotine oxidase synthesis was not abolished by the addition of cAMP but by that of novobiocin.
    Type of Medium: Electronic Resource
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  • 7
    ISSN: 1432-072X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Considerable behavioral differences were observed during growth of Clostridium kluyveri on ethanol-acetate and on crotonate media. The identity of the crotonate grown Clostridium with the ethanol grown Clostridium kluyveri was therefore established by three characteristic biosynthetic routes: 1. ribose is synthesized from CO2 and acetate via pyruvate, triose phosphate and a non-oxidative pentose phosphate pathway, 2. reduced one-carbon units are formed predominantly from CO2 and not from serine as usual, and 3. glutamate biogenesis follows an atypical stereochemical course.
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 132 (1982), S. 26-30 
    ISSN: 1432-072X
    Keywords: Arthrobacter oxidans ; 6-Hydroxy-l-nicotine oxidase ; Nicotine metabolism ; Plasmids
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The spontaneous loss byArthrobacter oxidans cells of the nicotine-degrading ability (Nic+) was 0.06%. It could be increased by treatment with plasmid-curing agents up to 8%. It was possible by conjugation to restore the Nic+ phenotype in such cured derivatives and to transfer the Nic+ character to Nic- Arthrobacter species. Plasmid DNA, 160 kb in size as judged by contour length measurements, could be isolated from cleared lysates ofA. oxidans cells by acridine yellow chromatography. Agarose gel electrophoresis of DNA isolated fromArthrobacter exconjugates revealed the occurrence of plasmid DNA within these strains; its mobility was similar to that of the plasmid DNA present inA. oxidans. Although the expression and inducibility of the transferred genes was poor in most of theArthrobacter species exconjugants, apparently authentic 6-hydroxy-l-nicotine oxidase could be identified in these cells after enrichment by an enzyme-specific chromatography.
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 116 (1978), S. 175-180 
    ISSN: 1432-072X
    Keywords: D-6-Hydroxynicotine oxidase ; Flavoprotein ; Amino acid analysis ; Peptide mapping ; Terminal amino acids
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract In Arthrobacter oxidans, an enzymatically inactive protein which is in a close biosynthetic relationship to the active D-6-hydroxynicotine oxidase and may serve as a precursor for its formation was purified and shown to be homogeneous by gel electrophoresis. It consists of one polypeptide chain of about the same molecular weight (50 000 daltons) as the active enzyme. The purified protein lacks the absorption in the visible range characteristic of flavoproteins. Amino acid analysis and peptide mapping yielded similar results for both proteins. They also share the same C-terminal amino acids,-lysinetyrosine; the N-terminal residue is serine in the case of D-6-hydroxynicotine oxidase while that of the coinduced protein was found to be blocked.
    Type of Medium: Electronic Resource
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  • 10
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 138 (1984), S. 15-17 
    ISSN: 1432-072X
    Keywords: Arthrobacter ; Nicotine degradation ; Plasmid
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A method for the extraction of the high molecular weight plasmid AO 1 from the gram-positive soil bacterium Arthrobacter oxidans is presented. Following digestion of this DNA with the restriction endonucleases Accl, Bam HI, Eco RI and Hind III, an average molecular mass of 157.8 kb was estimated. This value is in good agreement with the 160 kb size determined previously by electron microscopy (Brandsch et al. 1982). Using the same method, no plasmid DNA was found in strains of the genus Arthrobacter which do not degrade nicotine, e.g., A. albidus, A. globiformis and A. auricans.
    Type of Medium: Electronic Resource
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