Skip to main content
Log in

The effect of gyrase inhibitors and cyclic AMP on induction and glucose repression of the 6-hydroxy-nicotine oxidases in Arthrobacter oxidans

  • Original Papers
  • Published:
Archives of Microbiology Aims and scope Submit manuscript

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.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Similar content being viewed by others

Abbreviations

6-HDNO:

6-hydroxy-D-nicotine oxidase

6-HLNO:

6-hydroxy-L-nicotine oxidase

cAMP:

cyclic 3′,5′-adenosine monophosphate

Enzymes:

Adenylate cyclase

ATP:

pyrophosphate-lyase (cyclizing) (EC 4.6.1.1)

cAMP-phosphodiesterase:

3′:5′-cyclic-nucleotide 5′-nucleotido-hydrolase (EC 3.1.4.17)

DNA gyrase:

DNA topoisomerase II (EC 5.99)

DNA polymerase:

deoxynucleosidetriphosphate: DNA desoxynucleotidyl-transferase (EC 2.7.7.7)

6-hydroxy-L-nicotine oxidase:

6-hydroxy-L-nicotine: oxygen oxidoreductase (EC 1.5.3.5)

6-hydroxy-D-nicotine oxidase:

6-hydroxy-D-nicotine: oxygen oxidoreductase (EC 1.5.3.6)

β-lactamase:

penicillin amido-β-lactamhydrolase (EC 3.5.2.6)

nicotine dehydrogenase:

nicotine: (acceptor)6-oxidoreductase (hydroxylating) (EC 1.5.99.4)

References

  • Botsford JW (1981) Cyclic nucleotides in procaryotes. Microbiol Rev 45:640–642

    Google Scholar 

  • Brühmüller M, Schimz A, Messmer L, Decker K (1975) Covalently bound FAD in D-6-hydroxynicotine oxidase. Immunological studies on D- and L-6-hydroxynicotine oxidase. Evidence for a D-enzyme precursor. J. Biol Chem 7747-7751

  • Cozarelli NR (1980) DNA gyrase and the supercoiling of DNA. Science 207:953–960

    Google Scholar 

  • Decker K (1976) Structure and synthesis of a flavoprotein with covalently bound FAD. Trends in Biochem Sciences 1:184–185

    Google Scholar 

  • Decker K, Dai VD, Möhler H, Brühmüller M (1972) D- and L-6-hydroxynicotine oxidase, enantiozymes of Arthrobacter oxidans. Z. Naturforsch 27b:1072–1073

    Google Scholar 

  • Eberwein H, Gries FA, Decker K (1961) Über den Abbau des Nicotins durch Bakterienenzyme. II. Isolierung und Charakterisierung eines nicotinabbauenden Bodenbakteriums. Hoppe-Seyler's Z Physiol Chem 323:236–248

    Google Scholar 

  • Gloger M, Decker K (1969) Zum Mechanismus der Induktion nicotinabbauender Enzyme in Arthrobacter oxydans. Z Naturforsch 24b:1016–1025

    Google Scholar 

  • Gómez-Eichelmann MC (1981) Effect of nalidixic acid and novobiocin on pBR 322 minicells. J Bacteriol 14:745–752

    Google Scholar 

  • Hamilton RW, Kolenbrander PE (1978) Regulation of cyclic AMP levels in Arthrobacter crystallopoietes and a morphogenetic mutant. J Bacteriol 134:1064–1073

    Google Scholar 

  • Krulwich TA, Ensign JC (1969) Alteration of glucose metabolism of Arthrobacter crystallopoietes by compounds which induce sphere-torod morphogenesis. J Bacteriol 97:526–534

    Google Scholar 

  • Liu LF, Wang JC (1978) Micrococcus luteus DNA gyrase: active components and a model for its supercoiling of DNA. Proc Natl Acad Sci USA 75:2098–2102

    Google Scholar 

  • Möhler H, Brühmüller M, Decker K (1972) Covalently bound flavin in D-6-hydroxynicotine oxidase. Identification of the 8α-(N3-histidyl)-riboflavin-linkage between FAD and the apoenzyme. Eur J Biochem 29:152–155

    Google Scholar 

  • Ostrowski J, Hulanicka D (1981) Effect of DNA gyrase inhibitors on gene expression of the cysteine regulon. Mol Gen Gent 181:363–366

    Google Scholar 

  • Phillips A, Mulfinger LM (1981) Cyclic adenosine 3′, 5′-monophosphate levels in Pseudomonas putida and Pseudomonas aeruginosa during induction and carbon catabolite repression of histidase synthesis. J Bacteriol 145:1286–1292

    Google Scholar 

  • Reeves HC, Messmer L, Decker K (1976) Induction of D-6-hydroxynicotine oxidase in resting cells of Arthrobacter oxidans. Arch Microbiol 111:111–116

    Google Scholar 

  • Sanzey B (1979) Modulation of gene expression by drugs affecting deoxyribonucleic acid gyrase. J Bacteriol 138:40–47

    Google Scholar 

  • Schechter LS, Gold Z, Krulwich TA (1972) Enzyme induction and repression in Arthrobacter crystallopoietes. Arch Microbiol 85: 280–293

    Google Scholar 

  • Siegel LS, Hylmon PB, Phibbs Jr PV (1977) Cyclic adenosine 3′,5′-monophosphate levels and activities of adenylate cyclase and cyclic adenosine 3′,5′-monophosphate phosphodiesterase in Pseudomonas and Bacteroides. J. Bacteriol 129:87–96

    Google Scholar 

  • Smith CL, Kubo M, Imamoto F (1978) Promotor-specific inhibition of transcription by antibodies which act on DNA gyrase. Nature (London) 275:420–423

    Google Scholar 

  • Sugino A, Bott KF (1980) Bacillus subtilis deoxyribonucleic acid gyrase. J Bacteriol 141:1331–1339

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

Brandsch, R., Decker, K. 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, 274–277 (1982). https://doi.org/10.1007/BF00521289

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00521289

Key words

Navigation