Literature DB >> 5573731

Induction specificity and catabolite repression of the early enzymes in camphor degradation by Pseudomonas putida.

R A Hartline, I C Gunsalus.   

Abstract

The ability of bornane and substituted bornanes to induce the early enzymes for d(+)-camphor degradation and control of these enzymes by catabolite repression were studied in a strain of a Pseudomonas putida. Bornane and 20 substituted bornane compounds showed induction. Of these 21 compounds, bornane and 8 of the substituted bornanes provided induction without supporting growth. Oxygen, but not nitrogen, enhanced the inductive potency of the unsubstituted bornane ring. All bornanedione isomers caused induction, and those with substituents on each of the three consecutive carbon atoms, including the methyl group at the bridgehead carbon, showed induction without supporting growth. Although it was not possible to obtain experimental data for a case of absolute gratuitous induction by compounds not supporting growth, indirect evidence in support of gratuitous induction is presented. It is proposed that the ability of P. putida to tolerate the unusually high degree of possible gratuitous induction observed for camphor catabolism may be related to the infrequent occurrence of bicyclic ring structures in nature. Survival of an organism with a broad specificity for gratuitous induction is discussed. Glucose and succinate, but not glutamate, produced catabolite repression of the early camphor-degrading enzymes. Pathway enzymes differ in their degree of sensitivity to succinate-provoked catabolite repression. The ability of a compound to produce catabolite repression is not, however, directly related to the duration of the lag period (diauxic lag) between growth on camphor and growth on the repressing compound.

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Year:  1971        PMID: 5573731      PMCID: PMC285118          DOI: 10.1128/jb.106.2.468-478.1971

Source DB:  PubMed          Journal:  J Bacteriol        ISSN: 0021-9193            Impact factor:   3.490


  11 in total

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Authors:  J MONOD; G COHEN-BAZIRE; M COHN
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3.  Mixed function oxidation. IV. An induced methylene hydroxylase in camphor oxidation.

Authors:  J Hedegaard; I C Gunsalus
Journal:  J Biol Chem       Date:  1965-10       Impact factor: 5.157

4.  Monoxygenases. VII. Camphor ketolactonase I and the role of three protein components.

Authors:  C A Yu; I C Gunsalus
Journal:  J Biol Chem       Date:  1969-11-25       Impact factor: 5.157

5.  The ferroprotein component of a methylene hydroxylase.

Authors:  D W Cushman; R L Tsai; I C Gunsalus
Journal:  Biochem Biophys Res Commun       Date:  1967-03-09       Impact factor: 3.575

6.  Mixed function oxidation. V. Flavin interaction with a reduced diphosphopyridine nucleotide dehydrogenase, one of the enzymes participating in camphor lactonization.

Authors:  P W Trudgill; R DuBus; I C Gunsalus
Journal:  J Biol Chem       Date:  1966-03-10       Impact factor: 5.157

7.  Enzyme induction and repression in anabolic and catabolic pathways.

Authors:  I C Gunsalus; A U Bertland; L A Jacobson
Journal:  Arch Mikrobiol       Date:  1967

8.  The conversion of catechol and protocatechuate to beta-ketoadipate by Pseudomonas putida. IV. Regulation.

Authors:  L N Ornston
Journal:  J Biol Chem       Date:  1966-08-25       Impact factor: 5.157

9.  The aerobic pseudomonads: a taxonomic study.

Authors:  R Y Stanier; N J Palleroni; M Doudoroff
Journal:  J Gen Microbiol       Date:  1966-05

10.  Synthesis of the enzymes of the mandelate pathway by Pseudomonas putida. I. Synthesis of enzymes by the wild type.

Authors:  G D Hegeman
Journal:  J Bacteriol       Date:  1966-03       Impact factor: 3.490

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  14 in total

1.  camR, a negative regulator locus of the cytochrome P-450cam hydroxylase operon.

Authors:  H Koga; H Aramaki; E Yamaguchi; K Takeuchi; T Horiuchi; I C Gunsalus
Journal:  J Bacteriol       Date:  1986-06       Impact factor: 3.490

Review 2.  Microbial catabolism, the carbon cycle and environmental pollution.

Authors:  S Dagley
Journal:  Naturwissenschaften       Date:  1978-02

3.  Unusual spectroscopic and ligand binding properties of the cytochrome P450-flavodoxin fusion enzyme XplA.

Authors:  Soi H Bui; Kirsty J McLean; Myles R Cheesman; Justin M Bradley; Stephen E J Rigby; Colin W Levy; David Leys; Andrew W Munro
Journal:  J Biol Chem       Date:  2012-04-12       Impact factor: 5.157

4.  The PalkBFGHJKL promoter is under carbon catabolite repression control in Pseudomonas oleovorans but not in Escherichia coli alk+ recombinants.

Authors:  I E Staijen; R Marcionelli; B Witholt
Journal:  J Bacteriol       Date:  1999-03       Impact factor: 3.490

5.  Transcription of the cam operon and camR genes in Pseudomonas putida PpG1.

Authors:  M Fujita; H Aramaki; T Horiuchi; A Amemura
Journal:  J Bacteriol       Date:  1993-11       Impact factor: 3.490

6.  Evidence for autoregulation of camR, which encodes a repressor for the cytochrome P-450cam hydroxylase operon on the Pseudomonas putida CAM plasmid.

Authors:  H Aramaki; Y Sagara; M Hosoi; T Horiuchi
Journal:  J Bacteriol       Date:  1993-12       Impact factor: 3.490

7.  Camphor revisited: involvement of a unique monooxygenase in metabolism of 2-oxo-delta 3-4,5,5-trimethylcyclopentenylacetic acid by Pseudomonas putida.

Authors:  H J Ougham; D G Taylor; P W Trudgill
Journal:  J Bacteriol       Date:  1983-01       Impact factor: 3.490

8.  Purification and characterization of a cam repressor (CamR) for the cytochrome P-450cam hydroxylase operon on the Pseudomonas putida CAM plasmid.

Authors:  H Aramaki; Y Sagara; H Kabata; N Shimamoto; T Horiuchi
Journal:  J Bacteriol       Date:  1995-06       Impact factor: 3.490

9.  Catabolite repression of the toluene degradation pathway in Pseudomonas putida harboring pWW0 under various conditions of nutrient limitation in chemostat culture.

Authors:  W A Duetz; S Marqués; B Wind; J L Ramos; J G van Andel
Journal:  Appl Environ Microbiol       Date:  1996-02       Impact factor: 4.792

10.  Carbon source-dependent inhibition of xyl operon expression of the Pseudomonas putida TOL plasmid.

Authors:  A Holtel; S Marqués; I Möhler; U Jakubzik; K N Timmis
Journal:  J Bacteriol       Date:  1994-03       Impact factor: 3.490

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