Substrate interactions between toluene and methyltert-butyl ether (MTBE) during microbial degradation by Pseudomonas putida

2010 ◽  
Vol 30 (3) ◽  
pp. 278-283 ◽  
Author(s):  
S.G. Lee ◽  
D.J. Kim ◽  
J.W. Choi ◽  
S.H. Lee
Keyword(s):  
Pseudomonas Putida ◽  
Microbial Degradation ◽  
Butyl Ether ◽  
Substrate Interactions

Microbial degradation of the morphine alkaloids: identification of morphinone as an intermediate in the metabolism of morphine by Pseudomonas putida M10

1990 ◽  
Vol 154 (5) ◽  
pp. 465-470 ◽  
Author(s):  
Neil C. Bruce ◽  
Clare J. Wilmot ◽  
Keith N. Jordan ◽  
Anna E. Trebilcock ◽  
Lauren D. Gray Stephens ◽  
...  
Keyword(s):  
Pseudomonas Putida ◽  
Microbial Degradation ◽  
Morphine Alkaloids

scholarly journals Oxidation of Methyl tert-Butyl Ether by Alkane Hydroxylase in Dicyclopropylketone-Induced and n-Octane-Grown Pseudomonas putida GPo1

2004 ◽  
Vol 70 (8) ◽  
pp. 4544-4550 ◽  
Author(s):  
Christy A. Smith ◽  
Michael R. Hyman
Keyword(s):  
Pseudomonas Putida ◽  
Kinetic Studies ◽  
Butyl Alcohol ◽  
Amyl Alcohol ◽  
Methyl Tert Butyl Ether ◽  
Rich Medium ◽  
Hydroxylase Activity ◽  
Alkane Hydroxylase ◽  
Butyl Ether ◽  
Putative Mechanism

ABSTRACT The alkane hydroxylase enzyme system in Pseudomonas putida GPo1 has previously been reported to be unreactive toward the gasoline oxygenate methyl tert-butyl ether (MTBE). We have reexamined this finding by using cells of strain GPo1 grown in rich medium containing dicyclopropylketone (DCPK), a potent gratuitous inducer of alkane hydroxylase activity. Cells grown with DCPK oxidized MTBE and generated stoichiometric quantities of tert-butyl alcohol (TBA). Cells grown in the presence of DCPK also oxidized tert-amyl methyl ether but did not appear to oxidize either TBA, ethyl tert-butyl ether, or tert-amyl alcohol. Evidence linking MTBE oxidation to alkane hydroxylase activity was obtained through several approaches. First, no TBA production from MTBE was observed with cells of strain GPo1 grown on rich medium without DCPK. Second, no TBA production from MTBE was observed in DCPK-treated cells of P. putida GPo12, a strain that lacks the alkane-hydroxylase-encoding OCT plasmid. Third, all n-alkanes that support the growth of strain GPo1 inhibited MTBE oxidation by DCPK-treated cells. Fourth, two non-growth-supporting n-alkanes (propane and n-butane) inhibited MTBE oxidation in a saturable, concentration-dependent process. Fifth, 1,7-octadiyne, a putative mechanism-based inactivator of alkane hydroxylase, fully inhibited TBA production from MTBE. Sixth, MTBE-oxidizing activity was also observed in n-octane-grown cells. Kinetic studies with strain GPo1 grown on n-octane or rich medium with DCPK suggest that MTBE-oxidizing activity may have previously gone undetected in n-octane-grown cells because of the unusually high Ks value (20 to 40 mM) for MTBE.

scholarly journals Distribution of Camphor Monooxygenase Genes in Soil Bacteria

2015 ◽  
Vol 10 (2) ◽  
Author(s):  
N. Ngadiman ◽  
Hikaru Suenaga ◽  
Masatoshi Goto ◽  
Kensuke Furukawa
Keyword(s):  
Pseudomonas Putida ◽  
Microbial Degradation ◽  
Genomic Dna ◽  
Soil Bacteria ◽  
Southern Analysis ◽  
Bacterial Strains ◽  
Gene Distribution

In microbial degradation of camphor, the first step is oxidation by multiunit enzyme, camphormonooxygenase, encoded by cam genes (camA,B,C). Seven camphor-utilizing bacterial strains have been isolatedfrom soil at various locations. CamA,B,C genes of Pseudomonas putida strain PpG1 and strain GF2001 were used asprobes to explore their abundance in the camphor-utilizing bacteria. Southern analysis revealed that all of thecam genes of GF2001 could hybridize well to the SpeI-digested genomic DNA of strains tested, whereas PpG1 camgenes were not. This result suggested that the GF2001 type cam genes are widely distributed among the camphorutilizingstrains in the environment. Thus strain GF2001 and seven newly isolated strains share a commonevolutionary origin.Key words: Camphor monooxygenase genes, gene distribution, sail bacteria.

Biotransformation of dibenzothiophene to dibenzothiophene sulfone by Pseudomonas putida

1989 ◽  
Vol 35 (5) ◽  
pp. 603-605 ◽  
Author(s):  
MeLanie R. Mormile ◽  
Ronald M. Atlas
Keyword(s):  
Pseudomonas Putida ◽  
Microbial Degradation ◽  
Sulfur Metabolism ◽  
Crystalline Compound ◽  
Dibenzothiophene Sulfone

A strain of Pseudomonas putida was isolated that transforms dibenzothiophene (DBT) to DBT sulfone (DBT-5-dioxide) via DBT-5-oxide. It also degrades DBT to 3-hydroxy-2-formyl benzothiophene via an alternate and previously described pathway, and to an unidentified red crystalline compound. Neither DBT sulfone nor 3-hydroxy-2-formyl benzothiophene are further degraded by this organism.Key words: dibenzothiophene, microbial degradation, Pseudomonas, dibenzothiophene sulfone, sulfur metabolism.

scholarly journals Propane and n-Butane Oxidation by Pseudomonas putida GPo1

2006 ◽  
Vol 72 (1) ◽  
pp. 950-952 ◽  
Author(s):  
Erika L. Johnson ◽  
Michael R. Hyman
Keyword(s):  
Cell Growth ◽  
Pseudomonas Putida ◽  
Enzyme System ◽  
Butane Oxidation ◽  
Hydroxylase Activity ◽  
Alkane Hydroxylase ◽  
Butyl Ether ◽  
Support Cell

ABSTRACT Propane and n-butane inhibit methyl tertiary butyl ether oxidation by n-alkane-grown Pseudomonas putida GPo1. Here we demonstrate that these gases are oxidized by this strain and support cell growth. Both gases induced alkane hydroxylase activity and appear to be oxidized by the same enzyme system used for the oxidation of n-octane.

scholarly journals Microbial degradation of the morphine alkaloids. Purification and characterization of morphine dehydrogenase from Pseudomonas putida M10

1991 ◽  
Vol 274 (3) ◽  
pp. 875-880 ◽  
Author(s):  
N C Bruce ◽  
C J Wilmot ◽  
K N Jordan ◽  
L D G Stephens ◽  
C R Lowe
Keyword(s):  
Affinity Chromatography ◽  
Pseudomonas Putida ◽  
Hydroxy Group ◽  
Microbial Degradation ◽  
Purification Procedure ◽  
Metal Centre ◽  
Purification And Characterization ◽  
Ph Optimum ◽  
Morphine Alkaloids

The NADP(+)-dependent morphine dehydrogenase that catalyses the oxidation of morphine to morphinone was detected in glucose-grown cells of Pseudomonas putida M10. A rapid and reliable purification procedure involving two consecutive affinity chromatography steps on immobilized dyes was developed for purifying the enzyme 1216-fold to electrophoretic homogeneity from P. putida M10. Morphine dehydrogenase was found to be a monomer of Mr 32,000 and highly specific with regard to substrates, oxidizing only the C-6 hydroxy group of morphine and codeine. The pH optimum of morphine dehydrogenase was 9.5, and at pH 6.5 in the presence of NADPH the enzyme catalyses the reduction of codeinone to codeine. The Km values for morphine and codeine were 0.46 mM and 0.044 mM respectively. The enzyme was inhibited by thiol-blocking reagents and the metal-complexing reagents 1,10-phenanthroline and 2,2′-dipyridyl, suggesting that a metal centre may be necessary for activity of the enzyme.

Microbial degradation of methyl tert-butyl ether and tert-butyl alcohol in the subsurface

2004 ◽  
Vol 70 (3-4) ◽  
pp. 173-203 ◽  
Author(s):  
Torsten C. Schmidt ◽  
Mario Schirmer ◽  
Holger Weiß ◽  
Stefan B. Haderlein
Keyword(s):  
Microbial Degradation ◽  
Butyl Alcohol ◽  
Methyl Tert Butyl Ether ◽  
Butyl Ether ◽  
Tert Butyl ◽  
Tert Butyl Alcohol
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