Metabolism of Alkanes by <i>Rhodococcus erythropolis</i>

Lofgren, John A.; Haddad, Sandra; Kendall, Kevin

doi:10.1021/bk-1995-0607.ch020

Cited by 6 publications

(6 citation statements)

References 8 publications

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“…This presumption is supported by the results of Nieder and Shapiro (1975) who described the appearance of mutants growing selectively with n‐alkanes of defined chain lengths. Similarly, Lofgren et al. (1995) found mutants of R. erythropolis which were not able to grow with n‐alkanes of specific chain lengths anymore.…”

Section: Discussionmentioning

confidence: 88%

Distribution of alkB genes within n-alkane-degrading bacteria

Vomberg

Klinner

2000

J Appl Microbiol

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Fifty‐four bacterial strains belonging to 37 species were tested for their ability to assimilate short chain and/or medium chain liquid n‐alkanes. A gene probe derived from the alkB gene of Pseudomonas oleovorans ATCC 29347 was utilized in hybridization experiments. Results of Southern hybridization of PCR‐amplificates were compared with those of colony hybridization and dot blot hybridization. Strongest signals were received only from Gram‐negative bacteria growing solely with short n‐alkanes (C10). Hybridization results with soil isolates growing with n‐alkanes of different chain lengths suggested as well that alkB genes seem to be widespread only in solely short‐chain n‐alkane‐degrading pseudomonads. PCR products of Rhodococcus sp., Nocardioides sp., Gordona sp. and Sphingomonas sp. growing additionally or solely with medium‐chain n‐alkane as hexadecane had only few sequence identity with alkB though hybridizing with the gene probe. The derived amino acid sequence of the alkB‐amplificate of Pseudomonas aureofaciens showed high homology (95%) with AlkB from Ps. oleovorans. alkB gene disruptants were not able to grow with decane.

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Section: Discussionmentioning

confidence: 88%

Distribution of alkB genes within n-alkane-degrading bacteria

Vomberg

Klinner

2000

J Appl Microbiol

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“…On the basis of previous knowledge of the Rhodococcus metabolism − and proteome analysis of strain R138, we investigated the metabolism of GCL by R. erythropolis . Our results suggest that GCL is both completely dissimilated (CO 2 production during Krebs cycle) and assimilated (glyoxylate cycle, lipids biosynthesis) during bacterial growth without the production of toxic compounds.…”

Section: Discussionmentioning

confidence: 99%

“…To this end, at least three hypotheses can be proposed. (i) R. erythropolis is a bacterium known for its ability to degrade a wide range of recalcitrant molecules including molecules derived from lignin, pesticides or petroleum. ,, The degradation steps of these compounds are often associated to an intermediate lactonase activity (i.e., enol-lactone-hydrolyzing activities) responsible for linearization of the molecule before joining β-ketoadipate or β-oxidation pathways. ,− QsdA activity could also have this role. Indeed, analyzing neighboring sequences downstream QsdA reveals the presence of a contiguous sequence encoding for the long-chain fatty acid-CoA ligase FadD (data not shown).…”

Section: Discussionmentioning

confidence: 99%

Catabolic Pathway of Gamma-caprolactone in the Biocontrol Agent Rhodococcus erythropolis

et al. 2011

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Gamma-caprolactone (GCL) is well-known as a food flavor and has been recently described as a biostimulant molecule promoting the growth of bacteria with biocontrol activity against soft-rot pathogens. Among these biocontrol agents, Rhodococcus erythropolis, characterized by a remarkable metabolic versatility, assimilates various γ-butyrolactone molecules with a branched-aliphatic chain, such as GCL. The assimilative pathway of GCL in R. erythropolis was investigated by two-dimensional gel electrophoresis coupled to matrix-assisted laser desorption ionization (MALDI) mass spectrometry (MS) analysis. This analysis suggests the involvement of the lactonase QsdA in ring-opening, a feature confirmed by heterologous expression in Escherichia coli. According to proteome analysis, the open-chain form of GCL was degraded by β- and ω-oxidation coupled to the Krebs cycle and β-ketoadipate pathway. Ubiquity of qsdA gene among environmental R. erythropolis isolates was verified by PCR. In addition to a previous N-acyl homoserine lactone catabolic function, QsdA may therefore be involved in an intermediate degradative step of cyclic recalcitrant molecules or in synthesis of flavoring lactones.

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“…There are strains able to grow on n-decane to n-triacontane (Milekhina et al, 1998), on n-dodecane to n-dotriacontane (Whyte et al, 1998) or on n-hexane to n-eicosane and on pristane (Bej et al, 2000). The rhodococci, however, also include strains metabolizing only a rather narrow spectrum of n-alkanes ranging from n-undecane to n-heptadecane (Lofgren et al, 1995) or from n-dodecane to n-eicosane (Sorkoh et al, 1990). Like some other Rhodococcus species (Bej et al, 2000;Whyte et al, 1998), strain MS11 was psychrotolerant, since it could grow at 5 u C, while its optimum temperature was 20 u C.…”

Section: Discussionmentioning

confidence: 99%

Degradation of alkanes and highly chlorinated benzenes, and production of biosurfactants, by a psychrophilic Rhodococcus sp. and genetic characterization of its chlorobenzene dioxygenase

Rapp

Gabriel-Jürgens

2003

Microbiology

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Rhodococcus sp. strain MS11 was isolated from a mixed culture. It displays a diverse range of metabolic capabilities. During growth on 1,2,4-trichlorobenzene, 1,2,4,5-tetrachlorobenzene (1,2,4,5-TeCB) and 3-chlorobenzoate stoichiometric amounts of chloride were released. It also utilized all three isomeric dichlorobenzenes and 1,2,3-trichlorobenzene as the sole carbon and energy source. Furthermore, the bacterium grew well on a great number of n-alkanes ranging from n-heptane to n-triacontane and on the branched alkane 2,6,10,14-tetramethylpentadecane (pristane) and slowly on n-hexane and n-pentatriacontane. It was able to grow at temperatures from 5 to 30 degrees C, with optimal growth at 20 degrees C, and could tolerate 6 % NaCl in mineral salts medium. Genes encoding the initial chlorobenzene dioxygenase were detected by using a primer pair that was designed against the alpha-subunit (TecA1) of the chlorobenzene dioxygenase of Ralstonia (formerly Burkholderia) sp. strain PS12. The amino acid sequence of the amplified part of the alpha-subunit of the chlorobenzene dioxygenase of Rhodococcus sp. strain MS11 showed >99 % identity to the alpha-subunit of the chlorobenzene dioxygenase from Ralstonia sp. strain PS12 and the parts of both alpha-subunits responsible for substrate specificity were identical. The subsequent enzymes dihydrodiol dehydrogenase and chlorocatechol 1,2-dioxygenase were induced in cells grown on 1,2,4,5-TeCB. During cultivation on medium-chain-length n-alkanes ranging from n-decane to n-heptadecane, including 1-hexadecene, and on the branched alkane pristane, strain MS11 produced biosurfactants lowering the surface tension of the cultures from 72 to

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Metabolism of Alkanes by Rhodococcus erythropolis

Cited by 6 publications

References 8 publications

Distribution of alkB genes within n-alkane-degrading bacteria

Distribution of alkB genes within n-alkane-degrading bacteria

Catabolic Pathway of Gamma-caprolactone in the Biocontrol Agent Rhodococcus erythropolis

Degradation of alkanes and highly chlorinated benzenes, and production of biosurfactants, by a psychrophilic Rhodococcus sp. and genetic characterization of its chlorobenzene dioxygenase

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