Identification of Genes and Proteins Necessary for Catabolism of Acyclic Terpenes and Leucine/Isovalerate in
            <i>Pseudomonas aeruginosa</i>

Förster-Fromme, Karin; Höschle, Birgit; Mack, Christina; Bott, Michael; Armbruster, Wolfgang; Jendrossek, Dieter

doi:10.1128/aem.00853-06

Cited by 68 publications

(97 citation statements)

References 32 publications

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“…Although both are acyclic monoterpenes, the degradation of citronellol and myrcene is achieved by different catabolic pathways with specific genes and enzymes (Iurescia et al 1999;Aguilar et al 2006;Föster-Fromme et al 2006). Conversely, the citronellol and geraniol degradation pathways share most of the enzymes, and the ability of IBPse 105 to use just one of these monoterpenes, confirms the existence of different metabolic routes (upper pathway) for their oxidation .…”

Section: Resultsmentioning

confidence: 96%

“…The spectrum of degradation of monoterpenes of P. mendocina IBPse 105 is restricted when compared with that of P. mendocina ATCC 25411 (Cantwell et al 1978), and other species of the genus (Cantwell et al 1978;Díaz-Pérez et al 2004;Föster-Fromme et al 2006).…”

Section: Resultsmentioning

confidence: 99%

“…In the lower pathway, a carboxilation, a hydration and the removal of acetil-CoA leads to the production of 3-oxo-7-methyloctanoyl-CoA, which is transformed in 3-methylcrotonoyl-CoA by two rounds of oxidation. This metabolite is then metabolized by the leucine catabolic pathway producing acetil-CoA and acetoacetate (Díaz-Pérez et al 2004;Aguilar et al 2006;Föster-Fromme et al 2006).…”

mentioning

confidence: 99%

“…Two gene clusters are involved in the catabolic pathways for acyclic monoterpenes in P. aeruginosa: the atu cluster (atuABCDEFG) responsible for the lower pathway, and the liu cluster (liuRABCDE) involved in both acyclic monoterpenes and leucine catabolism (Stover et al 2000;Díaz-Pérez et al 2004;Aguilar et al 2006;Föster-Fromme et al 2006). …”

mentioning

confidence: 99%

“…principal hydrocarbon chain that makes the degradation of these compounds particularly recalcitrant (Föster-Fromme et al 2006). However, several bacteria, particularly Pseudomonas (P. aeruginosa, P. citronellolis, and P. mendocina), can use these compounds as sole carbon source (Cantwell et al 1978;Campos-García and Soberón-Chávez, 2000;Díaz-Pérez et al 2004).…”

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confidence: 99%

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Degradation of citronellol, citronellal and citronellyl acetate by Pseudomonas mendocina IBPse 105

Tozoni¹,

Zacaria²,

Vanderlinde³

et al. 2010

Electron. J. Biotechnol.

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Financial support: COREDES/FAPERGS, and D. Tozoni held a CAPES scholarship during the development of this work.Keywords: biodegradation, citronellol catabolism, monoterpenes degradation, P. mendocina. Abbreviations: GC-MS: gas chromatography-mass spectrometryThe purpose of this work was to stud the Terpenes or terpenoids are widespread in nature, and are biodegradation of citronellol, citronellal and citronellyl the most important component of the essential oil of many acetate by a soil Pseudomonas mendocina strain (IBPse higher plants (Loza-Tavera, 1999). These compounds are 105) isolated from a Cymbopogon windelandi field. This characterized by methyl-branched molecular structures strain efficiently used citronellol, citronellal, citronellyl derived from isoprene. Monoterpenes and their oxygenated acetate and myrcene as sole source of carbon, but was forms consist of two isoprene units (C10), and can be cyclic not able to grow on other 15 monoterpenoids evaluated.(1,8-cineole, camphor, etc.) or acyclic (citronellol, geraniol, Gas chromatography-mass spectrometry (GC-MS) citral, etc.). analysis of metabolites accumulation during P. medocina IBPse 105 growth on citronellol showed that Citronellol, citronellal and citronellyl acetate are among the this strain uses the citronellol catabolic pathway main constituent of the essential oils of several plants, like described for other species of the genus. IBPse 105 citrus, citronella grass, roses, lemongrass, basil, lemon degradation of citronellyl acetate initiates by its eucalyptus, among others, being responsible for the hydrolysis to citronellol. The mini-Tn5 insertion in aromatic and biological properties, including antibacterial mutant IBPse 105-303, impaired in citronellol activity, of these oils (Hammer et al. 1999; Dorman and degradation, but able to grow on citronellal, was located Deans. 2000;Bakkali et al. 2008). in a homologous of the P. aeruginosa atuB gene, that Acyclic terpenoids contain a 3-methyl substitution in the codifies citronellol deshydrogenase.

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Section: Resultsmentioning

confidence: 96%

Section: Resultsmentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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Degradation of citronellol, citronellal and citronellyl acetate by Pseudomonas mendocina IBPse 105

Tozoni¹,

Zacaria²,

Vanderlinde³

et al. 2010

Electron. J. Biotechnol.

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Enzymatic Synthesis of Tertiary Alcohols

Müller

2014

ChemBioEng Reviews

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Tertiary alcohols are found as a motif in many pharmaceuticals and natural products. Elucidation of their biosynthesis is thus a good starting point for the identification of enzymes for the synthesis of chiral tertiary alcohols. To date, however, relatively few enzymatic methods for such syntheses have been established in biotechnological processes. Whereas secondary alcohols can be efficiently synthesized via the (asymmetric) reduction of ketones, a generally applicable method for the enzymatic synthesis of tertiary alcohols has been more difficult to identify. Herein, a survey of the biocatalytic methods for the synthesis of (chiral) tertiary alcohols is presented. Advantages and disadvantages of the respective methods are discussed from a synthetic point of view.

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Identification of Additional Players in the Alternative Biosynthesis Pathway to Isovaleryl‐CoA in the Myxobacterium Myxococcus xanthus

et al. 2008

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Isovaleryl-CoA (IV-CoA) is usually derived from the degradation of leucine by using the Bkd (branched-chain keto acid dehydrogenase) complex. We have previously identified an alternative pathway for IV-CoA formation in myxobacteria that branches from the well-known mevalonate-dependent isoprenoid biosynthesis pathway. We identified 3-hydroxy-3-methylglutaryl-CoA (HMG-CoA) synthase (MvaS) to be involved in this pathway in Myxococcus xanthus, which is induced in mutants with impaired leucine degradation (e.g., bkd(-)) or during myxobacterial fruiting-body formation. Here, we show that the proteins required for leucine degradation are also involved in the alternative IV-CoA biosynthesis pathway through the efficient catalysis of the reverse reactions. Moreover, we conducted a global gene-expression experiment and compared vegetative wild-type cells with bkd mutants, and identified a five-gene operon that is highly up-regulated in bkd mutants and contains mvaS and other genes that are directly involved in the alternative pathway. Based on our experiments, we assigned roles to the genes required for the formation of IV-CoA from HMG-CoA. Additionally, several genes involved in outer-membrane biosynthesis and a plethora of genes encoding regulatory proteins were decreased in expression levels in the bkd(-) mutant; this explains the complex phenotype of bkd mutants including a lack of adhesion in developmental submerse culture.

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Identification of Genes and Proteins Necessary for Catabolism of Acyclic Terpenes and Leucine/Isovalerate in Pseudomonas aeruginosa

Cited by 68 publications

References 32 publications

Degradation of citronellol, citronellal and citronellyl acetate by Pseudomonas mendocina IBPse 105

Degradation of citronellol, citronellal and citronellyl acetate by Pseudomonas mendocina IBPse 105

Enzymatic Synthesis of Tertiary Alcohols

Identification of Additional Players in the Alternative Biosynthesis Pathway to Isovaleryl‐CoA in the Myxobacterium Myxococcus xanthus

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