The <i>Rhodococcus erythropolis</i> DCL14 limonene‐1,2‐epoxide hydrolase gene encodes an enzyme belonging to a novel class of epoxide hydrolases

Barbirato, Fabien; Verdoes, J.C.; Bont, J.A.M. de; Werf, M.J. van der

doi:10.1016/s0014-5793(98)01322-2

Cited by 48 publications

(29 citation statements)

References 32 publications

(59 reference statements)

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“…These results led to the speculation that ChEH might hydrolyse its substrate via a diVerent mechanism and represents the Wrst mammalian EH member similar to the recently described bacterial LEH (EC. 3.3.2.8) from Rhodococcus erythropolis (Barbirato et al 1998). The LEH hydrolyses its substrate in a single step mechanism and further shares structural similarity to an epoxide hydrolase from Mycobacterium tuberculosum (TbEH1).…”

Section: Other Mammalian Epoxide Hydrolasesmentioning

confidence: 99%

Mammalian epoxide hydrolases in xenobiotic metabolism and signalling

2009

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Epoxide hydrolases catalyse the hydrolysis of electrophilic-and therefore potentially genotoxic-epoxides to the corresponding less reactive vicinal diols, which explains the classiWcation of epoxide hydrolases as typical detoxifying enzymes. The best example is mammalian microsomal epoxide hydrolase (mEH)-an enzyme prone to detoxiWcation-due to a high expression level in the liver, a broad substrate selectivity, as well as inducibility by foreign compounds. The mEH is capable of inactivating a large number of structurally diVerent, highly reactive epoxides and hence is an important part of the enzymatic defence of our organism against adverse eVects of foreign compounds. Furthermore, evidence is accumulating that mammalian epoxide hydrolases play physiological roles other than detoxiWcation, particularly through involvement in signalling processes. This certainly holds true for soluble epoxide hydrolase (sEH) whose main function seems to be the turnover of lipid derived epoxides, which are signalling lipids with diverse functions in regulatory processes, such as control of blood pressure, inXammatory processes, cell proliferation and nociception. In recent years, the sEH has attracted attention as a promising target for pharmacological inhibition to treat hypertension and possibly other diseases. Recently, new hitherto uncharacterised epoxide hydrolases could be identiWed in mammals by genome analysis. The expression pattern and substrate selectivity of these new epoxide hydrolases suggests their participation in signalling processes rather than a role in detoxiWcation. Taken together, epoxide hydrolases (1) play a central role in the detoxiWcation of genotoxic epoxides and (2) have an important function in the regulation of physiological processes by the control of signalling molecules with an epoxide structure.

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Section: Other Mammalian Epoxide Hydrolasesmentioning

confidence: 99%

Mammalian epoxide hydrolases in xenobiotic metabolism and signalling

2009

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“…The limA gene coding for limonene-1,2-epoxide hydrolase, an enzyme involved in limonene degradation in R. erythropolis DCL14, was cloned using a combination of polymerase chain reaction and colony filter hybridization (21). Using the N-terminal amino acid sequence of the purified enzyme (15), two degenerated primers were designed at the beginning and the end of the 50-amino acid-long stretch.…”

Section: Cloning and Sequencing Of The Cdh Gene (Limc)mentioning

confidence: 99%

Stereoselective Carveol Dehydrogenase from Rhodococcus erythropolis DCL14

Werf

Ven

Barbirato

et al. 1999

Journal of Biological Chemistry

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A novel nicotinoprotein, catalyzing the dichlorophenolindophenol-dependent oxidation of carveol to carvone, was purified to homogeneity from Rhodococcus erythropolis DCL14. The enzyme is specifically induced after growth on limonene and carveol. Dichlorophenolindophenol-dependent carveol dehydrogenase (CDH) is a homotetramer of 120 kDa with each subunit containing a tightly bound NAD(H) molecule. The enzyme is optimally active at pH 5.5 and 50°C and displays a broad substrate specificity with a preference for substituted cyclohexanols. When incubated with a diastereomeric mixture of (4R)

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“…Whether other CYP450s are responsible for the oxygenation of limonene in the degradation pathway needs to be further explored. In contrast to R. erythropolis, which possesses a unique epoxide hydrolase that is not a classic ␣-␤ hydrolase (43), Gs has such a classical enzyme (CMQ_7009), and this was significantly upregulated when (ϩ)-limonene was the only substrate. While knocking out this gene in Gs did not totally abolish (ϩ)-limonene utilization, as the mutant was still able to grow, mycelium density was lighter than in the wild type.…”

Section: Discussionmentioning

confidence: 86%

Gene Discovery for Enzymes Involved in Limonene Modification or Utilization by the Mountain Pine Beetle-Associated Pathogen Grosmannia clavigera

Wang

Lim

Madilao

et al. 2014

Appl Environ Microbiol

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bTo successfully colonize and eventually kill pine trees, Grosmannia clavigera (Gs cryptic species), the main fungal pathogen associated with the mountain pine beetle (Dendroctonus ponderosae), has developed multiple mechanisms to overcome host tree chemical defenses, of which terpenoids are a major component. In addition to a monoterpene efflux system mediated by a recently discovered ABC transporter, Gs has genes that are highly induced by monoterpenes and that encode enzymes that modify or utilize monoterpenes [especially (؉)-limonene]. We showed that pine-inhabiting Ophiostomale fungi are tolerant to monoterpenes, but only a few, including Gs, are known to utilize monoterpenes as a carbon source. Gas chromatography-mass spectrometry (GC-MS) revealed that Gs can modify (؉)-limonene through various oxygenation pathways, producing carvone, p-mentha-2,8-dienol, perillyl alcohol, and isopiperitenol. It can also degrade (؉)-limonene through the C-1-oxygenated pathway, producing limonene-1,2-diol as the most abundant intermediate. Transcriptome sequencing (RNA-seq) data indicated that Gs may utilize limonene 1,2-diol through beta-oxidation and then valine and tricarboxylic acid (TCA) metabolic pathways. The data also suggested that at least two gene clusters, located in genome contigs 108 and 161, were highly induced by monoterpenes and may be involved in monoterpene degradation processes. Further, gene knockouts indicated that limonene degradation required two distinct Baeyer-Villiger monooxygenases (BVMOs), an epoxide hydrolase and an enoyl coenzyme A (enoyl-CoA) hydratase. Our work provides information on enzyme-mediated limonene utilization or modification and a more comprehensive understanding of the interaction between an economically important fungal pathogen and its host's defense chemicals.

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The Rhodococcus erythropolis DCL14 limonene‐1,2‐epoxide hydrolase gene encodes an enzyme belonging to a novel class of epoxide hydrolases

Cited by 48 publications

References 32 publications

Mammalian epoxide hydrolases in xenobiotic metabolism and signalling

Mammalian epoxide hydrolases in xenobiotic metabolism and signalling

Stereoselective Carveol Dehydrogenase from Rhodococcus erythropolis DCL14

Gene Discovery for Enzymes Involved in Limonene Modification or Utilization by the Mountain Pine Beetle-Associated Pathogen Grosmannia clavigera

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