Characterization of an <i>Arabidopsis</i> cDNA for a soluble epoxide hydrolase gene that is inducible by auxin and water stress

Kiyosue, Tomohiro; Beetham, Jeffrey K.; Pinot, Frank; Hammock, Bruce D.; Yamaguchi-Shinozaki, Kazuko; Shinozaki, Kazuo

doi:10.1046/j.1365-313x.1994.6020259.x

Cited by 69 publications

(62 citation statements)

References 27 publications

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“…[6,39] The CEEH2 sequence confirmed by RACE agreed with the WormBase predicted mRNA from gene model K06C5.5 ( Figure 2). The CEEH1 sequence corresponded to the predicted mRNA from gene model K02F3.6 (Figure 1).…”

Section: Discussionsupporting

confidence: 64%

Identification of two epoxide hydrolases in Caenorhabditis elegans that metabolize mammalian lipid signaling molecules

Harris

Aronov

Jones

et al. 2008

Archives of Biochemistry and Biophysics

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We have identified two genes in the genomic database for C. elegans that code for proteins with significant sequence similarity to the mammalian soluble epoxide hydrolase (sEH). The respective transcripts were cloned from a mixed stage cDNA library from C. elegans. The corresponding proteins obtained after recombinant expression in insect cells hydrolyzed standard epoxide hydrolase substrates, including epoxyeicosatrienoic acids (EETs) and leukotoxins (EpOMEs). The enzyme activity was inhibited by urea-based compounds originally designed to inhibit the mammalian sEH. In vivo inhibition of the enzymes using the most potent of these compounds resulted in elevated levels of the EpOMEs in the nematode. These results suggest that the hydrolases are involved in the metabolism of possible lipid signaling molecules in C. elegans.

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Section: Discussionsupporting

confidence: 64%

Identification of two epoxide hydrolases in Caenorhabditis elegans that metabolize mammalian lipid signaling molecules

Harris

Aronov

Jones

et al. 2008

Archives of Biochemistry and Biophysics

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“…An epoxide hydrolase from A. thaliana (AtsEH) has been cloned (Kiyosue et al, 1994). AtsEH is only 20% similar to ATHCOR1 and is not expressed in flowers (Kiyosue et al, 1994).…”

Section: Discussionmentioning

confidence: 99%

“…AtsEH is only 20% similar to ATHCOR1 and is not expressed in flowers (Kiyosue et al, 1994). However, an epoxide hydrolase from potato, which is highly homologous to AtsEH, is induced by MeJA and wounding (Stapleton et al, 1994).…”

Section: Discussionmentioning

confidence: 99%

Differential Expression of a Novel Gene in Response to Coronatine, Methyl Jasmonate, and Wounding in the Coi1Mutant of Arabidopsis1

et al. 1998

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Coronatine is a phytotoxin produced by some plant-pathogenic bacteria. It has been shown that coronatine mimics the action of methyl jasmonate (MeJA) in plants. MeJA is a plant-signaling molecule involved in stress responses such as wounding and pathogen attack. In Arabidopsis thaliana, MeJA is essential for pollen grain development. The coi1 (for coronatine-insensitive) mutant of Arabidopsis, which is insensitive to coronatine and MeJA, produces sterile male flowers and shows an altered response to wounding. When the differential display technique was used, a message that was rapidly induced by coronatine in wild-type plants but not in coi1 was identified and the corresponding cDNA was cloned. The coronatine-induced gene ATHCOR1 (for A. thaliana coronatineinduced) is expressed in seedlings, mature leaves, flowers, and siliques but was not detected in roots. The expression of this gene was dramatically reduced in coi1 plants, indicating that COI1 affects its expression. ATHCOR1 was rapidly induced by MeJA and wounding in wild-type plants. The sequence of ATHCOR1 shows no strong homology to known proteins. However, the predicted polypeptide contains a conserved amino acid sequence present in several bacterial, animal, and plant hydrolases and includes a potential ATP/GTP-binding-site motif (P-loop).

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“…In plants, epoxide hydrolase activities have been detected in e.g. mouse ear cress, spinach, soya bean, rape, tobacco and potato [1][2][3][4][5][6][7][8]. A suggested physiological role of the plant enzymes is through their involvement in the epoxide fatty acid metabolism and biosynthetic pathway of cutin [9].…”

Section: Introductionmentioning

confidence: 99%

Catalysis of potato epoxide hydrolase, StEH1

Elfström

Widersten

2005

Biochemical Journal

134

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The kinetic mechanism of epoxide hydrolase (EC 3.3.2.3) from potato, StEH1 (Solanum tuberosum epoxide hydrolase 1), was studied by presteady-state and steady-state kinetics as well as by pH dependence of activity. The specific activities towards the different enantiomers of TSO (trans-stilbene oxide) as substrate were 43 and 3 µmol · min −1 · mg −1 with the R,R-or S,S-isomers respectively. The enzyme was, however, enantioselective in favour of the S,S enantiomer due to a lower K m value. The pH dependences of k cat with R,R or S,S-TSO were also distinct and supposedly reflecting the pH dependences of the individual kinetic rates during substrate conversion. The rate-limiting step for TSO and cis-and trans-epoxystearate was shown by rapid kinetic measurements to be the hydrolysis of the alkylenzyme intermediate. Functional characterization of point mutants verified residues Asp 105 , Tyr 154 , Tyr 235 and His 300 as crucial for catalytic activity. All mutants displayed drastically decreased enzymatic activities during steady state. Presteady-state measurements revealed the base-deficient H300N (His 300 → Asn) mutant to possess greatly reduced efficiencies in catalysis of both chemical steps (alkylation and hydrolysis).

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Characterization of an Arabidopsis cDNA for a soluble epoxide hydrolase gene that is inducible by auxin and water stress

Cited by 69 publications

References 27 publications

Identification of two epoxide hydrolases in Caenorhabditis elegans that metabolize mammalian lipid signaling molecules

Identification of two epoxide hydrolases in Caenorhabditis elegans that metabolize mammalian lipid signaling molecules

Differential Expression of a Novel Gene in Response to Coronatine, Methyl Jasmonate, and Wounding in the Coi1Mutant of Arabidopsis1

Catalysis of potato epoxide hydrolase, StEH1

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