Cloning and expression of soluble epoxide hydrolase from potato

Andrew Stapleton, Jeffrey K. Beetham, Franck Pinot, Joan E. Garbarino, David R. Rockhold, Mendel Friedman, Bruce D. Hammock, William R. Belknap

Research output: Contribution to journalArticle

86 Citations (Scopus)

Abstract

Five cDNAs encoding a putative soluble epoxide hydrolase (sEH) from potato were isolated and characterized. The cDNAs contained open reading frames encoding 36 kDa polypeptides which were highly homologous to the carboxy terminal region of mammalian sEH. When one of the cDNAs was expressed in a baculovirus system a soluble 38 kDa protein with epoxide hydrolase activity was produced. The recombinant enzyme hydrolyzed a commonly used diagnostic substrate for the soluble form of mammalian EH. Inhibitor profiles of the recombinant potato and mammalian sEH were also similar. The expression of sEH in potato was found to be regulated by both developmental and environmental signals. Levels of mRNA for sEH were higher in meristematic tissue than in mature leaves. This mRNA was also observed to accumulate on wounding and application of exogenous methyl jasmonate.

Original languageEnglish (US)
Pages (from-to)251-258
Number of pages8
JournalPlant Journal
Volume6
Issue number2
StatePublished - 1994

Fingerprint

epoxide hydrolase
Epoxide Hydrolases
Solanum tuberosum
Organism Cloning
molecular cloning
potatoes
Complementary DNA
Messenger RNA
Baculoviridae
methyl jasmonate
Open Reading Frames
open reading frames
polypeptides
Peptides
Enzymes
enzymes

ASJC Scopus subject areas

  • Plant Science

Cite this

Stapleton, A., Beetham, J. K., Pinot, F., Garbarino, J. E., Rockhold, D. R., Friedman, M., ... Belknap, W. R. (1994). Cloning and expression of soluble epoxide hydrolase from potato. Plant Journal, 6(2), 251-258.

Cloning and expression of soluble epoxide hydrolase from potato. / Stapleton, Andrew; Beetham, Jeffrey K.; Pinot, Franck; Garbarino, Joan E.; Rockhold, David R.; Friedman, Mendel; Hammock, Bruce D.; Belknap, William R.

In: Plant Journal, Vol. 6, No. 2, 1994, p. 251-258.

Research output: Contribution to journalArticle

Stapleton, A, Beetham, JK, Pinot, F, Garbarino, JE, Rockhold, DR, Friedman, M, Hammock, BD & Belknap, WR 1994, 'Cloning and expression of soluble epoxide hydrolase from potato', Plant Journal, vol. 6, no. 2, pp. 251-258.
Stapleton A, Beetham JK, Pinot F, Garbarino JE, Rockhold DR, Friedman M et al. Cloning and expression of soluble epoxide hydrolase from potato. Plant Journal. 1994;6(2):251-258.
Stapleton, Andrew ; Beetham, Jeffrey K. ; Pinot, Franck ; Garbarino, Joan E. ; Rockhold, David R. ; Friedman, Mendel ; Hammock, Bruce D. ; Belknap, William R. / Cloning and expression of soluble epoxide hydrolase from potato. In: Plant Journal. 1994 ; Vol. 6, No. 2. pp. 251-258.
@article{5f46695954a0488a8f1142f4be35a2e6,
title = "Cloning and expression of soluble epoxide hydrolase from potato",
abstract = "Five cDNAs encoding a putative soluble epoxide hydrolase (sEH) from potato were isolated and characterized. The cDNAs contained open reading frames encoding 36 kDa polypeptides which were highly homologous to the carboxy terminal region of mammalian sEH. When one of the cDNAs was expressed in a baculovirus system a soluble 38 kDa protein with epoxide hydrolase activity was produced. The recombinant enzyme hydrolyzed a commonly used diagnostic substrate for the soluble form of mammalian EH. Inhibitor profiles of the recombinant potato and mammalian sEH were also similar. The expression of sEH in potato was found to be regulated by both developmental and environmental signals. Levels of mRNA for sEH were higher in meristematic tissue than in mature leaves. This mRNA was also observed to accumulate on wounding and application of exogenous methyl jasmonate.",
author = "Andrew Stapleton and Beetham, {Jeffrey K.} and Franck Pinot and Garbarino, {Joan E.} and Rockhold, {David R.} and Mendel Friedman and Hammock, {Bruce D.} and Belknap, {William R.}",
year = "1994",
language = "English (US)",
volume = "6",
pages = "251--258",
journal = "Plant Journal",
issn = "0960-7412",
publisher = "Wiley-Blackwell",
number = "2",

}

TY - JOUR

T1 - Cloning and expression of soluble epoxide hydrolase from potato

AU - Stapleton, Andrew

AU - Beetham, Jeffrey K.

AU - Pinot, Franck

AU - Garbarino, Joan E.

AU - Rockhold, David R.

AU - Friedman, Mendel

AU - Hammock, Bruce D.

AU - Belknap, William R.

PY - 1994

Y1 - 1994

N2 - Five cDNAs encoding a putative soluble epoxide hydrolase (sEH) from potato were isolated and characterized. The cDNAs contained open reading frames encoding 36 kDa polypeptides which were highly homologous to the carboxy terminal region of mammalian sEH. When one of the cDNAs was expressed in a baculovirus system a soluble 38 kDa protein with epoxide hydrolase activity was produced. The recombinant enzyme hydrolyzed a commonly used diagnostic substrate for the soluble form of mammalian EH. Inhibitor profiles of the recombinant potato and mammalian sEH were also similar. The expression of sEH in potato was found to be regulated by both developmental and environmental signals. Levels of mRNA for sEH were higher in meristematic tissue than in mature leaves. This mRNA was also observed to accumulate on wounding and application of exogenous methyl jasmonate.

AB - Five cDNAs encoding a putative soluble epoxide hydrolase (sEH) from potato were isolated and characterized. The cDNAs contained open reading frames encoding 36 kDa polypeptides which were highly homologous to the carboxy terminal region of mammalian sEH. When one of the cDNAs was expressed in a baculovirus system a soluble 38 kDa protein with epoxide hydrolase activity was produced. The recombinant enzyme hydrolyzed a commonly used diagnostic substrate for the soluble form of mammalian EH. Inhibitor profiles of the recombinant potato and mammalian sEH were also similar. The expression of sEH in potato was found to be regulated by both developmental and environmental signals. Levels of mRNA for sEH were higher in meristematic tissue than in mature leaves. This mRNA was also observed to accumulate on wounding and application of exogenous methyl jasmonate.

UR - http://www.scopus.com/inward/record.url?scp=0028486021&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0028486021&partnerID=8YFLogxK

M3 - Article

VL - 6

SP - 251

EP - 258

JO - Plant Journal

JF - Plant Journal

SN - 0960-7412

IS - 2

ER -