PMID:11368347: Difference between revisions

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<span style = 'font-size: large'> '''Tholl, D, Croteau, R and Gershenzon, J'''  (2001) Partial purification and characterization of the short-chain prenyltransferases, gernayl diphospate synthase and farnesyl diphosphate synthase, from Abies grandis (grand fir).''Arch. Biochem. Biophys.'' '''386''':233-42</span>
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'''Tholl, D, Croteau, R and Gershenzon, J'''  (2001) Partial purification and characterization of the short-chain prenyltransferases, gernayl diphospate synthase and farnesyl diphosphate synthase, from Abies grandis (grand fir). ''Arch. Biochem. Biophys.'' '''386''':233-42
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!align=left  |Abstract
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In the conifer Abies grandis (grand fir), a secreted oleoresin rich in mono-, sesqui-, and diterpenes serves as a constitutive and induced defense against insects and pathogenic fungi. Geranyl diphosphate (GPP) and farnesyl diphosphate (FPP) synthase, two enzymes which form the principal precursors of the oleoresin mono- and sesquiterpenes, were isolated from the stems of 2-year-old grand fir saplings. These enzymes were partially purified by sequential chromatography on DEAE-Sepharose, Mono-Q, and phenyl-Sepharose to remove competing phosphohydrolase and isopentenyl diphosphate (IPP) isomerase activities. GPP and FPP synthase formed GPP and E,E-FPP, respectively, as the sole products of the enzymatic condensation of IPP and dimethylallyl diphosphate (DMAPP). The properties of both enzymes are broadly similar to those of other prenyltransferases. The apparent native molecular masses are 54 +/- 3 kDa for GPP synthase and 110 +/- 6 kDa fo
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=11368347 PubMed]


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|{{TableHeadingColor}} |'''Abstract''' || In the conifer Abies grandis (grand fir), a secreted oleoresin rich in mono-, sesqui-, and diterpenes serves as a constitutive and induced defense against insects and pathogenic fungi. Geranyl diphosphate (GPP) and farnesyl diphosphate (FPP) synthase, two enzymes which form the principal precursors of the oleoresin mono- and sesquiterpenes, were isolated from the stems of 2-year-old grand fir saplings. These enzymes were partially purified by sequential chromatography on DEAE-Sepharose, Mono-Q, and phenyl-Sepharose to remove competing phosphohydrolase and isopentenyl diphosphate (IPP) isomerase activities. GPP and FPP synthase formed GPP and E,E-FPP, respectively, as the sole products of the enzymatic condensation of IPP and dimethylallyl diphosphate (DMAPP). The properties of both enzymes are broadly similar to those of other prenyltransferases. The apparent native molecular masses are 54 +/- 3 kDa for GPP synthase and 110 +/- 6 kDa fo
!align=left  |Keywords
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Alkyl and Aryl Transferases/antagonists & inhibitors; Alkyl and Aryl Transferases/chemistry; Alkyl and Aryl Transferases/isolation & purification; Alkyl and Aryl Transferases/metabolism; Catalysis/drug effects; Cations, Divalent/pharmacology; Chromatography, Gas; Chromatography, Ion Exchange; Coenzymes/pharmacology; Enzyme Induction; Farnesyltranstransferase; Gymnosperms/enzymology; Intramolecular Lyases/metabolism; Kinetics; Magnesium/pharmacology; Manganese/pharmacology; Molecular Weight; Plant Diseases; Plant Stems/enzymology; Polyisoprenyl Phosphates/pharmacology; Sesquiterpenes
|{{TableHeadingColor}} nowrap |'''Links''' ||  [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=11368347 PubMed]
 
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Latest revision as of 04:15, 15 September 2013

Citation

Tholl, D, Croteau, R and Gershenzon, J (2001) Partial purification and characterization of the short-chain prenyltransferases, gernayl diphospate synthase and farnesyl diphosphate synthase, from Abies grandis (grand fir). Arch. Biochem. Biophys. 386:233-42

Abstract

In the conifer Abies grandis (grand fir), a secreted oleoresin rich in mono-, sesqui-, and diterpenes serves as a constitutive and induced defense against insects and pathogenic fungi. Geranyl diphosphate (GPP) and farnesyl diphosphate (FPP) synthase, two enzymes which form the principal precursors of the oleoresin mono- and sesquiterpenes, were isolated from the stems of 2-year-old grand fir saplings. These enzymes were partially purified by sequential chromatography on DEAE-Sepharose, Mono-Q, and phenyl-Sepharose to remove competing phosphohydrolase and isopentenyl diphosphate (IPP) isomerase activities. GPP and FPP synthase formed GPP and E,E-FPP, respectively, as the sole products of the enzymatic condensation of IPP and dimethylallyl diphosphate (DMAPP). The properties of both enzymes are broadly similar to those of other prenyltransferases. The apparent native molecular masses are 54 +/- 3 kDa for GPP synthase and 110 +/- 6 kDa fo

Links

PubMed

Keywords

Alkyl and Aryl Transferases/antagonists & inhibitors; Alkyl and Aryl Transferases/chemistry; Alkyl and Aryl Transferases/isolation & purification; Alkyl and Aryl Transferases/metabolism; Catalysis/drug effects; Cations, Divalent/pharmacology; Chromatography, Gas; Chromatography, Ion Exchange; Coenzymes/pharmacology; Enzyme Induction; Farnesyltranstransferase; Gymnosperms/enzymology; Intramolecular Lyases/metabolism; Kinetics; Magnesium/pharmacology; Manganese/pharmacology; Molecular Weight; Plant Diseases; Plant Stems/enzymology; Polyisoprenyl Phosphates/pharmacology; Sesquiterpenes

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